NOVEL MULTI-SPECIFIC MOLECULES

§102 §103 §112 §DOUBLEPATENT

DETAILED ACTION Notice of Pre-AIA or AIA Status The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA . Election/Restrictions 1. The Election filed August 17, 2026 in response to the Office Action of June 16, 2026 is acknowledged and has been entered. Applicant's election with traverse of Group I claims 1, 18, 19, 21-23, 25, 26, 28-30,33-35,37, 39, 40, 42, 44-47, 49, and 52-56 is acknowledged. Applicant also elected the following species: PNG media_image1.png 718 553 media_image1.png Greyscale PNG media_image2.png 322 560 media_image2.png Greyscale Applicant argues that furthermore, the multi-specific molecule of Group I are defined in methods of Group II. Therefore, they should be considered to have unity given the claims are drawn to (2) A product and process of use of said product as defined in 37 CFR 1.475(b). Applicant argues that specifically, the examiner pointed out that Groups I and II lack unity of invention because even though the inventions of these groups require the technical feature of a multi-specific molecule, because the technical feature is not a special technical feature as it does not make a contribution over the prior art in view of WO2018/223182 Al (Dougall et al. Dec. 13, 2018, IDS), "Dougall" and Ring et al. (Proc. Natl. Acad. Sci. U.S.A. 114 (49) E10578-E10585, https://doi.org/10.1073/pnas.1710877114 (No. 20, 2017), "Ring". Applicant argues that specifically, neither of "Dougall" nor "Ring" disclosed the technical feature "(c) a target antigen binding domain that binds to a target antigen expressed on a target cell co-expressing the target antigen and CD47". Thus, the technical feature of a multi-specific molecule is a special technical feature over "Dougall" nor "Ring". Applicant’s arguments have been considered, but have not been found persuasive. The target antigen binding domains of Dougall that bind to a target antigen, which comprises antigen-binding domains that bind specifically to immune checkpoint molecule (ICM) expressed on immune cells, bind molecules distinct from CD47 and thus would be able to bind to a target cell co-expressing the target antigen and CD47. Additionally, Dougall teaches that target antigen includes PD-L1 (see ¶ [0028]), which is co-expressed with CD47 as claimed. For these reasons the restriction requirement is deemed to be proper and is therefore made FINAL. 2. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35,37, 39, 40, 42, 44-47, 49, 52-56, 58 and 67 are pending. 3. Claims 39, 40, 42, 58 and 67 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention or species, there being no allowable generic or linking claim. 4. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35,37, 44-47, 49, and 52-56 are currently under consideration as drawn to the elected species. Priority 5. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Nucleotide and/or Amino Acid Sequence Disclosures Summary of Requirements for Patent Applications Filed On Or After July 1, 2022, That Have Sequence Disclosures 6. 37 CFR 1.831(a) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.831(b) must contain a “Sequence Listing XML”, as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.831-1.835. This “Sequence Listing XML” part of the disclosure may be submitted: 1. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter “Legal Framework”) in XML format, together with an incorporation by reference statement of the material in the XML file in a separate paragraph of the specification (an incorporation by reference paragraph) as required by 37 CFR 1.835(a)(2) or 1.835(b)(2) identifying: a. the name of the XML file b. the date of creation; and c. the size of the XML file in bytes; or 2. In accordance with 37 CFR 1.831(a) using the symbols and format requirements of 37 CFR 1.832 through 1.834 on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation by reference statement of the material in the XML format according to 37 CFR 1.52(e)(8) and 37 CFR 1.835(a)(2) or 1.835(b)(2) in a separate paragraph of the specification identifying: a. the name of the XML file; b. the date of creation; and c. the size of the XML file in bytes. SPECIFIC DEFICIENCIES AND THE REQUIRED RESPONSE TO THIS NOTICE ARE AS FOLLOWS: Specific deficiency - Sequences appearing in the drawings (FIG. 23) are not identified by sequence identifiers in accordance with 37 CFR 1.831(c). Sequence identifiers for sequences (i.e., “SEQ ID NO:X” or the like) must appear either in the drawings or in the Brief Description of the Drawings. Required response – Applicant must provide: Amended drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers; AND/OR A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers (i.e., “SEQ ID NO:X” or the like) into the Brief Description of the Drawings, consisting of: • A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version); • A copy of the amended specification without markings (clean version); and • A statement that the substitute specification contains no new matter. Information Disclosure Statement 7. The information disclosure statement filed July 02, 2026 fails to comply with 37 CFR 1.98(a)(3)(i) because it does not include a concise explanation of the relevance, as it is presently understood by the individual designated in 37 CFR 1.56(c) most knowledgeable about the content of the information, of each reference listed that is not in the English language. It has been placed in the application file, but the lined-out information referred to therein has not been considered. Specification 8. The use of the term nanobody, which is a trade name or a mark used in commerce (see NANOBODY (Ser. No. 85573029, Reg. Date Dec. 13, 2016)), has been noted in this application. The term should be accompanied by the generic terminology; furthermore, the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term. Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. 9. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35,37, 44-47, 49, and 52-56 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 1 is drawn to “wherein the multi-specific molecule selectively induces effector function of an immune effector cell co-expresses SIRP-alpha and the activating receptor in the presence of the target antigen”. It is unclear what co-expresses SIRP-alpha and the activating receptor in the presence of the target antigen, the multi-specific molecule, immune effector cell, or something else. Thus, claim 1 and its dependent claims are indefinite. Amendment of claim 1 to, e.g., “wherein the multi-specific molecule selectively induces effector function of an immune effector cell which co-expresses SIRP-alpha and the activating receptor in the presence of the target antigen” would help to obviate this rejection. Claim 47 recites the limitation "the claudin 18.2 binding domain" in part b). There is insufficient antecedent basis for this limitation in the claim. Claim 47 recites the limitation "the PD-L1 binding domain" in part c). There is insufficient antecedent basis for this limitation in the claim. Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(d): (d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph: Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. 10. Claim 47 rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 47 is drawn to the multi-specific molecule of claim 33,wherein a) the SIRP-alpha binding domain further comprises one or more amino acid residue substitutions or modifications yet retains specific binding to human SIRPa . . . optionally wherein at least one of the substitutions or modifications is in one or more of the CDR sequences, and/or in one or more of the non-CDR sequences of the heavy chain variable region or light chain variable region. Claim 33 is drawn to the SIRP-alpha binding antibody domain with specific HCDR and LCDR domains some of which contain specific potential substitutions. Thus, claim 47, which encompasses unlimited amino acid residue substitutions or modifications in any part of the SIRP-alpha binding domain fails to include all of the limitations of the claim upon which it depends. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. Claim Rejections - 35 USC § 112 The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. 11. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35, 37, 44-47, 49, and 52-56 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 759 F.3d 1285, 111 USPQ2d 1780 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species.” Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010). On 22 February 2018, the USPTO provided a Memorandum clarifying the Written Description Guidelines for claims drawn to antibodies, which can be found at www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. That Memorandum indicates that, in compliance with recent legal decisions, the disclosure of a fully characterized antigen no longer is sufficient written description of an antibody to that antigen. Accordingly, the instant claims have been evaluated in view of that guidance. Scope of the claimed genus The claims are drawn broadly drawn to: A multi-specific molecule comprising: (a) a SIRP-alpha binding domain, (b) an activating receptor-binding domain, and (c) a target antigen binding domain that binds to a target antigen expressed on a target cell co-expressing the target antigen and CD47, wherein the activating receptor-binding domain comprises an Fc domain, optionally the Fc domain is derived from IgG1 or IgG4,wherein the target antigen binding domain comprises a target antigen binding antibody domain, wherein the SIRP-alpha binding domain comprises a SIRP-alpha binding antibody domain, and wherein the multi-specific molecule selectively induces effector function of an immune effector cell co-expresses SIRP-alpha and the activating receptor in the presence of the target antigen. The dependent claims include a SIRP-alpha binding antibody domain having only the HCDRs, LCDRs, one heavy chain or one light chain defined (e.g., claims 33-35) and unlimited mutations in the SIRP-alpha binding antibody or a target antigen binding antibody domain (e.g., claim 47). Thus, the claims encompass a large genus of multi-specific molecules comprising a large genus of SIRP-alpha binding antibody domains and target antigen binding antibody domains. State of the Relevant Art As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. See Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (see Section 3) “Antibody Structure and the Antigen Binding Site” and Figure 1). Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4. Almagro provides a detailed discussion regarding various methods of humanization, including rationale design approaches and empirical approaches based on random screening. Almagro, Sections 4 and 5. Overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those antibodies with desired functional properties was high. However, even if a selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”) Absent the conserved structure provided by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what an antibody with a particular set of functional properties would look like structurally. Summary of Species disclosed in the original specification The specification teaches five SIRP-alpha binding antibodies C25, C15, C42, C59 and C73 and variants thereof. See p. 7-10. The specification teaches thirteen PD-L1 heavy chain variable region binding domains. See p. 13-15. Are the disclosed species representative of the claimed genus? MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. The specification discloses the reduction to practice five SIRP-alpha binding antibodies and thirteen PD-L1 heavy chain variable region binding domains. Antibodies produced by different methods, such as in different species or in phage, or to different epitopes would have been generally expected to be highly structurally diverse, particularly in the CDR sequences. Thus, while Applicant has described five SIRP-alpha binding antibodies and thirteen PD-L1 heavy chain variable region binding domains, each genus is very large and there are only a few described species for each genus. The species described therefore cannot be considered representative of the large genus of multi-specific molecules comprising a large genus of SIRP-alpha binding antibody domains and target antigen binding antibody domains. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Identifying characteristics and structure/function correlation In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. To meet this requirement in the instant case, the specification must describe structural features that convey the claimed binding activity, a prerequisite for utility in the recited methods of treating. As noted above, the art generally accepted that the combination of the CDRs within the VH and VL pair of an antibody were essential for binding specificity. However, the claims encompass antibodies with mutated or missing CDR regions. Accordingly, the skilled artisan would not be able to discern a structure/function correlation for antibodies other than those comprising either all six CDRs (in the context of VH and VL regions) of one parental antibody, or the VH and VL of one parental antibody. Lastly, a recitation of “humanized” only implies a particular structure if it is coupled with a description of the parental antibody VH, VL, and/or CDRs. In the absence of at least a description of the three CDRs in the VL and the three CDRs in the VH from the same parental antibody, the skilled artisan could not envision which other “humanized” antibodies might be encompassed by the claimed genus. For all the reasons presented above, one of skill in the art would not know which of the countless other antibodies encompassed by the independent claims that meet the highly general structural requirements of the claims would also be able to specifically SIRP-alpha and a target antigen. Neither the specification nor the dependent claims provide sufficient additional structure or a structure/function correlation to provide an adequate written description of the genus claimed. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of antibodies as broadly claimed. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as claimed. Claim Rejections - 35 USC § 102 The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. (a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention. 12. Claim(s) 1, 18, 19, 21, 23, 25, 26, 28, 47, 49, and 52-53 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by US 2024/0101716 A1 (Li et al. Mar. 28, 2024, effectively filed Dec. 18, 2020). “Li”. Li teaches bispecific antibodies that have binding specificity to the signal regulatory protein alpha (SIRPα) protein and to the programmed death-ligand 1 (PD-L1) protein. The antibodies and fragments can bring peripheral macrophages to PD-L1+ tumor site, thereby enhancing tumor treatment. See abstract. Li teaches antibodies targeting both SIRPα and PD-L1 to enhance both T cell function and macrophage phagocytosis for treating cancers. By virtue of the specificity to PD-L1, the antibodies can bring peripheral M1 macrophages to the tumor site that is positive of PD-L1. The anti-SIRPα specificity can block CD47/SIRPα interaction thereby enhancing the engulfment of tumor cells by macrophages. It can also enable dendritic cells to process and present tumor antigens, leading to priming and boosting of tumor-specific CD8+effector T cells. See ¶¶ 0005. Li teaches an antibody comprising an anti-signal regulatory protein alpha (SIRPα) unit and an anti-programmed death-ligand 1 (PD-L1) unit, wherein the anti-SIRPα unit comprises an Fab fragment having binding specificity to a human SIRPα protein, and the anti-PD-L1 unit comprises a single-domain antibody (sdAb) having binding specificity to a human PD-L1 protein. See ¶¶ 0007. Li teaches the cancer cells express CD47 and PD-L1 and were bound by the PD-L1 antibody. See ¶¶ 0107, Example 4 and Fig. 4. Regarding claims 1, 18, 19, and 28, Li teaches the antibody further comprises an Fc fragment, which would bind to an Fc receptor. In some embodiments, the sdAb (VHH) is fused to the heavy chain of the Fab fragment. In some embodiments, the sdAb is fused to the light chain of the Fab fragment. In some embodiments, the sdAb is fused to the C-terminus of the heavy chain. In some embodiments, the sdAb is fused to the N-terminus of the heavy chain. See ¶¶ 0008 and Examples 9-11 and Fig. 6A-6D. It is noted that the linkage of the target binding domain to the N-terminus of the Fc domain includes indirect linkages with intervening amino acids, i.e. the VH domain. See Fig. 6B of Li. Regarding claims 1, 21, 23, 25 and 26, Li teaches two anti-SIRPα antibodies (HSP210-02-hz52, a humanized version from 248G3F6, and HSP210-03-hz51, a humanized version from 300A6A6) with the SIRP-alpha binding domain at the N-terminus of the IgG4 Fc domain. See Example 11, Table 29 and Fig. 6A-D. The anti-SIRPα antibodies comprise a Fab domain. See Fig. 6A-D. Regarding claim 23, the target antigen binding antibody domain is not limited to being bound to the N-terminus of the Fc domain. Regarding claim 47, the claim encompasses unlimited substitutions or modification of the SIRP-alpha binding domain and the PD-L1 binding domain. So, claim 47 is anticipated by Li. Regarding claim 49, Li teaches humanization of the antibodies of the invention. See ¶¶ 0026, 0041, 0077, 0081, 0084-0087, 0090 and 0092, Examples 5 and 10. Regarding claim 49, Li teaches that the antibodies may be conjugated to therapeutic agents, prodrugs, peptides, proteins, enzymes, viruses, lipids, biological response modifiers, pharmaceutical agents, or PEG. See ¶¶ 0096-0101. Regarding claim 52, Li teaches making pharmaceutical compositions with pharmaceutically acceptable carriers. See ¶¶ 0010, 0113 and 0121-0125. Regarding claim 53, Li teaches polynucleotides for encoding the antibodies of the disclosure. See ¶¶ 0102 and 0105. 13. Claim(s) 1, 18, 21, 25, 26, 28, 47, 49, and 52-56 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by US 2017/0073414 A1 (Weiskopf et al. Mar. 16, 2017), “Weiskopf”. Weiskopf teaches antibodies that are bispecific for SIRPα and a second antigen (termed Bi-specific Macrophage Enhancing (BiME) antibodies) and can block the interaction of CD47 expressed on a target cell of interest with SIRPα expressed on a phagocytic cell. See abstract, ¶¶ 0005, 0006, and 0086-0088 and Fig. 4A. Weiskopf teaches binding the antibody of the invention to a phagocytic cell thereby increasing phagocytosis of target cells expressing CD47. See ¶¶ 0009 and Fig. 4A. Weiskopf teaches that the bispecific antibody includes an Fc chain that can be bound by the Fc receptor. See ¶¶ 0086 and Figs. 4A-4C. Weiskopf teaches the dual variable domain-Ig comprising CD20 (rituximab) and SIRPa binding domains (KWAR23). The CD20 binding domain is linked to the N-terminus of the Fc domain, which would bind its receptor. See Fig. 4B. It is noted that the linkage of the target binding domain to the N-terminus of the Fc domain includes indirect linkages with intervening amino acids, i.e. the VH domain of KWAR23). Regarding claim 47, the claim encompasses unlimited substitutions or modification of the SIRP-alpha binding domain. So, claim 47 is anticipated by Weiskopf. Regarding claim 49, Weiskopf teaches humanization of the antibodies. See ¶¶ 0023, 0052, 0054, 0058, 0066, and 0075. Regarding claim 49, Weiskopf teaches antibody conjugates. See ¶¶ 0007, 0054, 0064, 0074, and 0092. Regarding claim 52, Weiskopf teaches making pharmaceutical compositions with pharmaceutically acceptable carriers. See abstract, ¶¶ 0006, 0012, and 0129-0136. Regarding claims 53-55, Weiskopf teaches the disclosure further provides: isolated nucleic acids encoding the antibodies and variants thereof; a vector comprising that nucleic acid, optionally operably linked to control sequences recognized by a host cell transformed with the vector; a host cell comprising that vector; a process for producing the antibody comprising culturing the host cell so that the nucleic acid is expressed and, optionally, recovering the antibody from the host cell culture (e.g. from the host cell culture medium). See ¶¶ 0012, 0023 and 0100-0106. Regarding claim 56, Weiskopf teaches a kit comprising the antibody and instructions for using the antibody. See ¶¶ 0008, 0137 and 0138. Weiskopf teaches the kit includes a subject SIRPα antibody and one or more antibodies selected from: CETUXIMAB (binds EGFR), PANITUMUMAB (binds EGFR), RITUXIMAB (binds CD20), TRASTUZUMAB (binds HER2), PERTUZUMAB (binds HER2), ALEMTUZUMAB (binds CD52), and BRENTUXIMAB (binds CD30), GEMTUZUMAB (binds CD33), LORVOTUZUMAB (binds CD56), IPILIMUMAB (binds CTLA-4 (CD152)), and NIVOLUMAB (binds PD-1 (CD279)), which are therapeutic agents. See ¶¶ 0137. Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. 14. Claim(s) 1, 18, 19, 21, 23, 25, 26, 28, 47, 49, and 52-56 are rejected under 35 U.S.C. 103 as being unpatentable over US 2024/0101716 A1 (Li et al. Mar. 28, 2024, effectively filed Dec. 18, 2020). “Li” as applied to claims 1, 18, 19, 21, 23, 25, 26, 28, 47, 49, and 52-53 above, and further in view of US 2017/0073414 A1 (Weiskopf et al. Mar. 16, 2017), “Weiskopf”. Li teaches as set forth above, but does not teach a vector comprising the nucleic acids encoding the bispecific antibodies, a host cell comprising the vector, or a kit comprising the bispecific antibodies and a second therapeutic agent. Weiskopf teaches as set forth above. It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Li and Weiskopf and use a host cell comprising a nucleic acid vector as taught by Weiskopf to express the bispecific antibodies of Li for their production because these are routine methods of antibody production as shown by the teachings of Weiskopf. One would have been motivated to use a host cell comprising a nucleic acid vector as taught by Weiskopf to express the bispecific antibodies of Li because these are known effective methods for antibody production. Also, it would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Li and Weiskopf and make a kit comprising the bispecific antibodies of Li and a second therapeutic agent in the form of a kit, like the kit taught by Weiskopf, for convenience, storage, and/or for the purpose of commercial sale and because the kit would provide additional therapeutic agents, such as rituximab and trastuzumab, for cancer treatment. Given the well-known advantages of providing reagents in kit form, one would be motivated to combine the bispecific antibodies of Li and a second therapeutic agent as taught by Weiskopf in a kit. 15. Claim(s) 1, 18, 19, 21-23, 25, 26, 28, 47, 49, and 52-56 are rejected under 35 U.S.C. 103 as being unpatentable over US 2024/0101716 A1 (Li et al. Mar. 28, 2024, effectively filed Dec. 18, 2020), “Li” in view of US 2017/0073414 A1 (Weiskopf et al. Mar. 16, 2017), as applied to claims 1, 18, 19, 21, 23, 25, 26, 28, 47, 49, and 52-56 above, and further in view of Spiess et al. (Mol. Immunology, 2015 67;95-106), “Spiess”. Li and Weiskopf teach as set forth above, but do not teach the multi-specific molecule structures of claims 22, 29 and 30 Spiess teaches many bispecific antibody drugs are designed to retarget T cells to kill tumor cells, whereas most others are intended to interact with two different disease mediators such as cell surface receptors, soluble ligands and other proteins. The modular architecture of antibodies has been exploited to create more than 60 different bispecific antibody formats. These diverse formats provide great opportunity to tailor the design of bispecific antibodies to match the proposed mechanisms of action and the intended clinical application. See abstract. Spiess teaches Bispecific IgG (BsIgG) is a commonly used BsAb format that is monovalent for each antigen (1 + 1 antigen-binding valency) with the binding domains linked to the N-terminus of the Fc domain. See § 2.1. Bispecific antibodies with IgG-like structure and Fig. 1. Spiess teaches bispecific antibodies with a binding domains on the C-terminus of the Fc domains. See Igg(H)-scFv*, IgG(H)-2scFv*, and Intrabody in Fig. 1. Spiess teaches bispecific antibodies with a binding domains on the C-terminus of the light chain. See IgG(L)-scFv and IgG(L)-V in Fig. 1. It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Li, Weiskopf and Spiess and make the bispecific antibodies of Li and Weiskopf in different bispecific antibody formats as taught by Spiess because Spiess teaches that diverse formats bispecific antibodies provide great opportunity to tailor the design of bispecific antibodies to match the proposed mechanisms of action and the intended clinical application. Thus, one of skill in the art would have been motivated to make the bispecific antibodies of Li and Weiskopf in different bispecific antibody formats as taught by Spiess to optimize the activity of the bispecific antibodies of Li and Weiskopf. Double Patenting The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer. 16. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35, 37, 47, 49, and 52-55 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 5, 8-11, 13, 16, 17, 19, 23, 26, 39 and 32-35, 40-42, 46 and 49 of co-pending Application No. 18/292,922 (US 2025/0270315) in view of US 2024/0101716 A1 (Li et al. Mar. 28, 2024, effectively filed Dec. 18, 2020), “Li” and in view of Spiess et al. (Mol. Immunology, 2015 67;95-106), “Spiess”. This is a provisional nonstatutory double patenting rejection. The ’922 claims are drawn to: 1. An antibody or an antigen-binding fragment thereof capable of specifically binding to human SIRPα, comprising a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3, wherein a) the HCDR1 comprises an amino acid sequence of DYYMS (SEQ ID NO: 1), the HCDR2 comprises an amino acid sequence of FIKNEANGYTTESSASVKG (SEQ ID NO: 2), the HCDR3 comprises an amino acid sequence of YDYYGSNYNWYFDA (SEQ ID NO: 3), the LCDR1 comprises an amino acid sequence of KASQNVRTAVA (SEQ ID NO: 4), and the LCDR2 comprises an amino acid sequence of LASKRHT (SEQ ID NO: 5), and the LCDR3 comprises an amino acid sequence of LQHWIHPLT (SEQ ID NO: 6), b) the HCDR1 comprises an amino acid sequence of X.sub.1YYMH (SEQ ID NO: 18), the HCDR2 comprises an amino acid sequence of RIDPEDX.sub.2EX.sub.3KYAPKFQG (SEQ ID NO: 19), the HCDR3 comprises an amino acid sequence of GX.sub.18X.sub.4X.sub.5Y (SEQ ID NO: 20), the LCDR1 comprises an amino acid sequence of SASSSVSSSYLY (SEQ ID NO: 10), LCDR2 comprises an amino acid sequence of STSNLAS (SEQ ID NO: 11), and the LCDR3 comprises an amino acid sequence of X.sub.6QWSSYPYT (SEQ ID NO: 21), c) the HCDR1 comprises an amino acid sequence of TYGMS (SEQ ID NO: 22), the HCDR2 comprises an amino acid sequence of WINTYSGVX.sub.19TX.sub.7ADDFX&G (SEQ ID NO: 38), the HCDR3 comprises an amino acid sequence of DPHX.sub.9YGX.sub.10SPAWFX.sub.11Y (SEQ ID NO: 39), the LCDR1 comprises an amino acid sequence of X.sub.12ASQX.sub.13 VGIX.sub.14VA (SEQ ID NO: 40), the LCDR2 comprises an amino acid sequence of SASNRX.sub.15T (SEQ ID NO: 41), and the LCDR3 comprises an amino acid sequence of QQYSX.sub.16YPX.sub.17T (SEQ ID NO: 42), or d) the HCDR1 comprises an amino acid sequence of EYVLS (SEQ ID NO: 43), the HCDR2 comprises an amino acid sequence of EIYPGTITTYYNEKFKG (SEQ ID NO: 44), the HCDR3 comprises an amino acid sequence of FYDYDGGWFAY (SEQ ID NO: 45), the LCDR1 comprises an amino acid sequence of SASSSVSSSDLH (SEQ ID NO: 46), the LCDR2 comprises an amino acid sequence of GTSNLAS (SEQ ID NO: 47), and the LCDR3 comprises an amino acid sequence of QQWSGYPWT (SEQ ID NO: 48), wherein X.sub.1 is A or D; X.sub.2 is G or A; X.sub.3 is T or S; X.sub.4 is L or Y; X.sub.5 is E or A; X.sub.6 is Y or H; X.sub.7 is Y or C; X.sub.8 is K or Q; X.sub.9 is Y or S; X.sub.10 is N or T or S; X.sub.11 is P or A or V; X.sub.12 is E or K; X.sub.13 is N or I; X.sub.14 is S or A; X.sub.15 is Y or F; X.sub.16 is S or T or A; X.sub.17 is F or L; X.sub.18 is S or absent; X.sub.19 is S or P. 3. The antibody or antigen-binding fragment thereof of claim 1, wherein a) the HCDR1 comprises an amino acid sequence of AYYMH (SEQ ID NO: 7) or DYYMH (SEQ ID NO: 13), b) the HCDR2 comprises an amino acid sequence selected from the group consisting of RIDPEDGESKYAPKFQG (SEQ ID NO: 8), RIDPEDGETKYAPKFQG (SEQ ID NO: 14) and RIDPEDAETKYAPKFQG (SEQ ID NO: 17), c) the HCDR3 comprises an amino acid sequence of GSYEY (SEQ ID NO: 9) or GLAY (SEQ ID NO: 15), d) the LCDR1 comprises an amino acid sequence of SASSSVSSSYLY (SEQ ID NO: 10), e) the LCDR2 comprises an amino acid sequence of STSNLAS (SEQ ID NO: 11), and f) the LCDR3 comprises an amino acid sequence of YQWSSYPYT (SEQ ID NO: 12) or HQWSSYPYT (SEQ ID NO: 16). 5. The antibody or antigen-binding fragment thereof of claim 1, wherein a) the HCDR1 comprises an amino acid sequence of TYGMS (SEQ ID NO: 22), b) the HCDR2 comprises an amino acid sequence selected from the group consisting of WINTYSGVSTCADDFKG (SEQ ID NO: 23), WINTYSGVPTYADDFQG (SEQ ID NO: 28) and WINTYSGVPTYADDFKG (SEQ ID NO: 33), c) the HCDR3 comprises an amino acid sequence selected from the group consisting of DPHSYGNSPAWFPY (SEQ ID NO: 24), DPHYYGTSPAWFAY (SEQ ID NO: 29) and DPHYYGSSPAWFVY (SEQ ID NO: 34), d) the LCDR1 comprises an amino acid sequence selected from the group consisting of KASQNVGISVA (SEQ ID NO: 25), KASQIVGIAVA (SEQ ID NO: 30) and EASQIVGIAVA (SEQ ID NO: 35), e) the LCDR2 comprises an amino acid sequence selected from the group consisting of SASNRYT (SEQ ID NO: 26) and SASNRFT (SEQ ID NO: 31), and f) the LCDR3 comprises an amino acid sequence selected from the group consisting of QQYSSYPLT (SEQ ID NO: 27), QQYSTYPFT (SEQ ID NO: 32) and QQYSAYPFT (SEQ ID NO: 37). 8. The antibody or an antigen-binding fragment thereof of claim 1, wherein a) a HCDR1 comprising the sequence of SEQ ID NO: 1, a HCDR2 comprising the sequence of SEQ ID NO: 2, and a HCDR3 comprising the sequence of SEQ ID NO: 3, a LCDR1 comprising the sequence of SEQ ID NO: 4, a LCDR2 comprising the sequence of SEQ ID NO: 5, and a LCDR3 comprising the sequence of SEQ ID NO: 6; or b) a HCDR1 comprising the sequence of SEQ ID NO: 7, a HCDR2 comprising the sequence of SEQ ID NO: 8, and a HCDR3 comprising the sequence of SEQ ID NO: 9, a LCDR1 comprising the sequence of SEQ ID NO: 10, a LCDR2 comprising the sequence of SEQ ID NO: 11, and a LCDR3 comprising the sequence of SEQ ID NO: 12; or c) a HCDR1 comprising the sequence of SEQ ID NO: 13, a HCDR2 comprising the sequence of SEQ ID NO: 14 or SEQ ID NO: 17, and a HCDR3 comprising the sequence of SEQ ID NO: 15, a LCDR1 comprising the sequence of SEQ ID NO: 10, a LCDR2 comprising the sequence of SEQ ID NO: 11, and a LCDR3 comprising the sequence of SEQ ID NO: 16; or d) a HCDR1 comprising the sequence of SEQ ID NO: 22, a HCDR2 comprising the sequence of SEQ ID NO: 23, and a HCDR3 comprising the sequence of SEQ ID NO: 24, a LCDR 1 comprising the sequence of SEQ ID NO: 25, a LCDR2 comprising the sequence of SEQ ID NO: 26, and a LCDR3 comprising the sequence of SEQ ID NO: 27; or e) a HCDR1 comprising the sequence of SEQ ID NO: 22, a HCDR2 comprising the sequence of SEQ ID NO: 28, and a HCDR3 comprising the sequence of SEQ ID NO: 29, a LCDR1 comprising the sequence of SEQ ID NO: 30, a LCDR2 comprising the sequence of SEQ ID NO: 31, and a LCDR3 comprising the sequence of SEQ ID NO: 32; or f) a HCDR1 comprising the sequence of SEQ ID NO: 22, a HCDR2 comprising the sequence of SEQ ID NO: 33, and a HCDR3 comprising the sequence of SEQ ID NO: 34, a LCDR1 comprising the sequence of SEQ ID NO: 35, a LCDR2 comprising the sequence of SEQ ID NO: 26, and a LCDR3 comprising the sequence of SEQ ID NO: 37; or g) a HCDR1 comprising the sequence of SEQ ID NO: 43, a HCDR2 comprising the sequence of SEQ ID NO: 44, and a HCDR3 comprising the sequence of SEQ ID NO: 45, a LCDR1 comprising the sequence of SEQ ID NO: 46, a LCDR2 comprising the sequence of SEQ ID NO: 47, and a LCDR3 comprising the sequence of SEQ ID NO: 48. 9. The antibody or an antigen-binding fragment thereof of claim 1, further comprising heavy chain HFR1, HFR2, HFR3 and HFR4, and light chain LFR1, LFR2, LFR3 and LFR4, wherein: a) the HFR1 comprises EVQLVQSGAEVKKPGATVKISCKX.sub.20SGFNIK (SEQ ID NO: 84) or a homologous sequence of at least 80% sequence identity thereof, b) the HFR2 comprises WVQQAPGKGLEWIG (SEQ ID NO: 74) or a homologous sequence of at least 80% sequence identity thereof, c) the HFR3 sequence comprises RVTITADTSTX.sub.21 TAYMELSSLRSEDTAVYYCDR (SEQ ID NO: 85) or a homologous sequence of at least 80% sequence identity thereof, d) the HFR4 comprises WGQGTLVTVSS (SEQ ID NO: 76) or a homologous sequence of at least 80% sequence identity thereof, e) the LFR1 comprises EIVLTQSPATLSLSPGERATLSC (SEQ ID NO: 77) or a homologous sequence of at least 80% sequence identity thereof, f) the LFR2 comprises WYQQKPGQAPKLWIY (SEQ ID NO: 78) or a homologous sequence of at least 80% sequence identity thereof, g) the LFR3 comprises GIPARFSGSGSGTDX.sub.22TLTISSLEPEDFAVYYC (SEQ ID NO: 86) or a homologous sequence of at least 80% sequence identity thereof, and h) the LFR4 comprises FGQGTKLEIK (SEQ ID NO: 80) or a homologous sequence of at least 80% sequence identity thereof, wherein X.sub.20 is A or V; X.sub.21 is N or D; X.sub.22 is Y or F. 10. The antibody or antigen-binding fragment thereof of claim 9, wherein: a) the HFR1 comprises EVQLVQSGAEVKKPGATVKISCKASGFNIK (SEQ ID NO: 83) or EVQLVQSGAEVKKPGATVKISCKVSGFNIK (SEQ ID NO: 73), or a homologous sequence of at least 80% sequence identity thereof, and/or b) the HFR2 comprises WVQQAPGKGLEWIG (SEQ ID NO: 74) or a homologous sequence of at least 80% sequence identity thereof, and/or c) the HFR3 sequence comprises RVTITADTSTNTAYMELSSLRSEDTAVYYCDR (SEQ ID NO: 75) or RVTITADTSTDTAYMELSSLRSEDTAVYYCDR (SEQ ID NO: 82) or a homologous sequence of at least 80% sequence identity thereof, and/or d) the HFR4 comprises WGQGTLVTVSS (SEQ ID NO: 76) or a homologous sequence of at least 80% sequence identity thereof, and/or e) the LFR1 comprises EIVLTQSPATLSLSPGERATLSC (SEQ ID NO: 77) or a homologous sequence of at least 80% sequence identity thereof, and/or f) the LFR2 comprises WYQQKPGQAPKLWIY (SEQ ID NO: 78) or a homologous sequence of at least 80% sequence identity thereof, and/or g) the LFR3 comprises GIPARFSGSGSGTDYTLTISSLEPEDFAVYYC (SEQ ID NO: 79) or GIPARFSGSGSGTDFTLTISSLEPEDFAVYYC (SEQ ID NO: 81) or a homologous sequence of at least 80% sequence identity thereof, and/or h) the LFR4 comprises FGQGTKLEIK (SEQ ID NO: 80) or a homologous sequence of at least 80% sequence identity thereof. 11. The antibody or an antigen-binding fragment thereof of claim 1, wherein the heavy chain variable region comprises the sequence selected from the group consisting of SEQ ID NO: 63, SEQ ID NO: 65 and SEQ ID NO: 67, and a homologous sequence thereof having at least 80% sequence identity yet retaining specific binding affinity to human SIRPα; and the light chain variable region comprises the sequence selected from the group consisting of SEQ ID NO: 64 and SEQ ID NO: 66, and a homologous sequence thereof having at least 80% sequence identity yet retaining specific binding affinity to human SIRPα. 13. The antibody or an antigen-binding fragment thereof of claim 1, wherein a) the heavy chain variable region comprises the sequence of SEQ ID NO: 49 and the light chain variable region comprises the sequence of SEQ ID NO: 50; or b) the heavy chain variable region comprises the sequence of SEQ ID NO: 51 and the light chain variable region comprises the sequence of SEQ ID NO: 52; or c) the heavy chain variable region comprises the sequence of SEQ ID NO: 53 and the light chain variable region comprises the sequence of SEQ ID NO: 54; or d) the heavy chain variable region comprises the sequence of SEQ ID NO: 55 and the light chain variable region comprises the sequence of SEQ ID NO: 56; or e) the heavy chain variable region comprises the sequence of SEQ ID NO: 57 and the light chain variable region comprises the sequence of SEQ ID NO: 58; or f) the heavy chain variable region comprises the sequence of SEQ ID NO: 59 and the light chain variable region comprises the sequence of SEQ ID NO: 60; or g) the heavy chain variable region comprises the sequence of SEQ ID NO: 61 and the light chain variable region comprises the sequence of SEQ ID NO: 62; or h) the heavy chain variable region comprises the sequence of SEQ ID NO: 63 and the light chain variable region comprises the sequence of SEQ ID NO: 64; or i) the heavy chain variable region comprises the sequence of SEQ ID NO: 63 and the light chain variable region comprises the sequence of SEQ ID NO: 66; or j) the heavy chain variable region comprises the sequence of SEQ ID NO: 65 and the light chain variable region comprises the sequence of SEQ ID NO: 64; or k) the heavy chain variable region comprises the sequence of SEQ ID NO: 67 and the light chain variable region comprises the sequence of SEQ ID NO: 64; or l) the heavy chain variable region comprises the sequence of SEQ ID NO: 67 and the light chain variable region comprises the sequence of SEQ ID NO: 66. 16. The antibody or an antigen-binding fragment thereof of claim 1, further comprising an Fc region, optionally an Fc region of human immunoglobulin (Ig), or optionally an Fc region of human IgG. 17. The antibody or an antigen-binding fragment thereof of claim 16, wherein the Fc region is derived from human IgG4, optionally wherein the Fc region derived from human IgG4 comprises a S228P mutation and/or a L235E mutation. 19. The antibody or an antigen-binding fragment thereof of claim 1, which is a) humanized; b) a monoclonal antibody, a bispecific antibody, a multi-specific antibody, a recombinant antibody, a chimeric antibody, a labeled antibody, a bivalent antibody, an anti-idiotypic antibody or a fusion protein; and/or c) a diabody, a Fab, a Fab′, a F(ab′).sub.2, a Fd, an Fv fragment, a disulfide stabilized FV fragment (dsFv), a (dsFv).sub.2, a bispecific dsFv (dsFv-dsFv′), a disulfide stabilized diabody (ds diabody), a single-chain antibody molecule (scFv), and scFv dimer (bivalent diabody), a multispecific antibody, a camelized single domain antibody, a nanobody, a domain antibody, or a bivalent domain antibody. 23. An antibody or an antigen-binding fragment thereof which competes for binding to human SIRPα with an antibody comprising: a) a heavy chain variable region comprising the sequence of SEQ ID NO: 53, and a light chain variable region comprising the sequence of SEQ ID NO: 54; b) a heavy chain variable region comprising the sequence of SEQ ID NO: 55, and a light chain variable region comprising the sequence of SEQ ID NO: 56; and/or c) a heavy chain variable region comprising the sequence of SEQ ID NO: 61 and a light chain variable region comprising the sequence of SEQ ID NO: 62. 26. The antibody or an antigen-binding fragment thereof of claim 1, which is bispecific, wherein a) the antibody or an antigen-binding fragment thereof is capable of specifically binding to a second antigen other than SIRPα, optionally wherein the second antigen is a tumor antigen, tumor surface antigen, an inflammatory antigen, an antigen of an infectious microorganism; or b) the antibody or an antigen-binding fragment thereof is capable of specifically binding to a second epitope on SIRPα. 30. The antibody or an antigen-binding fragment thereof of claim 1, which is linked to one or more conjugate moieties, optionally wherein the conjugate moiety comprises a clearance-modifying agent, a chemotherapeutic agent, a toxin, a radioactive isotope, a lanthanide, a luminescent label, a fluorescent label, an enzyme-substrate label, a DNA-alkylator, a topoisomerase inhibitor, a tubulin-binder, a purification moiety, or other anticancer drugs. 32. A pharmaceutical composition comprising the antibody or an antigen-binding fragment thereof of claim 1, and one or more pharmaceutically acceptable carriers. 33. An isolated polynucleotide encoding the antibody or an antigen-binding fragment thereof of claim 1. 34. A vector comprising the isolated polynucleotide of claim 33. 35. A host cell comprising the vector of claim 34. The SIRPα antibodies comprise HCDRs SEQ ID NOs: 23-25, LCDRs SEQ ID NOs: 26-28 and SEQ ID NOs: 1 and 2. See Appendix The ‘922 claims teach as set forth above, but do not teach making a bispecific molecule with a PD-L1 binding domain or the various bispecific structures claimed. Li and Spiess teach as set forth above. Li additionally teaches PD-L1 is a critical “don't find me” signal to the adaptive immune system. CD47/SIRPα transmits an anti-phagocytic signal, known as the “don't eat me” signal, to the innate immune system. It is contemplated that dual targeting both innate and adaptive immune checkpoints can help maximize anti-tumor therapeutic effect and elicit more durable responses. See ¶ 0033. It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘922 claims Li, and Spiess and make the bispecific antibodies of the ‘922 claims alos target PD-L1 as taught by Li because Li teaches that dual targeting both innate (CD47/SIRPα) and adaptive immune (PD-L1) checkpoints can help maximize anti-tumor therapeutic effect and elicit more durable responses and Li teaches effectively targeting SIRPα and PD-L1 with bispecific antibodies. It would also have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘922 claims Li, and Spiess and make the bispecific antibodies of the ‘922 claims and Li in different bispecific antibody formats as taught by Spiess because Spiess teaches that diverse formats bispecific antibodies provide great opportunity to tailor the design of bispecific antibodies to match the proposed mechanisms of action and the intended clinical application. Thus, one of skill in the art would have been motivated to make the bispecific antibodies of the ‘922 claims and Li in different bispecific antibody formats as taught by Spiess to optimize the activity of the bispecific antibodies of the ‘922 claims and Li. 17. Claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35, 37, 47, 49, and 52-56 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 5, 8-11, 13, 16, 17, 19, 23, 26, 39 and 32-35, 40-42, 46 and 49 of co-pending Application No. 18/292,922 (US 2025/0270315) in view of US 2024/0101716 A1 (Li et al. Mar. 28, 2024, effectively filed Dec. 18, 2020), “Li” and in view of Spiess et al. (Mol. Immunology, 2015 67;95-106), “Spiess” as applied to claims 1, 18, 19, 21-23, 25, 26, 28-30, 33-35, 37, 47, 49, and 52-55 above, in further view of US 2017/0073414 A1 (Weiskopf et al. Mar. 16, 2017). The ‘922 claims, Li and Spiess teach as set forth above, but do not teach a kit comprising the bispecific antibodies and a second therapeutic agent. Weiskopf teaches as set forth above. It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘922 claims, Li and Spiess and Weiskopf and make a kit comprising the bispecific antibodies of the ‘922 claims, Li Spiess and Weiskopf and a second therapeutic agent in the form of a kit, like the kit taught by Weiskopf, for convenience, storage, and/or for the purpose of commercial sale and because the kit would provide additional therapeutic agents, such as rituximab and trastuzumab, for cancer treatment. Given the well-known advantages of providing reagents in kit form, one would be motivated to combine the bispecific antibodies of the ‘922 claims, Li, Spiess and Weiskopf and a second therapeutic agent as taught by Weiskopf in a kit. This is a provisional nonstatutory double patenting rejection. 18. Claim 1, 18, 19, 21-23, 25, 26, 28-30, 33-34, 37, 44-47, 49, and 52-56 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 9-13, 15, 18, 28, 29, 38-40, 42, 43, 49 and 51 of co-pending Application No. 19/148,954 (reference application). The ‘954 claims are drawn to: 1. An anti-PDL1 single domain antibody (sdAb), comprising heavy chain complementarity determining regions (CDRs) 1, 2, and 3, wherein said CDR1 is different from an amino acid sequence set forth in SEQ ID NO: 32, 36 or 39 by no more than 3, 2 or 1 amino acid; said CDR2 is different from an amino acid sequence set forth in SEQ ID NO: 33, 35 or 37 by no more than 3, 2 or 1 amino acid; and said CDR3 is different from an amino acid sequence set forth in SEQ ID NO: 34 or 38 by no more than one amino acid. 9. A fusion protein, comprising: a) a first domain binding to PDL1, comprising heavy chain complementarity determining regions CDR1, CDR2, and CDR3, said CDR1, CDR2, and CDR3 have amino acid sequences about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identical to the amino acid sequences set forth in: (1) SEQ ID NOs: 32, 33, and 34, respectively;(2) SEQ ID NOs: 32, 35, and 34, respectively; (3) SEQ ID NOs: 36, 37, and 38, respectively; or (4) SEQ ID NOs: 39, 37, and 38, respectively; and b)a second domain binding to SIRPa . 10. The fusion protein of claim 9, wherein the first domain comprises an amino acid sequence at least 80%, 85%, 90%, 95%, 96%, 97%,98% or 99% identical to one of amino acid sequences set forth in SEQ ID NOs: 1-21. 11. The fusion protein of claim 9, wherein the second domain binds to SIRP a expressed by effector cells. 12. The fusion protein of claim 9, the second domain comprises a heavy chain variable region (VH) paired with a light chain variable region (VL), wherein a)the VH comprising CDR1, CDR2, and CDR3, wherein the VH CDR1, CDR2, and CDR3 have amino acid sequences about 80% to about 100% identical to amino acid sequences set forth in: (1) SEQ ID NOs: 40, 41, and 42, respectively; (2) SEQ ID NOs: 40, 43, and 44, respectively; and b)the VL comprising CDR1, CDR2, and CDR3, wherein the VL CDR1, CDR2, and CDR3 have amino acid sequences about 80% to about 100% identical to amino acid sequences set forth in SEQ ID NOs: 45, 46, and 47, respectively. 13. The fusion protein of claim 9, wherein the second domain comprises a light chain, wherein the light chain is a kappa (k)or lamda ( l) light chain; and/or wherein the light chain comprises a light chain constant region (CL) having an amino acid sequence set forth in SEQ ID NO: 30 or 31. 15. The fusion protein of claim 9, wherein the second domain comprises a heavy chain constant region 1 (CH1),and/or wherein the second domain is an anti-SIRP a Fab fragment; and/or the second domain comprises a VH-CH1 fragment paired with the light chain, wherein a) the VH-CH1 fragment having an amino acid sequence at least about 80%. about 90%.about 95%. about 96%. about 97%. about 98%, or about 99% identical to the amino acid sequence set forth in SEO ID NO: 22, and the light chain having an amino acid sequence at least about 80%. about 90%. about 95%. about 96%. about 97%. about 98%. or about 99% identical to the amino acid sequence set forth in SEO ID NO: 23:or b)the VH-CH1 fragment having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 24, and the light chain having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 25. 18. The fusion protein of claim 9, wherein the first domain and the second domain are covalently linked via a Fc fragment; wherein the first domain is fused to N-terminus of Fc fragment, and the second domain is fused to C-terminus of the Fc fragment; wherein the fusion protein is a symmetric bispecific molecule, wherein two first domains are fused to N-terminus of the Fc fragment and two second domains are fused to C-terminus of the Fc fragment; the C-terminus of the first domain is fused to the N-terminus of the fragment, and/or the C- terminus of the VH-CH1 fragment is fused to the C-terminus of the fragment; wherein the Fc fragment is derived from human immunoglobulin, optionally the human immunoglobulin is IgG4 or IgG1; wherein the Fc fragment is human IgG4 with mutation S228P, or human IgGl with mutation C220S, numbered by EU numbering scheme; wherein the Fc fragment comprises an amino acid sequence set forth in SEQ ID NO: 26 or 27; wherein the Fc fragment and the second domain are covalently linked via a peptide linker; wherein the peptide linker has the formula (Gly4Ser)n, n is an integer from 1 to 5; and/or wherein the first domain and the second domain are covalently linked via (Gly4Ser)3 or (Gly4Ser)4. 28. The fusion protein of claims 9, wherein the fusion protein comprises (1) a heavy chain having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 28, and a light chain having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 23; or (2) a heavy chain having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 48, and a light chain having an amino acid sequence at least about 80%, about 90%, about 95%, about 96%, about 97%, about 98%, or about 99% identical to the amino acid sequence set forth in SEQ ID NO: 25. 29. The fusion protein of claim 9, wherein the fusion protein enhances effector cells phagocytosis of tumor cells, optionally the tumor cells express target antigen to which the first domain binds; wherein the fusion protein binds to human PDL1 and human SIRPα; wherein the fusion protein barely induces the phagocytosis to human monocytes or human PBMCs; wherein the fusion protein at least partially reprograms M2 or M2 like macrophages to M1 or M1-like macrophages; wherein the fusion protein stimulates macrophage to produce inflammatory cytokine including TNF-a, IL-6 and CXCL-10; wherein the fusion protein barely induces PBMC to produce cytokines, which includes IL-2, IFN-y, TNF-α, IL-6 and IL-10; wherein the fusion protein blocks the interaction of PD1 and PDL1, optionally, the fusion protein blocks the interaction of PD1 and PDL1 with EC 50 no more than 10, 9, 8, or 7 nM; wherein the EC50 of binding activity of the fusion protein to the SIRPα is no more than 10, 5, 4,3,2, or 1 nM; and/or wherein the effector cells comprise macrophage. 38. An isolated polynucleotide encoding the single domain antibody of claim 1or encoding the fusion protein comprising the single domain antibody of claims 9. 39. A construct comprising the isolated polynucleotide of claim 38. The polynucleotide construct of claim 39 is a vector as it is used to express polynucleotide in claim 40. 40. An antibody expressing system, comprising the construct including the isolated polynucleotide of claim 38, wherein , the expressing system is a cell expression system. 42. A pharmaceutical composition comprising the anti-PDL1 single domain antibody of claims 1 or the fusion protein comprising the single domain antibody, and a pharmaceutically acceptable carrier. 43. A kit comprising the anti-PDL1 single domain antibody of claim 1, the fusion protein comprising the single domain antibody. This is interpreted as a combination of both components. SEQ ID NOs: 131, 132 and 133 are comprised by SEQ ID NOs: 1, 3-5 and 28 of the ‘954 claims. See Appendix. SEQ ID NO: 111 is comprised by SEQ ID NOs: 1 and 28 of the ‘954 claims. See Appendix. SEQ ID NOs: 137, 138 and 139 are comprised by SEQ ID NOs: 2, 7-12 and 15-18 of the ‘954 claims. See Appendix. SEQ ID NO: 118 is comprised by SEQ ID NO: 2 of the ‘954 claims. See Appendix. SEQ ID NOs: 23, 198 and 25 are comprised by SEQ ID NOs: 22 and 28 of the ‘954 claims. See Appendix. SEQ ID NOs:26, 27, and 28 are comprised by SEQ ID NOs: 23 and 25 of the ‘954 claims. See Appendix. SEQ ID NO: 159 is 98.5% identical to SEQ ID NOs: 22 and 28 of the ‘954 claims. See Appendix. SEQ ID NO: 160 is 99.1% identical to SEQ ID NOs: 23 and 25 of the ‘954 claims. See Appendix. SEQ ID NO: 9 is comprised by SEQ ID NOs: 22 and 28 of the ‘954 claims. See Appendix. SEQ ID NO: 10 is comprised by SEQ ID NOs: 23 of the ‘954 claims. See Appendix. Although the conflicting claims are not identical, they are not patentably distinct from each other because they relate to the same inventive concept and would have been obvious in view of the co-pending claims because the structure of the bispecific binding domains of the fusion protein could be engineered in different orientations to optimize its activity. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Conclusion 18. No claims allowed. The antibodies of claims 33-35, 37, and 44-46 are free of prior art. 19. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Greg Emch can be reached at 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /PETER J REDDIG/Primary Examiner, Art Unit 1646 APPENDIX Alignment of SEQ ID NOs: 23-25 with SEQ ID NO: 53 of ‘922 ALIGNMENT: Query Match 83.4%; Score 123.4; Length 113; Best Local Similarity 36.1%; Matches 26; Conservative 0; Mismatches 0; Indels 46; Gaps 2; Qy 1 DYYMH--------------RIDPEDGETKYAPKFQG------------------------ 22 ||||| ||||||||||||||||| Db 31 DYYMHWVKQRTEQGLEWIGRIDPEDGETKYAPKFQGKATITADTSSNTAYLQLSSLTSED 90 Qy 23 --------GLAY 26 |||| Db 91 TAVYYCDRGLAY 102 Alignment of SEQ ID NO: 1 with SEQ ID NO: 53 of ‘922 ALIGNMENT: Query Match 100.0%; Score 594; Length 113; Best Local Similarity 100.0%; Matches 113; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EVQLQQSGAELVKPGASVKLSCTASGFNIKDYYMHWVKQRTEQGLEWIGRIDPEDGETKY 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EVQLQQSGAELVKPGASVKLSCTASGFNIKDYYMHWVKQRTEQGLEWIGRIDPEDGETKY 60 Qy 61 APKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCDRGLAYWGQGTLVTVSA 113 ||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 APKFQGKATITADTSSNTAYLQLSSLTSEDTAVYYCDRGLAYWGQGTLVTVSA 113 Alignment of SEQ ID NOs: 26-28 with SEQ ID NO: 54 of ‘922 ALIGNMENT: Query Match 82.7%; Score 118.3; Length 108; Best Local Similarity 37.3%; Matches 28; Conservative 0; Mismatches 0; Indels 47; Gaps 2; Qy 1 SASSSVSSSYL---------------YSTSNLAS-------------------------- 19 ||||||||||| |||||||| Db 24 SASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIPARFSGSGSGTDYTLTISSLEPED 83 Qy 20 ------HQWSSYPYT 28 ||||||||| Db 84 FAVYYCHQWSSYPYT 98 Alignment of SEQ ID NO: 2 with SEQ ID NO: 54 of ‘922 ALIGNMENT: Query Match 100.0%; Score 562; Length 108; Best Local Similarity 100.0%; Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 QIVLTQSPAIMSASPGEKVTLTCSASSSVSSSYLYWYQQKPGSSPKLWIYSTSNLASGVP 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 QIVLTQSPAIMSASPGEKVTLTCSASSSVSSSYLYWYQQKPGSSPKLWIYSTSNLASGVP 60 Qy 61 ARFSGSGSGTSYSLTISSMEAEDAASYFCHQWSSYPYTFGGGTKLEIK 108 |||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ARFSGSGSGTSYSLTISSMEAEDAASYFCHQWSSYPYTFGGGTKLEIK 108 Alignment of SEQ ID NOs: 2 with SEQ ID NO: 54 of ‘922 ALIGNMENT: Query Match 100.0%; Score 562; Length 108; Best Local Similarity 100.0%; Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 QIVLTQSPAIMSASPGEKVTLTCSASSSVSSSYLYWYQQKPGSSPKLWIYSTSNLASGVP 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 QIVLTQSPAIMSASPGEKVTLTCSASSSVSSSYLYWYQQKPGSSPKLWIYSTSNLASGVP 60 Qy 61 ARFSGSGSGTSYSLTISSMEAEDAASYFCHQWSSYPYTFGGGTKLEIK 108 |||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ARFSGSGSGTSYSLTISSMEAEDAASYFCHQWSSYPYTFGGGTKLEIK 108 Alignment of SEQ ID NOs: 131, 132, and133 with SEQ ID NO: 4 of ‘954 US-19-148-954-4 Sequence 4, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 4 LENGTH: 119 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..119 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 83.4%; Score 126.7; Length 119; Best Local Similarity 36.1%; Matches 30; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GFTFSSHAMS---------------IDTSGTTT--------------------------- 18 |||||||||| |||||||| Db 26 GFTFSSHAMSWVRQAPGKGLEWVSDIDTSGTTTDYADSVKGRFTISRDNSKNTLYLQMNS 85 Qy 19 -----------AKGPREATDIRS 30 |||||||||||| Db 86 LRPEDTAVYYCAKGPREATDIRS 108 Alignment of SEQ ID NOs: 131, 132, and133 with SEQ ID NO: 28 of ‘954 US-19-148-954-28 Sequence 28, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 28 LENGTH: 587 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..587 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 83.4%; Score 126.7; Length 587; Best Local Similarity 36.1%; Matches 30; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GFTFSSHAMS---------------IDTSGTTT--------------------------- 18 |||||||||| |||||||| Db 26 GFTFSSHAMSWVRQAPGKGLEWVSDIDTSGTTTDYADSVKGRFTISRDNAKNTLYLQMNS 85 Qy 19 -----------AKGPREATDIRS 30 |||||||||||| Db 86 LKPEDTAVYYCAKGPREATDIRS 108 Alignment of SEQ ID NO: 111 with SEQ ID NO: 28 of ‘954 RESULT 3 US-19-148-954-28 Sequence 28, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 28 LENGTH: 587 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..587 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 100.0%; Score 619; Length 587; Best Local Similarity 100.0%; Matches 119; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EVQLVESGGGLVQAGGSLRLSCAASGFTFSSHAMSWVRQAPGKGLEWVSDIDTSGTTTDY 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EVQLVESGGGLVQAGGSLRLSCAASGFTFSSHAMSWVRQAPGKGLEWVSDIDTSGTTTDY 60 Qy 61 ADSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCAKGPREATDIRSWGQGTQVTVSS 119 ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ADSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCAKGPREATDIRSWGQGTQVTVSS 119 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 16 of ‘954 RESULT 2 US-19-148-954-16 Sequence 16, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 16 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQAPGKGLEWVASISRSGDTYYEDSVKGRFTISRDNAKNSVYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RAEDTAVYHCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 17 of ‘954 RESULT 3 US-19-148-954-17 Sequence 17, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 17 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKDREWVASISRSGDTYYEDSVKGRFTISRDNAKNSLYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RPEDTAVYYCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 18 of ‘954 RESULT 4 US-19-148-954-18 Sequence 18, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 18 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQAPGKGLEWVASISRSGDTYYEDSVKGRFTISRDNAKNSLYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RAEDTAVYYCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 12 of ‘954 RESULT 5 US-19-148-954-12 Sequence 12, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 12 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKDREWVSSISRSGDTYYEDSVKGRFTISRDNAKNSVYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RPEDTAVYHCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 8 of ‘954 RESULT 6 US-19-148-954-8 Sequence 8, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 8 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKDREWVASISRSGDTYYEDSVKGRFTISRDNAKNSVYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RAEDTAVYHCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 13 of ‘954 RESULT 7 US-19-148-954-13 Sequence 13, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 13 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKDREWVASISRSGDTYYEDSVKGRFTISRDNAKNSLYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RPEDTAVYHCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 10 of ‘954 RESULT 8 US-19-148-954-10 Sequence 10, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 10 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKDREWVASISRSGDTYYEDSVKGRFTISRDNAKNSVYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RPEDTAVYYCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 137, 138, and 139 with SEQ ID NO: 15 of ‘954 RESULT 9 US-19-148-954-15 Sequence 15, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 15 LENGTH: 123 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..123 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 85.5%; Score 148.7; Length 123; Best Local Similarity 39.1%; Matches 34; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 GRTFADAAWG---------------ISRSGDT---------------------------- 17 |||||||||| ||||||| Db 26 GRTFADAAWGWFRQVPGKGLEWVASISRSGDTYYEDSVKGRFTISRDNAKNSVYLQMNSL 85 Qy 18 ----------AARNSGAPSSIVIAYEY 34 ||||||||||||||||| Db 86 RPEDTAVYHCAARNSGAPSSIVIAYEY 112 Alignment of SEQ ID NOs: 118 with SEQ ID NO: 2 of ‘954 ALIGNMENT: Query Match 100.0%; Score 646; Length 123; Best Local Similarity 100.0%; Matches 123; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 QVQLVESGGGLVQAGGSLRLTCAASGRTFADAAWGWFRQVPGRDREWVASISRSGDTYYE 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 QVQLVESGGGLVQAGGSLRLTCAASGRTFADAAWGWFRQVPGRDREWVASISRSGDTYYE 60 Qy 61 DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYHCAARNSGAPSSIVIAYEYWGQGTQVT 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 DSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYHCAARNSGAPSSIVIAYEYWGQGTQVT 120 Qy 121 VSS 123 ||| Db 121 VSS 123 Alignment of SEQ ID NOs:23, 198, and 25 with SEQ ID NO: 22 of ‘954 US-19-148-954-22 Sequence 22, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 22 LENGTH: 216 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..216 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 83.2%; Score 121.4; Length 216; Best Local Similarity 36.1%; Matches 26; Conservative 0; Mismatches 0; Indels 46; Gaps 2; Qy 1 DYYMH--------------RIDPEDAETKYAPKFQG------------------------ 22 ||||| ||||||||||||||||| Db 31 DYYMHWVQQAPGKGLEWIGRIDPEDAETKYAPKFQGRVTITADTSTNTAYMELSSLRSED 90 Qy 23 --------GLAY 26 |||| Db 91 TAVYYCDRGLAY 102 Alignment of SEQ ID NOs:23, 198, and 25 with SEQ ID NO: 28 of ‘954 RESULT 5 US-19-148-954-28 Sequence 28, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 28 LENGTH: 587 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..587 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 83.2%; Score 121.4; Length 587; Best Local Similarity 36.1%; Matches 26; Conservative 0; Mismatches 0; Indels 46; Gaps 2; Qy 1 DYYMH--------------RIDPEDAETKYAPKFQG------------------------ 22 ||||| ||||||||||||||||| Db 402 DYYMHWVQQAPGKGLEWIGRIDPEDAETKYAPKFQGRVTITADTSTNTAYMELSSLRSED 461 Qy 23 --------GLAY 26 |||| Db 462 TAVYYCDRGLAY 473 Alignment of SEQ ID NOs:26, 27, and 28with SEQ ID NO: 23 of ‘954 RESULT 14 US-19-148-954-23 Sequence 23, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 23 LENGTH: 215 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..215 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 82.7%; Score 118.3; Length 215; Best Local Similarity 37.3%; Matches 28; Conservative 0; Mismatches 0; Indels 47; Gaps 2; Qy 1 SASSSVSSSYL---------------YSTSNLAS-------------------------- 19 ||||||||||| |||||||| Db 24 SASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIPARFSGSGSGTDFTLTISSLEPED 83 Qy 20 ------HQWSSYPYT 28 ||||||||| Db 84 FAVYYCHQWSSYPYT 98 Alignment of SEQ ID NOs: 26, 27, and 28 with SEQ ID NO: 25 of ‘954 RESULT 15 US-19-148-954-25 Sequence 25, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 25 LENGTH: 215 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..215 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 82.7%; Score 118.3; Length 215; Best Local Similarity 37.3%; Matches 28; Conservative 0; Mismatches 0; Indels 47; Gaps 2; Qy 1 SASSSVSSSYL---------------YSTSNLAS-------------------------- 19 ||||||||||| |||||||| Db 24 SASSSVSSSYLYWYQQKPGQAPKLLIYSTSNLASGIPARFSGSGSGTDYTLTISSLEPED 83 Qy 20 ------HQWSSYPYT 28 ||||||||| Db 84 FAVYYCHQWSSYPYT 98 Alignment of SEQ ID NO: 159 with SEQ ID NO: 22 of ‘954 US-19-148-954-22 Sequence 22, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 22 LENGTH: 216 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..216 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 98.5%; Score 588; Length 216; Best Local Similarity 98.2%; Matches 111; Conservative 1; Mismatches 1; Indels 0; Gaps 0; Qy 1 EVQLVQSGAEVKKPGATVKISCKVSGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 ||||||||||||||||||||||| |||||||||||||||||||||||||||||||||||| Db 1 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 Qy 61 APKFQGRVTITADTSTDTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 ||||||||||||||||:|||||||||||||||||||||||||||||||||||| Db 61 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 Alignment of SEQ ID NO: 159 with SEQ ID NO: 28 of ‘954 RESULT 6 US-19-148-954-28 Sequence 28, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 28 LENGTH: 587 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..587 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 98.5%; Score 588; Length 587; Best Local Similarity 98.2%; Matches 111; Conservative 1; Mismatches 1; Indels 0; Gaps 0; Qy 1 EVQLVQSGAEVKKPGATVKISCKVSGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 ||||||||||||||||||||||| |||||||||||||||||||||||||||||||||||| Db 372 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 431 Qy 61 APKFQGRVTITADTSTDTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 ||||||||||||||||:|||||||||||||||||||||||||||||||||||| Db 432 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 484 Alignment of SEQ ID NO: 160 with SEQ ID NO: 23 of ‘954 US-19-148-954-23 Sequence 23, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 23 LENGTH: 215 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..215 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 99.3%; Score 565; Length 215; Best Local Similarity 99.1%; Matches 107; Conservative 1; Mismatches 0; Indels 0; Gaps 0; Qy 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIP 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIP 60 Qy 61 ARFSGSGSGTDYTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108 |||||||||||:|||||||||||||||||||||||||||||||||||| Db 61 ARFSGSGSGTDFTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108 Alignment of SEQ ID NO: 160 with SEQ ID NO: 25 of ‘954 RESULT 5 US-19-148-954-25 Sequence 25, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 25 LENGTH: 215 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..215 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 97.7%; Score 556; Length 215; Best Local Similarity 99.1%; Matches 107; Conservative 0; Mismatches 1; Indels 0; Gaps 0; Qy 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIP 60 ||||||||||||||||||||||||||||||||||||||||||||||| |||||||||||| Db 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLLIYSTSNLASGIP 60 Qy 61 ARFSGSGSGTDYTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108 |||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ARFSGSGSGTDYTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108 Alignment of SEQ ID NO: 9 with SEQ ID NO: 22 of ‘954 US-19-148-954-22 Sequence 22, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 22 LENGTH: 216 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..216 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 100.0%; Score 597; Length 216; Best Local Similarity 100.0%; Matches 113; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 Qy 61 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 ||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 Alignment of SEQ ID NO: 9 with SEQ ID NO: 28 of ‘954 RESULT 3 US-19-148-954-28 Sequence 28, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 28 LENGTH: 587 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..587 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 100.0%; Score 597; Length 587; Best Local Similarity 100.0%; Matches 113; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 372 EVQLVQSGAEVKKPGATVKISCKASGFNIKDYYMHWVQQAPGKGLEWIGRIDPEDAETKY 431 Qy 61 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 113 ||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 432 APKFQGRVTITADTSTNTAYMELSSLRSEDTAVYYCDRGLAYWGQGTLVTVSS 484 Alignment of SEQ ID NO: 10 with SEQ ID NO: 23 of ‘954 US-19-148-954-23 Sequence 23, US/19148954 GENERAL INFORMATION APPLICANT: ELPISCIENCE (SUZHOU) BIOPHARMA, LTD. (en) TITLE OF INVENTION: ANTI-PDL1 SINGLE DOMAIN ANTIBODY, FUSION PROTEIN AND USE THEREOF (en) FILE REFERENCE: DCF231574WO CURRENT APPLICATION NUMBER: US/19/148,954 CURRENT FILING DATE: 2025-07-17 NUMBER OF SEQ ID NOS: 50 SEQ ID NO 23 LENGTH: 215 TYPE: PRT FEATURE: NAME/KEY: source LOCATION: 1..215 QUALIFIERS: mol_type = protein organism = synthetic construct Query Match 100.0%; Score 568; Length 215; Best Local Similarity 100.0%; Matches 108; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIP 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 EIVLTQSPATLSLSPGERATLSCSASSSVSSSYLYWYQQKPGQAPKLWIYSTSNLASGIP 60 Qy 61 ARFSGSGSGTDFTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108 |||||||||||||||||||||||||||||||||||||||||||||||| Db 61 ARFSGSGSGTDFTLTISSLEPEDFAVYYCHQWSSYPYTFGQGTKLEIK 108