Prosecution Insights
Last updated: April 18, 2026
Application No. 18/558,534

ANTI-CD40 ANTIBODY AND USE THEREOF

Non-Final OA §112§DP
Filed
Nov 02, 2023
Examiner
BORGEEST, CHRISTINA M
Art Unit
1675
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Sanyou Biopharmaceuticals Co. Ltd.
OA Round
1 (Non-Final)
55%
Grant Probability
Moderate
1-2
OA Rounds
3y 3m
To Grant
77%
With Interview

Examiner Intelligence

Grants 55% of resolved cases
55%
Career Allow Rate
392 granted / 709 resolved
-4.7% vs TC avg
Strong +22% interview lift
Without
With
+21.9%
Interview Lift
resolved cases with interview
Typical timeline
3y 3m
Avg Prosecution
37 currently pending
Career history
746
Total Applications
across all art units

Statute-Specific Performance

§101
10.0%
-30.0% vs TC avg
§103
24.3%
-15.7% vs TC avg
§102
18.6%
-21.4% vs TC avg
§112
29.4%
-10.6% vs TC avg
Black line = Tech Center average estimate • Based on career data from 709 resolved cases

Office Action

§112 §DP
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. Status of the Claims The preliminary amendment filed 11/02/2023 is acknowledged. Claims 2-20 are amended. No restriction is being imposed in this case. Claims 1-20 are under examination. Specification The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. See paragraphs [0062] and [0095]. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. Claim Rejections - 35 USC § 112 (b) 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 appl icant regards as his invention. Claims 7, 17 and 18 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 7 contains the trademark/trade name ForteBio ®. Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA), second paragraph. See Ex parte Simpson , 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name. In the present case, the trademark/trade name is used to identify/describe a kinetic binding assay and, accordingly, the identification/description is indefinite. Claim 17 recites the “[u] se of the anti-CD40 antibody or the antigen-binding fragment according to claim 1 … in the preparation of a drug for preventing or treating a tumor or an infectious disease in a subject ”, which is an attempt to claim a process without setting forth any steps involved in the process (see MPEP 2173.05(q) ) . Without any active, positive steps, it cannot be determined how this use is actually practiced. Further, it is not clear from the wording whether Applicant intends to claim a method of preparing a medicament or a method of treating/preventing. Claim 18, which depends from claim 17, also recites “the use”. The claims must particularly point out and distinctly define the metes and bounds of the subject matter that will be protected by the patent grant (see MPEP 2171). This issue could be addressed by amending the claim s t o clarif y whether the method is one of making a medicament or treating/preventing and adding active steps, for example, a step of administering the CD40 antibody or immunoconjugate . For the purpose of examination, the claims are interpreted as encompassing a method of treatment. Claim Rejections - 35 USC § 112(a) 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. Scope of Enablement Claims 1, 2 and 4 -20 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA), first paragraph, because the specification, while being enabling for an anti-CD40 antibody comprising a light chain variable regio n and a heavy chain variable region, wherein the light chain complementarity determining regions (LCDRs) and heavy chain complementarity determining regions (HCDRs) comprise: LCDR1 comprising SEQ ID NO: 1; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comp rising SEQ ID NO: 3; and HCDR1 comprising SEQ ID NO: 8; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 4 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 compri sing SEQ ID NO: 11 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 5 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 12 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 compris ing SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 13 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 6 and LCDR3 comprising an amino acid sequence of SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 14 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 10 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 15 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 16 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 17 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 and LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 18 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 2 ; LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 8 ; HCDR2 comprising SEQ ID NO: 9 and HCDR3 comprising SEQ ID NO: 19 ; LCDR1 comprising SEQ ID NO: 1 ; LCDR2 comprising SEQ ID NO: 7 ; LCDR3 comprising SEQ ID NO: 3 ; HCDR1 comprising SEQ ID NO: 20 ; HCDR2 comprising SEQ ID NO: 21 and H CDR3 comprising SEQ ID NO: 10 ; As well as methods of preparing said anti-CDR antibodies and treating lymphoma or colon cancer with said anti-CD40 antibodies , does not reasonably provide enablement for the claims as broadly recited . The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims. There are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue.” (See In re Wands , 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 Fed. Cir. 1988). These factors include, but are not limited to: (a) the breadth of the claims; (b) the nature of the invention; (c) the state of the prior art; (d) the level of one of ordinary skill; (e) the level of predictability in the art; (f) the amount of direction provided by the inventor; (g) the existence of working examples; and (h) the quantity of experimentation needed to make or use the invention based on the content of the disclosure. Claim 1 and its dependents encompass a mix and match approach to the LCDRs and HCDRs that amount to 512 possible combinations of light and heavy CDRs. In addition, claim 1 recites that each of the CDRs has “no more than 2 or no more than 1 amino acid change”, therefore, each CDR may have up to two amino acid substitutions. Since the CDRs comprise between 7-12 amino acid residues, this constitutes substituting between ~17-29% of the amino acids. Claim 4, which depends from claim 1, recites sequences of the light and full chain variable regions, but encompasses variations of up to 15% (i.e., 85% sequence identity) , which compounds the degree of variation encompassed by the CDRs. The claimed antibodies are described in the instant specification ( paragraph [0005] ): The present invention provides an agonistic anti-CD40 antibody with a high therapeutic index, wherein the antibody is capable of attenuating adverse effects of non-specific immune activation caused by CD40 activation while providing sufficient immune stimulation in a subject, and has one or more of the following properties: (1) binding to and activating CD40 (such as human CD40, cynomolgus monkey CD40 and mouse CD40) with a high affinity, for example, binding to CD40 with an affinity of about 10 -7 M to about 10 -10 M, as measured by ForteBio ® kinetic binding assay ; (2) enhancing a binding of CD40 to CD40L; (3) activating an antigen presenting cell, including, e.g., a dendritic cell (DC), a B cell, a monocyte and a macrophage, by binding to CD40 expressed on the antigen presenting cell; (4) inducing a CD40-expressing B cell to express CD95; (5) significantly enhancing a B cell-mediated immune response when a crosslinking effect is formed; and (6) barely or weakly enhancing a B cell-mediated immune response when a crosslinking effect is not formed. See also instant claim 7. Further, claims 17 and 18 recite the function preventing or treating a tumor or an infectious disease. In summary, the claims encompass anti-CD40 antibodies that can vary up to ~ 30% from the recited sequences , while disclosing only 12 anti-CD40 antibodies (see Table 6 at paragraph [0259] of the instant specification). The state of the art teaches antibody variable regions are composed of a heavy and light chain, each involved in providing for binding specificity. P redicting antibody amino acid substitution s while maintaining functionality i s complex. The art teaches that small changes in the amino acid structure of the CDRs can have larg e effects on activity. For instance, Piche-Nicholas et a l. ( MAbs . 2018; 10: 81-94. doi : 10.1080/19420862.2017.1389355) teach that the “binding affinity of IgG Molecules… to FcRn that differed by only a few amino acid residues in CDRs revealed that small changes in CDRs, as minute as one amino acid residue change, could alter affinity to FcRn up to 79-fold.” See p. 89, right column, last paragraph of Piche-Nicholas et al. In the instant case, how ever , the claims allow for swapping heavy and light chains for a total of 512 combinations in addition to a diversion from the recited CDRs by ~17-29% . Claim 4 compounds this because it recites up to 15% diversion from the recited heavy and light chains. Townsend et al. ( Frontiers in Immunology, 7, 388 2016 ) teach “[v] ariability in the antigen binding site is achieved by V(D)J recombination via heavy and light chain pairing ” , with the “ most diverse ” regions being the 6 CDR regions in the heavy and light chain. While the heavy chain is the most diverse, light chains are also important for binding specificity of antibodies, swapping light chains can “ change the antigen specificity of the antibody ” (see paragraph bridging pages 1-2). Furthermore, the light chain repertoire is extremely diverse being encoded by kappa and lambda gene segments, each with different V and J genes (see Townsend, p. 2, left column, 1 st two paragraphs; p. 4, right column, 1 st paragraph). Furthermore, the diversity of the immunoglobulin repertoire is mediated in part by different combinations of heavy and light chain V regions that pair to form a unique antibody binding site. See, for example, Rabia et al. ( Biochem . Engin . J. 137, 365-374, 2018), which teaches that “ the maximal chemical diversity of antibody CD Rs is unimaginably large …[ and ] it is extremely challenging to define the sequence determinant of antibody specificity ” (see p . 368 left column, 4 th paragraph ). Thus, the screening all of the possible anti-CD40 antibody variants for the recited function s, including preventing and treating tumors or infectious disease would require an undue amount of experimentation. Claim 17 recites preventing a tumor or an infectious disease. The specification discloses how to prepare the antiCD40 antibody of the invention along with variants thereto (see Example 1, pages 60-65 , Example 4, pages 70-74 ). Further, the specification discloses the antibody “ exhibited the enhanced CD40 binding activity to CD40L ” in a cell-based assay , activated immature dendritic cells and induced CD95 activity in human lymphoma cells that express CD40 on their cell surface (see Example 2, pages 65- 69; especially paragraphs [0216]; [0220]; [0222]). In addition, the specification discloses that the anti-CD40 antibody of the invention inhibited tumor growth in a mouse lymphoma model, inhibited tumors in a mouse model for colon adenocarcinoma (see Example 3, pages 69- 70 , especially paragraphs [0225]; [00229]). The variants bound to CD40 antigen, with one (C8-6) binding better than the parent antibody, induced CD95 activity in lymphoma cells and were weak agonists of CD40, potentially making them less hepatotoxic (see Example 4, pages 70-82; especially paragraphs [0242]; [0244]; [0246] ; [0256] ). The guidance in the instant specification present evidence that the parent anti-CD40 antibody of the invention may ameliorate lymphoma and colon cancer , but there is no guidance suggesting it could prevent or treat any tumor or infectious disease prior to disease onset . The evidence in the specification is not commensurate with the scope of the claimed invention . Due to the large quantity of experimentation necessary to test the variant antibodies for the ability to prevent/treat any cancer or infectious disease , the lack of direction/guidance presented in the specification regarding the same and the absence of working examples directed to the same , the complex nature of the invention, the unpredictability of the effects of mutation on antibody binding and function, and the breadth of the claims which fail to recite limitations on the antibodies or the patient population , undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope. Written Description Claim s 1, 2 and 4-20 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. This is a written description rejection . In deciding whether the application complies with the written description requirement of 35 USC 112(a) or 35 USC 112 (pre-AIA), first paragraph, it is necessary to understand what Applicant has possession of and what Applicant is claiming . Claim 1 and its dependents encompass a mix and match approach to the LCDRs and HCDRs that amount to 512 possible combinations of light and heavy chain CDRs. In addition, claim 1 allows for up to two amino acid substitutions in each CDR and s ince the CDRs comprise between 7-12 amino acid residues, this constitutes substituting between ~17-29% of the amino acids. Claim 4, which depends from claim 1, recites sequences of the light and full chain variable regions, but encompasses variations of up to 15% (i.e., 85% sequence identity), which compounds the degree of variation encompassed by the CDRs. Claim 7 recites the antibodies have the following functions: (1) binding to CD40 with an affinity of about 10 -7 M to about 10 -10 M, as measured by ForteBio ® kinetic binding assay and activating CD40 ; (2) enhancing a binding of CD40 to CD40L; (3) activating an antigen presenting cell, including, e.g., a dendritic cell (DC), a B cell, a monocyte and a macrophage, by binding to CD40 expressed on the antigen presenting cell; (4) inducing a CD40-expressing B cell to express CD95; (5) significantly enhancing a B cell-mediated immune response when a crosslinking effect is formed; and (6) barely or weakly enhancing a B cell-mediated immune response when a crosslinking effect is not formed. Further, claims 17 and 18 recite the function preventing or treating a tumor or an infectious disease. In summary, the claims encompass a vast genus of anti-CD40 antibodies that can vary up to ~ 30% from the recited sequences . To provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. The MPEP 2163(A) states “‘[a]n invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function.’” For inventions in emerging and unpredictable technologies, or for inventions characterized by factors not reasonably predictable which are known to one of ordinary skill in the art, more evidence is required to show possession. (See MPEP 2163(II)(A)(3)(a)( i )). From the specification , it is clear that Applicant has possession of 12 variant anti-CD40 antibodies and their encoding nucleotide sequences (see Tables 1-3 at paragraph [0186], pages 53-60). It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. The prior art teaches that small changes in the amino acid structure of the CDRs can have larg e effects on activity. For instance, Piche-Nicholas et a l. ( MAbs . 2018; 10: 81-94. doi : 10.1080/19420862.2017.1389355) teaches that the “binding affinity of IgG Molecules… to FcRn that differed by only a few amino acid residues in CDRs revealed that small changes in CDRs, as minute as one amino acid residue change, could alter affinity to FcRn up to 79-fold.” See p. 89, right column, last paragraph of Piche-Nicholas et al. In the instant case, however, very large changes in amino acid sequence of the CDRs is encompassed by the scope of the claims. Townsend et al. ( Frontiers in Immunology, 7, 388 2016 ) teach “[v] ariability in the antigen binding site is achieved by V(D)J recombination via heavy and light chain pairing ” , with the “ most diverse ” regions being the 6 CDR regions in the heavy and light chain. While the heavy chain is the most diverse, light chains are also important for binding specificity of antibodies, swapping light chains can “ change the antigen specificity of the antibody ” (see paragraph bridging pages 1-2). Furthermore, the light chain repertoire is extremely diverse being encoded by kappa and lambda gene segments, each with different V and J genes (see Townsend, p. 2, left column, 1 st two paragraphs; p. 4, right column, 1 st paragraph). Furthermore, the diversity of the immunoglobulin repertoire is mediated in part by different combinations of heavy and light chain V regions that pair to form a unique antibody binding site. See, for example, Rabia et al. ( Biochem . Engin . J. 137, 365-374, 2018), which teaches that “ the maximal chemical diversity of antibody CD Rs is unimaginably large …[ and ] it is extremely challenging to define the sequence determinant of antibody specificity ” (see p . 368 left column, 4 th paragraph ). In summary, given that the art is not reasonably predictable , the 12 species disclosed in the instant specification are not representative of the over 500 possible antibodies in addition to substitutions of between ~17-29% of the variable regions, including CDRs. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus. Vas-Cath Inc. v. Mahurkar , 19USPQ2d 1111, clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention . The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed. ” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). With the exception of the 12 antibodies disclosed at pages 53-56 of the instant specification , the skilled artisan cannot envision the detailed chemical structure of the encompassed polypeptides, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel , 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd. , 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird , 30 USPQ2d 1481 at 1483. In Fiddes , claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Therefore, only the 12 antibodies disclosed at pages 53-60 of the instant specification, but not the full breadth of the claim meets the written description provision of 35 U.S.C. §112, first paragraph. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115). 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 . Claims 1-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of copending Application No. 18/715,119 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of the reference application encompass anti-CD40 antibodies that share 100% sequence identity to a light chain comprising LCDRs 1-3 set forth in SEQ ID NOs: 1-3 and to heavy chains comprising HCDRs that share 100% sequence identity to SEQ ID NOs: 8-10; 8, 9 and 11; 8, 9 and 15; and 8, 9 and 19 and kits thereto. The claims of the reference application also recite the polynucleotides encoding the antibodies, vectors comprising said polynucleotides and host cells comprising said vectors as well as methods of producing the antibodies, use of the medicament in preventing or treating cancer and methods of treatment. The difference between the instant claims and those of the reference application are as follows. The claims of the reference application recite that the anti-CD40 antibody is part of a bispecific antibodies against CD40 and CLDN18.2. Nevertheless, the claims of the reference application anticipate the structure of the instantly claimed antibodies, as well as the methods of use, thus, when considered in light of the reference application claims, the instant claims are patentably distinct. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT CHRISTINA M BORGEEST whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-4482 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 9-5:30 EDT . 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, FILLIN "SPE Name?" \* MERGEFORMAT Jeffrey Stucker can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 5712720911 . 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. /CHRISTINA M BORGEEST/ Primary Examiner, Art Unit 1675
Read full office action

Prosecution Timeline

Nov 02, 2023
Application Filed
Apr 01, 2026
Non-Final Rejection — §112, §DP (current)

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12601744
BIOMARKERS AND METHODS FOR PREDICTING PRETERM BIRTH
2y 5m to grant Granted Apr 14, 2026
Patent 12599323
METHODS AND SYSTEMS FOR TREATING OR PREVENTING PREGNANCY-RELATED HYPERTENSIVE DISORDERS COMPRISING ANTI-sENG AND ANTI-sFLT-1 ANTIBODIES
2y 5m to grant Granted Apr 14, 2026
Patent 12599644
TREATMENT OF CORONAVIRUS INFECTION WITH FTL3 RECEPTOR INTERCTION LECTION (FRIL)
2y 5m to grant Granted Apr 14, 2026
Patent 12589161
PEGylated synthetic KL4 peptide, Compositions and Methods Thereof
2y 5m to grant Granted Mar 31, 2026
Patent 12578343
Novel Selective ACKR3 Modulators and Uses Thereof
2y 5m to grant Granted Mar 17, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

AI Strategy Recommendation

Get an AI-powered prosecution strategy using examiner precedents, rejection analysis, and claim mapping.
Powered by AI — typically takes 5-10 seconds

Prosecution Projections

1-2
Expected OA Rounds
55%
Grant Probability
77%
With Interview (+21.9%)
3y 3m
Median Time to Grant
Low
PTA Risk
Based on 709 resolved cases by this examiner. Grant probability derived from career allow rate.

Sign in with your work email

Enter your email to receive a magic link. No password needed.

Personal email addresses (Gmail, Yahoo, etc.) are not accepted.

Free tier: 3 strategy analyses per month