CTNF 17/793,355 CTNF 81569 Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. DETAILED ACTION Status of Application/Election/Restrictions 08-25-01 AIA Applicant’s election without traverse of Group I (claims 1-2,4,7-15, 25 and 27-29), SEQ ID NO:1 as sequence of amyloid-reactive peptide, SEQ ID NO:42 as sequence of cytoplastic domain, SEQ ID NO: 43 as sequence of chimeric receptor in the reply filed on August 11, 2025 is acknowledged. Claims 3, 5-6,16-24 and 26 are canceled. Claims 9-10 are amended. Claims 27-29 are newly added. Claims 1-2, 4, 7-15, 25 and new claims 27-29 are pending in this application. Election was made without traverse in the reply filed on August 11, 2025. 3. Claims 1-2, 4, 7-15, 25 and 27-29 are under examination with respect to SEQ ID NOs: 1, 42 and 43 in this office action. Priority 02-09 AIA 4. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, or 365(c) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date under 35 U.S.C. 119(e) or under 35 U.S.C. 120 as follows: The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of the first paragraph of 35 U.S.C. 112. See Transco Products, Inc. v. Performance Contracting, Inc. , 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994). The disclosure of the prior-filed application, provisional Application No. 62/962763, fails to provide adequate support or enablement in the manner provided by the first paragraph of 35 U.S.C. 112 for one or more claims of this application. The instant application claims a chimeric receptor comprising an extracellular domain comprising an amyloid-binding region; a transmembrane domain and a cytoplasmic domain comprising a signal domain, wherein the extracellular domain comprises an antibody or antigen-binding fragment thereof comprising SEQ ID NOs:21-26 for CDRH1-3 and CDRL1-3 respectively, which is not presented in the provisional Application No. 62/962763, filed on January 17, 2020. The antibody comprising specific SEQ ID NOs: for CDRH1-3 and CDRL1-3 was only disclosed in PCT/US2021/013727 filed on January 15, 2021 (see paragraphs [0011] of the specification). Therefore, the priority for the claimed chimeric receptor comprising an antibody having specific sequences of recited SEQ ID NOs: for CDRH1-3 and CDRL1-3 of the instant application is January 15, 2021 . Improper Markush Grouping 5. Claims 9, 13, 15, 27 and 29 are rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch , 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi , 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use . A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 706.03(y). The Markush grouping of SEQ ID NOs: for amyloid-reactive peptide recited in claims 9, 27 and 29, the Markush grouping of SEQ ID NOs: for cytoplasmic domain recited in claim 13 and the Markush grouping of SEQ ID NOs: for chimeric receptor recited in claim 15 are improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: The recited alternative species do not share a single structural similarity, as each SEQ ID NO: for amyloid-reactive peptide, each SEQ ID NO: for cytoplasmic domain and each SEQ ID NO: for chimeric receptor has a different chemical structure in that it consists of a different amino acid sequence. Each SEQ ID NO: of polypeptide has a different biological activity in that it has a different biological activity and effect as admitted by Applicant (see p. of the specification). Thus, the different SEQ ID NOs: for amyloid-reactive peptide, the different SEQ ID NOs: for cytoplasmic domain and the different SEQ ID NOs: for chimeric receptor do not share a single structural similarity or biological activity. To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use. Claim Rejections - 35 USC § 112 07-30-02 AIA 6. 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. 07-34-01 Claim 10 is 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. 07-34-05 AIA Claim 10 recites the limitation " the antibody CH2 domain… " in line 2 of the claim . There is insufficient antecedent basis for this limitation in the claim. Claim Rejections - 35 USC § 112 07-30-01 AIA 7. 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. 07-31-01 AIA Claim s 1-2, 4, 7-15, 25 and 27-29 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. To provide adequate written description and 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. Claims 1-2, 4, 7 and 12-14 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprises an amyloid binding region that is an antibody or antigen binding fragment thereof including an antibody comprising SEQ ID NOs: 21-26 for CDRH1-3 and CDRL1-3 respectively. Claims 1, 8-15, 25 and 27 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprising an amyloid binding region that is an amyloid-reactive peptide including an amyloid reactive peptide comprising the sequence set forth in SEQ ID NOs: 1-18. Claims 28-29 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprising an amyloid-reactive peptide and further comprising a globular domain including an immunoglobulin domain, and wherein the cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage. The claims encompass a genus of chimeric receptor comprising from N-terminal to C-terminal direction: a genus of extracellular domain comprising a genus of amyloid binding region, a genus of transmembrane domain, a genus of cytoplasmic domain and a genus of antibody or antigen-binding fragment thereof and a genus of amyloid-reactive peptide. Claims 2 and 6 encompass a genus of structurally and functionally undefined antibody or antigen-binding fragment thereof. Claims 8,10 and 28 encompass a genus of structurally and functionally undefined amyloid-reactive peptide. Claim 12 encompasses a genus of structurally and functionally undefined cytoplasmic domain or cytoplasmic domain I, cytoplasmic domain II or functional fragment thereof. Claim 28 encompasses a genus of cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and a genus of a globular domain including an immunoglobulin domain. Applicant has not disclosed sufficient species for the broad genus of chimeric receptor, the broad genus of extracellular domain, the broad genus of amyloid binding region, the broad genus of transmembrane domain, the broad genus of cytoplasmic domain, the broad genus of antibody or antigen binding fragment thereof, the broad genus of amyloid-reactive peptide, the broad genus of cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and a genus of a globular domain including an immunoglobulin domain. The specification provides insufficient description to demonstrate that Applicant is in possession of the claimed genera of chimeric receptor, extracellular domain, amyloid binding region, transmembrane domain, cytoplasmic domain, antibody or antigen binding fragment thereof, amyloid-reactive peptide, cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and globular domain including an immunoglobulin domain. In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant is in possession of and what Applicant is claiming. M.P.E.P. § 2163 instructs: An 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. . . . An applicant may show possession of an invention by disclosure of drawings or structural chemical formulas that are sufficiently detailed to show that applicant was in possession of the claimed invention as a whole. . . . An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics.” This standard has not been met in this case. The specification only showed reduction in hepatic amyloid load based on 123 I-SAP scintigraphy after infusion of monoclonal antibody or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I -m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 binding human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B). The specification describes sequences of the CDRH1-3 and CDRL1-3 of m11-1F4 antibody, the VH and VL of scFv of m11-1F4 antibody shown in Tables B and 1, sequences of amyloid-binding peptides shown in Table A, sequences of amyloid-binding region shown in Tables 2-3 and the concept and sequences of chimeric antigen receptor (CAR) and chimeric antigen-receptor-phagocytic (CAR-P) in Table C. While the specification describes a hypothetic schematic drawing of the claimed chimeric receptor in figure 1 and prophetic examples of full-length chimeric receptor constructs as shown in Table C (p 45-46, Table C) and the structures of prophetic 11-1F4CARtandem in Table 1, p5+14CARFc e R in Table 2 and CAR-P constructs in Table 3, the specification provides insufficient description to demonstrate that Applicant is in possession of the prophetic examples of 11-1F4 CAR tandem , p5+14 CAR FcR shown in Tables 1-3 or the claimed genus of chimeric receptor because the CAR exerts effects through both target binding and intracellular signaling in view of Kim et al. (JCI, Insight, 2014; 9:e175015). There is no data to support that the prophetic examples of 11-1F4 CAR tandem , p5+14 CAR FcR shown in Tables 1-3 or the claimed genus of chimeric receptor can target to amyloid beta or activate macrophages in vitro or in vivo. There is no structural and functional relationship or correlation between the prophetic examples of 11-1F4 CAR tandem , p5+14 CAR FcR shown in Tables 1-3 and the 124I -m11-1F4 monoclonal antibody or p5+14 in reducing hepatic amyloid load or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I -m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 binding human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B). There is also no structural and functional relationship or correlation between the claimed genus of chimeric receptor and the 124I -m11-1F4 monoclonal antibody or p5+14 in reducing hepatic amyloid load or biodistribution of AL amyloid (light chain-associated amyloid) based on 124I -m11-1F4 monoclonal antibody (Example 1, Figures 2 and 4A-4D) or p5+14 binding human AL amyloid in tissue and PET/CT imaging in patients with AL amyloidosis (Example 1, Figures 5A-B). The specification provides no information or data for a species of the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed chimeric receptors to demonstrate that the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor are capable of performing the same activity as 124I -m11-1F4 monoclonal antibody or p5+14 shown in Example 1 and figures 4-5. The specification provides no structural and functional relationship or correlation between the claimed genus of chimeric receptor or a hypothetic schematic drawing of figure 1/the structures of prophetic antibody-based CAR-P/CAR,11-1F4CARtandem/prophetic peptide-based CAR-P/CAR, p5+14CARFc e R shown in Tables 1- 3 and the 124I -m11-1F4 monoclonal antibody shown in Example 1, Figures 2 and 4A-4D or p5+14 binding in patients with AL amyloidosis shown in Example 1, Figures 5A-B. There is no identification of any particular portion of the structure that must be conserved. The instant specification fails to provide sufficient descriptive information, such as definitive structural or functional features of the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor. There is no description of the conserved regions which are critical to the function of the genus claimed. There is no description of the sites at which variability may be tolerated and there is no information regarding the relation of structure of the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor to the function of 124I -m11-1F4 monoclonal antibody or p5+14 as shown in Example 1 and figures 4-5. Furthermore, the prior art does not provide compensatory structural or correlative teachings sufficient to enable one of skill to identify whether the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor might be capable of performing the same activity as 124I -m11-1F4 monoclonal antibody or p5+14 shown in Example 1 and figures 4-5. Since the common characteristics/features of other chimeric receptors or the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor are unknown, a skilled artisan cannot envision the functional correlations of the prophetic examples of full length chimeric receptor constructs shown in Table 3 or Table C or the claimed genus of chimeric receptor with the claimed invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the genus of chimeric receptor, extracellular domain, amyloid binding region, transmembrane domain, cytoplasmic domain, antibody or antigen binding fragment thereof, amyloid-reactive peptide, cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and globular domain including an immunoglobulin domain. Based on MPEP § 2161.01 and §2163, “to satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116”. Vas-Cath Inc. v. Mahurkar , 19USPQ2d 1111, clearly states “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). As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of chimeric receptor, extracellular domain, amyloid binding region, transmembrane domain, cytoplasmic domain, antibody or antigen binding fragment thereof, amyloid-reactive peptide, cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage and globular domain including an immunoglobulin domain; 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. Therefore, the claimed chimeric receptor has not met 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). Applicant is directed to the Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement. See MPEP § 2161.01 and 2163 . 07-06 AIA 15-10-15 8. In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. Claim Rejections - 35 USC § 102 07-07-aia AIA 07-07 9. 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 – 07-08-aia AIA (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. 07-12-aia AIA (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. 07-15 AIA Claim s 1-2, 7 and 12-14 are rejected under 35 U.S.C. 102( a)(1) & (a)(2 ) as being anticipated by Rosenthal (US2019/0233496, published Aug 1, 2019, priority Mar 23, 2016, as in IDS) . Claims 1-2, 7 and 12-14 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprises an amyloid binding region that is an antibody or antigen binding fragment thereof including an antibody comprising SEQ ID NOs: 21-26 for CDRH1-3 and CDRL1-3 respectively. Rosenthal (US2019/0233496) teaches a chimeric receptor having the structures described in Figures 1-4,8A,9A, 13A, 15A ( PNG media_image1.png 156 744 media_image1.png Greyscale ), wherein the chimeric receptor comprises: (1) an extracellular ligand-binding domain, wherein the ligand is an agent associated with a neurological disease, disorder, or injury; (2) a transmembrane domain; and (3) a signaling domain, wherein binding of the ligand to the chimeric receptor expressed in an immune cell activates the signaling domain, and the activated signaling domain induces and/or enhances (i) cell survival of the immune cell, (ii) proliferation of the immune cell, (iii) migration of the immune cell, (iv) functionality of the immune cell, or any combination thereof including macrophages (see figure 1A; [0008]-[0009];[0026]; [0085]-[0102]; [0100]; [0105]-[0107]; [0111]-[0112]; [0164]-[0166]; [0238]; Examples 26-29, claims 1-4, 6, 8-9, 11, 13, 15, 17-24, 27, 29-33, 35, 37-42, 44, 46-48, 50-55, 62-70, 74, 87). Rosenthal teaches that the extracellular ligand binding domain of the chimeric receptor includes an antibody, a single-domain antibody, humanized antibody or scFv, anti-Abeta scFv as in claim 2 ([0087]-[0088]; [0220]) and that the ligand includes amyloid beta as in claim 2 ([0009]; [0111]; [0164]-[0166]; [0238], Examples 26-29), and the chimeric receptor includes further comprising a flexible linker between the transmembrane domain and the signaling domain (see [0085]-[0112]), and wherein the cytoplasmic domain comprising a signal domain of receptor when activated activates a macrophage (see [0238], Example 26-29), which meet the limitations as shown in instant claims 1-2, 7 and 12-14, and the schematic chimeric receptor shown in the structures of Figures 1 and 3 in instant application (Figures 1 and 3 of the instant application). Rosenthal teaches that the antibody or antigen-binding fragment is humanized as in claim 7 (see [0220]), wherein the cytoplasmic domain includes Fc e R, which comprises a cytoplasmic domain I or II or functional fragment thereof as in claims 12-13 (see [0097]; [0085]-[0112], claim 9 and 11), and wherein binding of an amyloid to the extracellular domain activates the cytoplasmic domain of the chimeric receptor as in claim 14 (see [0085]-[0112]; [0238], Examples 26-29). Thus, claims 1-2, 7 and 12-14 are anticipated by Rosenthal (US2019/0233496) . Claim Rejections - 35 USC § 103 07-20-aia AIA 10. 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 of this title, 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. 07-23-aia AIA The factual inquiries set forth in Graham v. John Deere Co. , 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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. 07-20-02-aia AIA 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. 07-21-aia AIA Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Rosenthal (US2019/0233496) in view of Lentzsch (US20190038745, published on Feb 7, 2019, priority Aug 1, 2017, as in IDS) . Rosenthal is set forth above but does not teach SEQ ID NOs: 21-26 for CDRH1-3 and CDRL1-3 for an anti-Amyloid beta antibody in claim 4. While Rosenthal does not teach that the anti-Amyloid beta antibody comprises SEQ ID NOs: 21-26 for CDRH1-3 and CDRL1-3 recited in claim 4, Lentzsch teaches this limitation and provides motivation and an expectation of success because Lentzsch teaches a humanized or chimeric anti-amyloid fibril antibody, 11-1F4 antibody comprising a VH and a VL and wherein the VH comprises SEQ ID NO: 48 which comprises the sequences of instant SEQ ID NOs: 21-23 for CDRH1-3 and the VL comprises SEQ ID NO: 47 which comprises sequences of instant SEQ ID NOs: 24-26 for CDRL1-3 and the method of treating amyloid deposition diseases using the11-1F4 antibody (see the sequence alignment below; abstract; para. []). A person of ordinary skill in the art would have recognized that selecting and applying the known humanized or chimeric anti-amyloid fibril antibody, 11-1F4 antibody comprising the known CDRH1-3 and CDRL1-3 of SEQ ID NOs:21-26 respectively to the anti-Abeta antibody or scFv of the Rosenthal’s chimeric receptor would have yielded the predictable result of the claimed chimeric receptor comprising an extracellular domain comprising an antibody or antigen binding fragment having recited SEQ ID NOs:21-26 for CDRH1-3 and CDRL1-3 and resulted in an improved product. Using the known humanized or chimeric anti-amyloid fibril antibody, 11-1F4 antibody comprising the known CDRH1-3 and CDRL1-3 of SEQ ID NOs:21-26 respectively to the anti-Abeta antibody or scFv in the Rosenthal’s chimeric receptor would generate the claimed chimeric receptor and expand application of the Rosenthal’s chimeric receptor in pharmaceutical purposes, and would increase patient’s satisfaction with treatment of amyloid deposition diseases using an anti-Abeta antibody because the humanized or chimeric anti-amyloid fibril antibody, 11-1F4 antibody has been used for treatment of amyloid deposition diseases. Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known humanized or chimeric anti-amyloid fibril antibody, 11-1F4 antibody comprising the known CDRH1-3 and CDRL1-3 of SEQ ID NOs:21-26 respectively to the anti-Abeta antibody or scFv of the Rosenthal’s chimeric receptor, and yield the predictable result of the claimed chimeric receptor comprising an extracellular domain comprising an antibody or antigen binding fragment having recited SEQ ID NOs:21-26 for CDRH1-3 and CDRL1-3. SEQ ID NO:21-SEQ ID NO:22-SEQ ID NO:23 Sequence 48, US/16021168 Publication No. US20190038745A1 GENERAL INFORMATION APPLICANT: Trustees of Columbia University in the City of New York TITLE OF INVENTION: METHODS AND COMPOSITIONS FOR TREATMENT OF AMYLOID DEPOSITION TITLE OF INVENTION: DISEASES FILE REFERENCE: 8441-0009-1 CURRENT APPLICATION NUMBER: US/16/021,168 CURRENT FILING DATE: 2018-06-28 PRIOR APPLICATION NUMBER: US 62/538,821 PRIOR FILING DATE: 2017-08-01 PRIOR APPLICATION NUMBER: US 62/637,609 PRIOR FILING DATE: 2018-03-02 NUMBER OF SEQ ID NOS: 54 SEQ ID NO 48 LENGTH: 111 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: The sequence contains sequences from Homo sapiens and Mus Musculus Query Match 84.5%; Score 134.4; Length 111; Best Local Similarity 38.7%; Matches 29; Conservative 0; Mismatches 0; Indels 46; Gaps 2; Qy 1 GFSLSSYGVS--------------VIWGDGSTNYHPNLMS-------------------- 26 |||||||||| |||||||||||||||| Db 26 GFSLSSYGVSWVRQPPGKGLEWLGVIWGDGSTNYHPNLMSRLSISKDISKSQVLFKLNSL 85 Qy 27 ------------LDY 29 ||| Db 86 QTDDTATYYCVTLDY 100 SEQ ID NO:24-SEQ ID NO:25-SEQ ID NO:26 US-16-021-168-47 (NOTE: this sequence has 5 duplicates in the database searched) Sequence 47, US/16021168 Publication No. US20190038745A1 GENERAL INFORMATION APPLICANT: Trustees of Columbia University in the City of New York TITLE OF INVENTION: METHODS AND COMPOSITIONS FOR TREATMENT OF AMYLOID DEPOSITION TITLE OF INVENTION: DISEASES FILE REFERENCE: 8441-0009-1 CURRENT APPLICATION NUMBER: US/16/021,168 CURRENT FILING DATE: 2018-06-28 PRIOR APPLICATION NUMBER: US 62/538,821 PRIOR FILING DATE: 2017-08-01 PRIOR APPLICATION NUMBER: US 62/637,609 PRIOR FILING DATE: 2018-03-02 NUMBER OF SEQ ID NOS: 54 SEQ ID NO 47 LENGTH: 112 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: The sequence contains sequences from Homo sapiens and Mus musculus Query Match 85.4%; Score 144.3; Length 112; Best Local Similarity 40.5%; Matches 32; Conservative 0; Mismatches 0; Indels 47; Gaps 2; Qy 1 RSSQSLVHRNGNTYLH---------------KVSNRFS---------------------- 23 |||||||||||||||| ||||||| Db 24 RSSQSLVHRNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPRDFSGSGSGTDFTLKISRV 83 Qy 24 ----------FQTTYVPNT 32 ||||||||| Db 84 EAEDLGLYFCFQTTYVPNT 102 07-21-aia AIA 11. Claim s 8-11, 15, 25 and 27-29 are rejected under 35 U.S.C. 103 as being unpatentable over Rosenthal (US2019/0233496) in view of Wall et al. (US20160243230, published Aug 25, 2016, priority Aug 26,2014, as in IDS) and Elson et al. (US2017/0298129, published Oct 19, 2017, priority May 14, 2007, as in IDS) . Claims 8-11,15, 25 and 27 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprising an amyloid binding region that is an amyloid-reactive peptide including an amyloid reactive peptide comprising the sequence set forth in SEQ ID NOs: 1-18. Claims 28-29 are drawn to a chimeric receptor comprising from N-terminal to C-terminal direction: an extracellular domain comprising an amyloid binding region; a transmembrane domain; and a cytoplasmic domain comprising a singling domain, wherein the extracellular domain comprising an amyloid-reactive peptide and further comprising a globular domain including an immunoglobulin domain, and wherein the cytoplasmic domain comprising a signaling domain of a receptor when activated activating a macrophage. Rosenthal is set forth above but does not teach an amyloid-reactive peptide comprising the sequence of recited SEQ ID NOs: including SEQ ID NO: 1 recited in claims 8-9, 15, 25 and 27-29, or joined directly or indirectly via a spacer to the antibody CH2 domain or fragment thereof recited in claims 10-11. While Rosenthal does not teach that the extracellular domain comprises an amyloid-reactive peptide comprising the sequence of recited SEQ ID NOs: including SEQ ID NO: 1 as recited in claims 8-9, 15, 25 and 27-29, or joined directly or indirectly via a spacer to the antibody CH2 domain or fragment thereof recited in claims 10-11, Wall et al. (US20160243230) and Elson et al. (US2017/0298129) teach these limitations and provides motivation and an expectation of success. Wall teaches amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof, which comprises instant SEQ ID NO:1 and the method of treating amyloid deposition diseases using the amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof (see the sequence alignment; abstract; [0068]-[0069]; [0077]; [0102]; [0115]-[0139], tables 1-3, [0152];). Elson teaches a fusion protein comprising an interest of protein joined directly or indirectly via a spacer to the antibody CH2 domain or fragment thereof that comprises an amino acid sequence at least 85% identical to the amino acid sequence of SEQ ID NO:33 as recited in claims 10-11 (see SEQ ID NO:59; para. [0012]-[0015]; [0131]; claims 1-4, 8 and 21). A person of ordinary skill in the art would have recognized that selecting and applying the known amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof and the known antibody CH2 domain or fragment thereof that comprises an amino acid sequence at least 85% identical to the amino acid sequence of instant SEQ ID NO:33 to generate a fusion protein comprising the amyloid-reactive peptide joined via a spacer as disclosed by Wall and Elson to the Rosenthal’s chimeric receptor would have yielded the predictable result of the claimed chimeric receptor comprising an extracellular domain comprising an amyloid-reactive peptide comprising recited SEQ ID NOs: including SEQ ID NO:1, and wherein the amyloid-reactive peptide is linked directly or indirectly via a spacer to an antibody CH2 domain or fragment thereof comprising an amino acid sequence at least 85% identical to instant SEQ ID NO:33, and resulted in an improved product. Using the known amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof and the known antibody CH2 domain or fragment thereof to generate a fusion protein in the Rosenthal’s chimeric receptor would generate the claimed chimeric receptor and expand application of the Rosenthal’s chimeric receptor in pharmaceutical purposes, and would increase patient’s satisfaction with treatment of amyloid deposition diseases using an amyloid-reactive peptide including p5 or p5+14 and fusion peptides thereof because the amyloid-reactive peptide including p5 or p5+14 and fusion peptides thereof have been used for treatment of amyloid deposition diseases as taught by Wall and linking an antibody CH2 domain or fragment thereof comprising an amino acid sequence at least 85% identical to instant SEQ ID NO:33 via a spacer has been used for generation of a fusion protein as taught by Elson. Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to select and apply the known amyloid-reactive peptides including p5 or p5+14 and fusion peptides thereof and the known antibody CH2 domain or fragment thereof that comprises an amino acid sequence at least 85% identical to the amino acid sequence of instant SEQ ID NO:33 to generate a fusion protein comprising the amyloid-reactive peptide joined via a spacer as disclosed by Wall and Elson to the Rosenthal’s chimeric receptor, and yield the predictable result of the claimed chimeric receptor comprising an extracellular domain comprising an amyloid-reactive peptide comprising recited SEQ ID NOs: including SEQ ID NO:1, and wherein the amyloid-reactive peptide is linked directly or indirectly via a spacer to an antibody CH2 domain or fragment thereof comprising an amino acid sequence at least 85% identical to instant SEQ ID NO:33. SEQ ID NO:1 Sequence 1, US/15052772 Publication No. US20160243230A1 GENERAL INFORMATION APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION TITLE OF INVENTION: TARGETING IMMUNOTHERAPY FOR AMYLOIDOSIS FILE REFERENCE: 05820.P004U1 CURRENT APPLICATION NUMBER: US/15/052,772 CURRENT FILING DATE: 2016-02-24 PRIOR APPLICATION NUMBER: PCT/US2015/046523 PRIOR FILING DATE: 2015-08-24 PRIOR APPLICATION NUMBER: 62/041,888 PRIOR FILING DATE: 2014-08-26 NUMBER OF SEQ ID NOS: 56 SEQ ID NO 1 LENGTH: 26 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: Description of Artificial Sequence: Synthetic peptide FEATURE: OTHER INFORMATION: Peptide p5 Query Match 100.0%; Score 121; Length 26; Best Local Similarity 100.0%; Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26 |||||||||||||||||||||||||| Db 1 KAQKAQAKQAKQAQKAQKAQAKQAKQ 26 Double Patenting 08-33 AIA 12. 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. 08-35 AIA Claim s 1, 8-15, 25 and 27-29 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 1-57 of copending Application No. 19/107007 . Although the claims at issue are not identical, they are not patentably distinct from each other because the chimeric receptor recited in claims of Application No. 19/107007 (the ‘007 Application) anticipate the claimed chimeric receptor recited in the claims of the instant Application. Claims 1-57 of the ‘007 Application claim a chimeric receptor comprising from N-terminal to C-terminal direction: an amyloid-reactive peptide, a CH3 or a CH2 domain or fragment thereof, a transmembrane domain and a cytoplasmic domain comprising an intracellular signaling domain, an engineered cell comprising the chimeric receptor and a method for removing an amyloid deposit using the claimed chimeric receptor or engineered cell. The chimeric receptor recited in the claims of the ‘007 Applicant meets the limitations recited in instant claims 1, 8-15, 25 and 27-29 and thus anticipates instant claims. Therefore, claims 1, 8-15, 25 and 27-29 of the instant Application are not patentably distinct from claims 1-57 of the ‘007 Application because c1, 8-15, 25 and 27-29 of the instant Application are anticipated by claims 1-57 of the ‘007 Application . This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Conclusion 13. NO CLAIM IS ALLOWED. 07-96 AIA 14. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. WO2019006062 teaches an anti-amyloid chimeric mAb 11-1F4 comprising a VH of SEQ ID NO:48 which comprises CDRH1-3 of instant SEQ ID NOs: 21-23 and a VL of SEQ ID NO:47 which comprises CDRL1-3 of instant SEQ ID NOs: 24-26 (see the sequence alignment below). SEQ ID NO:21-SEQ ID NO:22-SEQ ID NO:23 BFZ31755 (NOTE: this sequence has 12 duplicates in the database searched) ID BFZ31755 standard; protein; 111 AA. XX AC BFZ31755; XX DT 21-FEB-2019 (first entry) XX DE Anti-amyloid chimeric mAb 11-1F4 VH, SEQ 48. XX KW Amyloid; amyloidosis; antibody production; antibody therapy; KW chimeric antibody; heavy chain variable region; immunoassay; KW metabolic-gen.; monoclonal antibody; protein detection; therapeutic. XX OS Mus musculus. OS Homo sapiens. OS Chimeric. XX FH Key Location/Qualifiers FT Region 31..36 FT /note= "CDR1" FT Region 50..75 FT /note= "CDR2" FT Region 98..100 FT /note= "CDR3" XX CC PN WO2019006062-A1. XX CC PD 03-JAN-2019. XX CC PF 28-JUN-2018; 2018WO-US039905. XX PR 29-JUN-2017; 2017US-0526835P. XX CC PA (UYCO ) UNIV COLUMBIA NEW YORK. XX CC PI Jones T, Levy A, Obrien S; XX DR WPI; 2019-017245/05. DR N-PSDB; BFZ31752. XX CC PT Chimeric mouse-human antibody comprises VK region and VH region which CC PT binds to epitope expressed by b-pleated sheet configuration of amyloid CC PT fibrils with higher affinity than mouse antibody. XX CC PS Claim 1; SEQ ID NO 48; 43pp; English. XX CC The present invention relates to a chimeric mouse-human antibody, useful CC for treating amyloid deposition diseases. The invention also includes: CC (1) a pharmaceutical composition comprising the antibody and a carrier; CC (2) a method for treating amyloid deposition disease in a patient; (3) a CC method for producing a chimeric antibody; (4) a vector construct such as CC 11-1F4VK.pKN100, 11-1F4VHpG1D200 and pG1KD200-11-1 F4; (5) a method for CC detecting the presence of amyloid deposits in the patient; (6) a chimeric CC mouse-human antibody produced by co-transfecting in mammalian cells of CC the vector constructs 11-1 F4VK.pKN100 and 11-F4VH.pG1 D200 or CC transfecting in mammalian cells of the super vector construct pG1 KD200- CC 11-1F4; (7) a polypeptide comprising the chimeric mouse-human antibody; CC and (8) a polynucleotide encoding the polypeptide. The present sequence CC is a mouse-human anti-amyloid chimeric monoclonal antibody (mAb) 11-1F4 CC heavy chain variable region (VH), useful for treating amyloid deposition CC diseases. XX SQ Sequence 111 AA; Query Match 84.5%; Score 134.4; Length 111; Best Local Similarity 38.7%; Matches 29; Conservative 0; Mismatches 0; Indels 46; Gaps 2; Qy 1 GFSLSSYGVS--------------VIWGDGSTNYHPNLMS-------------------- 26 |||||||||| |||||||||||||||| Db 26 GFSLSSYGVSWVRQPPGKGLEWLGVIWGDGSTNYHPNLMSRLSISKDISKSQVLFKLNSL 85 Qy 27 ------------LDY 29 ||| Db 86 QTDDTATYYCVTLDY 100 SEQ ID NO:24-SEQ ID NO:25-SEQ ID NO:26 BFZ31754 (NOTE: this sequence has 4 duplicates in the database searched) ID BFZ31754 standard; protein; 112 AA. XX AC BFZ31754; XX DT 21-FEB-2019 (first entry) XX DE Anti-amyloid chimeric mAb 11-1F4 VL, SEQ 47. XX KW Amyloid; amyloidosis; antibody production; antibody therapy; KW chimeric antibody; immunoassay; light chain variable region; KW metabolic-gen.; monoclonal antibody; protein detection; therapeutic. XX OS Mus musculus. OS Homo sapiens. OS Chimeric. XX FH Key Location/Qualifiers FT Region 24..40 FT /note= "CDR1" FT Region 55..61 FT /note= "CDR2" FT Region 94..103 FT /note= "CDR3" XX CC PN WO2019006062-A1. XX CC PD 03-JAN-2019. XX CC PF 28-JUN-2018; 2018WO-US039905. XX PR 29-JUN-2017; 2017US-0526835P. XX CC PA (UYCO ) UNIV COLUMBIA NEW YORK. XX CC PI Jones T, Levy A, Obrien S; XX DR WPI; 2019-017245/05. DR N-PSDB; BFZ31763. XX CC PT Chimeric mouse-human antibody comprises VK region and VH region which CC PT binds to epitope expressed by b-pleated sheet configuration of amyloid CC PT fibrils with higher affinity than mouse antibody. XX CC PS Claim 1; SEQ ID NO 47; 43pp; English. XX CC The present invention relates to a chimeric mouse-human antibody, useful CC for treating amyloid deposition diseases. The invention also includes: CC (1) a pharmaceutical composition comprising the antibody and a carrier; CC (2) a method for treating amyloid deposition disease in a patient; (3) a CC method for producing a chimeric antibody; (4) a vector construct such as CC 11-1F4VK.pKN100, 11-1F4VHpG1D200 and pG1KD200-11-1 F4; (5) a method for CC detecting the presence of amyloid deposits in the patient; (6) a chimeric CC mouse-human antibody produced by co-transfecting in mammalian cells of CC the vector constructs 11-1 F4VK.pKN100 and 11-F4VH.pG1 D200 or CC transfecting in mammalian cells of the super vector construct pG1 KD200- CC 11-1F4; (7) a polypeptide comprising the chimeric mouse-human antibody; CC and (8) a polynucleotide encoding the polypeptide. The present sequence CC is a mouse-human anti-amyloid chimeric monoclonal antibody (mAb) 11-1F4 CC light chain variable region (VL), useful for treating amyloid deposition CC diseases. XX SQ Sequence 112 AA; Query Match 85.4%; Score 144.3; Length 112; Best Local Similarity 40.5%; Matches 32; Conservative 0; Mismatches 0; Indels 47; Gaps 2; Qy 1 RSSQSLVHRNGNTYLH---------------KVSNRFS---------------------- 23 |||||||||||||||| ||||||| Db 24 RSSQSLVHRNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPRDFSGSGSGTDFTLKISRV 83 Qy 24 ----------FQTTYVPNT 32 ||||||||| Db 84 EAEDLGLYFCFQTTYVPNT 102 US20190083616 teaches an amyloid-reactive peptide comprising SEQ ID NO:1 which is 100% identical to instant SEQ ID NO:1 (see the sequence alignment below). SEQ ID NO:1 Sequence 1, US/16036900 Publication No. US20190083616A1 GENERAL INFORMATION APPLICANT: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION TITLE OF INVENTION: TARGETING IMMUNOTHERAPY FOR AMYLOIDOSIS FILE REFERENCE: 05820.004US3 CURRENT APPLICATION NUMBER: U