HER3 ANTIGEN-BINDING MOLECULES

§103 §112

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 . 1. The Amendment filed July 24, 2026 in response to the Office Action of March 24, 2026, is acknowledged and has been entered. Claims 24-43 are pending and being examined. Claims 24-39 are amended. New Rejection (necessitated by amendments) 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. 2. Claims 27, 31, 35, and 39 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention. Claims 27, 31, 35, and 39 recite and encompass an antigen-binding molecule comprising: “(a) a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:24, and comprising the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:44 HC-CDR3 having the amino acid sequence of SEQ ID NO:47; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:74, and comprising the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SAS (SEQ ID NO:92) LC-CDR3 having the amino acid sequence of SEQ ID NO:95; or (b) …” and so forth. A sequence alignment of the instantly claimed VH and VL SEQ ID NOs with the CDR SEQ ID NOs required to be present within them demonstrates a greater than 70% minimum sequence identity is required in order for the claimed VH and VL sequences to comprise the claimed CDR sequences. For example, VH SEQ ID NO:24 has an 84.1% sequence identity to a sequence comprising all of CDR SEQ ID NOs:41, 44, and 47 as recited by the claims (see sequence alignment below and Query Match %). Therefore, a sequence comprising less than 84.1% sequence identity to SEQ ID NO:24 (i.e., 70% as claimed) will exclude sequence identity to the CDR sequences required to be present, therefore, the claims as currently constituted are not enabled to comprise the claimed CDR sequences. Similarly, VL SEQ ID NO:74 has a 71.9% sequence identity to a sequence comprising all of CDR SEQ ID NOs:88, SAS, and 95 as recited by the claims (see sequence alignment below and Query Match %). Therefore, a sequence comprising less than 71.9% sequence identity to SEQ ID NO:74 (i.e., 70% as claimed) will exclude sequence identity to the CDR sequences required to be present and is not enabled to comprise the claimed CDR sequences. The same logic applies to the antigen-binding molecules recited in parts (b)-(q) of the claims. VH SEQ ID NO:24 aligned with CDR SEQ ID NOs:41+44+47: US-18-458-997-24 Filing date in PALM: 2023-08-30 Sequence 24, US/18458997 Publication No. US20240092937A1 GENERAL INFORMATION APPLICANT: Hummingbird Bioscience Holdings Pte. Ltd. (en) TITLE OF INVENTION: HER3 ANTIGEN-BINDING MOLECULES (en) FILE REFERENCE: H0969.70000US04 CURRENT APPLICATION NUMBER: US/18/458,997 CURRENT FILING DATE: 2023-08-30 NUMBER OF SEQ ID NOS: 231 SEQ ID NO 24 LENGTH: 120 TYPE: PRT FEATURE: NAME/KEY: REGION LOCATION: 1..120 QUALIFIERS: note = 10D1 heavy chain variable region FEATURE: NAME/KEY: source LOCATION: 1..120 QUALIFIERS: mol_type = protein organism = synthetic construct % Result Query Filing No. Score Match Length ID Date Dups Description ------------------------------------------------------------------------------------------------------------- 1 134.5 84.1 120 US-16-170-370A-24 2018-10-25 9 HER3 Antigen-Binding Molecules ALIGNMENT: Query Match 84.1%; Score 134.5; Length 120; Best Local Similarity 34.5%; Matches 29; Conservative 0; Mismatches 0; Indels 55; Gaps 2; Qy 1 GYSITSGYS-----------------IHYSGGT--------------------------- 16 ||||||||| ||||||| Db 26 GYSITSGYSWHWIRQFPGNKLEWMGSIHYSGGTNYNPSLKSRISITRDTSKNQFFLQLNS 85 Qy 17 -----------ARMTTAPRYPFDY 29 ||||||||||||| Db 86 VTTEDTATYFCARMTTAPRYPFDY 109 VL SEQ ID NO:74 aligned with CDR SEQ ID NOs:88+SAS+95: US-18-458-997-74 Filing date in PALM: 2023-08-30 Sequence 74, US/18458997 Publication No. US20240092937A1 GENERAL INFORMATION APPLICANT: Hummingbird Bioscience Holdings Pte. Ltd. (en) TITLE OF INVENTION: HER3 ANTIGEN-BINDING MOLECULES (en) FILE REFERENCE: H0969.70000US04 CURRENT APPLICATION NUMBER: US/18/458,997 CURRENT FILING DATE: 2023-08-30 NUMBER OF SEQ ID NOS: 231 SEQ ID NO 74 LENGTH: 107 TYPE: PRT FEATURE: NAME/KEY: REGION LOCATION: 1..107 QUALIFIERS: note = 10D1 light chain variable region FEATURE: NAME/KEY: source LOCATION: 1..107 QUALIFIERS: mol_type = protein organism = synthetic construct % Result Query Filing No. Score Match Length ID Date Dups Description ------------------------------------------------------------------------------------------------------------- 4 64.7 71.9 107 US-16-170-370A-74 2018-10-25 9 HER3 Antigen-Binding Molecules ALIGNMENT: Query Match 71.9%; Score 64.7; Length 107; Best Local Similarity 25.4%; Matches 18; Conservative 0; Mismatches 0; Indels 53; Gaps 2; Qy 1 QIVGSN-----------------SAS---------------------------------- 9 |||||| ||| Db 27 QIVGSNVAWYQQKPGQSPKPLIYSASYRYSGVPDRFTASGSGTDFTLTITNVQSEDLAEY 86 Qy 10 --QQYSSHPLT 18 ||||||||| Db 87 FCQQYSSHPLT 97 Maintained Rejection (addressing amendments) 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. 3. Claims 24, 28, 32, 36, and 40-43 remain 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. This is a WRITTEN DESCRIPTION rejection. The claims are drawn to: an antigen-binding molecule comprising a heavy chain variable (VH) region and a light chain variable (VL) region, wherein the antigen-binding molecule specifically binds to HER3, and wherein binding to HER3 comprises contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:230 and SEQ ID NO:231; a nucleic acid encoding the antibody, a cell comprising the nucleic acid encoding the antibody; and a method of treating a cancer in a subject, comprising administering to a subject a therapeutically effective amount of an antigen-binding molecule comprising a heavy chain variable (VH) region and a light chain variable (VL) region, wherein the antigen-binding molecule specifically binds to HER3, and wherein binding to HER3 comprises contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:230 and SEQ ID NO:231. Thus, the claims identify the antigen-binding molecule by function only, where the function is to: bind HER3 and come into contact with one or more amino acid residues of the region of HER3 shown in SEQ ID NO:230 and SEQ ID NO:231; and treat cancer in a subject. No antigen-binding molecule or antibody structure is recited. The instant specification discloses seventeen total 10D1 antibody and 10D1-derived clones comprising defined pairs of VH and VL sequences in the Table of Example 1: PNG media_image1.png 668 430 media_image1.png Greyscale The instant specification discloses that the antibodies bind to a motif 1 (SEQ ID NO:230) and motif 2 (SEQ ID NO:231) within SEQ ID NO:229: The site of HER3 to which 10D1 and 10D1-derived clones was determined to bind corresponds to positions 218 to 235 of the amino acid sequence of human HER3 (as shown e.g. In SEQ ID NO:1); the amino acid sequence for this region of HER3 Is shown in SEQ ID NO:229. Within this region, two consensus binding site motifs were identified, and are shown in SEQ ID NOs:230 and 231. Thus, the instant specification describes seventeen 10D1 derivative antibodies that function as claimed, wherein each of the seventeen antibodies comprises a defined single set of VH and VL sequences. The specification fails to disclose any other antigen-binding molecules or antibodies that possess the function of binding HER3 and coming into contact with the region of HER3 shown in SEQ ID NO:230 and 231, and treating cancer in a subject. To provide adequate written description and evidence of possession of the claimed antibody genus, the instant specification can structurally describe representative antigen-binding molecules or antibodies that function to bind HER3 and come into contact with SEQ ID NO:230 and 231, and treat cancer, or describe structural features common to the members of the genus, which features constitute a substantial portion of the genus. Alternatively, the specification can show that the claimed invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics (see University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) and Enzo Biochem, Inc. V. Gen-Probe Inc.). A disclosure that does not adequately describe a product itself logically cannot adequately describe a method of using that product. Although Applicants may argue that it is possible to screen for antibodies that bind HER3 and function as claimed, the court found in (Rochester v. Searle, 358 F.3d 916, Fed Cir., 2004) that screening assays are not sufficient to provide adequate written description for an invention because they are merely a wish or plan for obtaining the claimed chemical invention. “As we held in Lilly, “[a]n adequate written description of a DNA … ‘requires a precise definition, such as by structure, formula, chemical name, or physical properties,’ not a mere wish or plan for obtaining the claimed chemical invention.” 119 F.3d at 1566 (quoting Fiers, 984 F.2d at 1171). For reasons stated above, that requirement applies just as well to non-DNA (or RNA) chemical inventions.” Knowledge of screening methods provides no information about the structure of any future antibodies yet to be discovered that may function as claimed. The HER3 epitope comprising SEQ ID NO:230 and 231 provides no information about the structure of an antibody that binds to it. In this case, the only factor present in the claims is a recitation of the antibody function. The instant specification fails to describe structural features common to the members of the genus, which features constitute a substantial portion of the genus because the instant specification discloses only seventeen defined exemplary antibody VH and VL sequence pairs that function as claimed. A definition by function does not suffice to define the genus because it is only an indication of what the antibody does, rather than what it is. Applicants have not established any reasonable structure-function correlation with regards to the sequences in the variable domains or CDRs that can be altered and still maintain the claimed functions of binding HER3 at epitopes SEQ ID NO:230 and 231 and treating cancer. The instant specification also fails to describe a representative number of antibody sequences for the genus of antibodies that function as claimed. One could not readily envision members of the broadly claimed genus required to practice the invention. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus required to make and practice the claimed invention. Given the lack of representative examples to support the full scope of the claimed antibodies and those used in the claimed method, and lack of reasonable structure-function correlation with regards to what sequences can be altered and maintain the claimed functions, the present claims lack adequate written description. Thus, the specification does not provide an adequate written description of antibodies that bind HER3 at epitopes SEQ ID NO:2301 and 231 that is required to practice the claimed invention. Since the specification fails to adequately describe the product to which the claimed method uses, it also fails to adequately describe the method. Examiner Suggestion: Amend the rejected claims to recite and require the antigen-binding molecule/ antibody comprise at least the six heavy and light chain CDR SEQ ID NOs of claims 25 or 26 required to function as claimed. Response to Arguments 4. Applicants argue that the disclosed seventeen 10D1 and 10D1 derivative antibodies are sufficiently representative of the claimed genus. Applicants argue that the claimed antibodies are readily obtainable by routine methods such as antibody phage display screening for HER3 antigen binding. Applicants argue that the decision in Rochester argued by Examiner is not applicable to the instant claims because in Rochester, no exemplary species of claimed non-steroidal compounds were disclosed in the specification. Applicants argue that in the instant case, they have disclosed seventeen exemplary species of antibody within their claimed genus. 5. The arguments have bene considered but are not persuasive. Contrary to arguments, the 17 disclosed species of highly homologous 10D1 and 10D1 derivative antibodies are not sufficiently representative of the claimed genus of antigen-binding molecules. When considering whether the specification discloses a sufficient representative number of species to satisfy written description, one must account for the breadth of the claimed genus. MPEP 2163 states: 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. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (Claims directed to a functionally defined genus of antibodies were not supported by a disclosure that "only describe[d] one type of structurally similar antibodies" that "are not representative of the full variety or scope of the genus."). The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure "indicates that the patentee has invented species sufficient to constitute the gen[us]." See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) ("[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated."). "A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004) Satisfactory disclosure of a "representative number" depends on whether one of skill in the art would recognize that the inventor was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. See, e.g., Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are "representative of the full variety or scope of the genus," or by the establishment of "a reasonable structure-function correlation." Such correlations may be established "by the inventor as described in the specification," or they may be "known in the art at the time of the filing date." See AbbVie, 759 F.3d at 1300-01, 111 USPQ2d 1780, 1790-91 (Fed. Cir. 2014) (Holding that claims to all human antibodies that bind IL-12 with a particular binding affinity rate constant (i.e., koff) were not adequately supported by a specification describing only a single type of human antibody having the claimed features because the disclosed antibody was not representative of other types of antibodies in the claimed genus, as demonstrated by the fact that other disclosed antibodies had different types of heavy and light chains, and shared only a 50% sequence similarity in their variable regions with the disclosed antibodies.). Description of a representative number of species does not require the description to be of such specificity that it would provide individual support for each species that the genus embraces. In the instant case claimed genus of antigen-binding molecules is vast and highly variable, encompassing any antigen-binding molecule or antibody of any sequence structure or chemical formula that functions to bind to HER3 region comprising SEQ ID NOs:230 and 231. Seventeen highly homologous 10D1 antibodies fail to provide a representative number of exemplary species for the vast genus of highly structurally variable antigen-binding molecules that function as claimed. One of skill in the art could not immediately envision members of the vast genus claimed based on the disclosure of only seventeen highly homologous 10D1 antibodies. Contrary to arguments, the decision in Rochester is relevant, and knowledge of routine screening methods to produce antibodies does not place Applicants in possession of the claimed genus of antigen-binding molecules. MPEP 2163 states: Conversely, describing a composition by its function alone typically will not suffice to sufficiently describe the composition. See Eli Lilly, 119 F.3 at 1568, 43 USPQ2d at 1406 (Holding that description of a gene’s function will not enable claims to the gene "because it is only an indication of what the gene does, rather than what it is."); see also Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen Inc. v. Chugai Pharm. Co., 927 F.2d 1200, 18 USPQ2d 1016 (Fed. Cir. 1991)). An adequate written description of a chemical invention also requires a precise definition, such as by structure, formula, chemical name, or physical properties, and not merely a wish or plan for obtaining the chemical invention claimed. See, e.g., Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004) (The patent at issue claimed a method of selectively inhibiting PGHS-2 activity by administering a non-steroidal compound that selectively inhibits activity of the PGHS-2 gene product, however the patent did not disclose any compounds that can be used in the claimed methods. While there was a description of assays for screening compounds to identify those that inhibit the expression or activity of the PGHS-2 gene product, there was no disclosure of which peptides, polynucleotides, and small organic molecules selectively inhibit PGHS-2. The court held that "[w]ithout such disclosure, the claimed methods cannot be said to have been described."). In the instant case, making and screening for antibodies that function as claimed is merely a wish or plan for obtaining the claimed antigen-binding molecule. MPEP 2163 states: For example, disclosure of an antigen fully characterized by its structure, formula, chemical name, physical properties, or deposit in a public depository does not, without more, provide an adequate written description of an antibody claimed by its binding affinity to that antigen, even when preparation of such an antibody is routine and conventional. See Amgen Inc. v. Sanofi, 872 F.3d 1367, 1378, 124 USPQ2d 1354, 1361 (Fed. Cir. 2017)("knowledge of the chemical structure of an antigen [does not give] the required kind of structure-identifying information about the corresponding antibodies"); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1351-52, 97 USPQ2d 1870, 1877 (Fed. Cir. 2011)(patent disclosed the antigen the claimed antibody was supposed to bind, but did not disclose any antibodies with the specific claimed properties). In the instant case, knowledge of the HER3 epitope comprising SEQ ID NOs:230 and 231, even when preparation of an antibody against an epitope is routine and conventional, does not provide an adequate written description of an antibody claimed by its binding affinity to that epitope. Maintained Rejections 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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp. 6. Claims 24-43 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-25 of U.S. Patent No. 10,662,241 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming and antigen-binding molecule comprising a VH and VL region comprising the same CDR sequences instantly claimed that bind to HER3 epitope comprising SEQ ID NOs:230 and 231, a nucleic acid encoding the antigen-binding molecule, a cell expressing the antigen-binding molecule, and method of treating cancer in a subject comprising administering the antigen-binding molecule, wherein the cancer comprises cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, and more, rendering obvious instant claims 24-40. The US Patent claims: 1. An antigen-binding molecule that specifically binds to HER3, comprising: (i) a heavy chain variable (VH) region having the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:45 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region having the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SEQ ID NO:92 LC-CDR3 having the amino acid sequence of SEQ ID NO:95. 2. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises: a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83. 3. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises: a VH region having the following framework regions (FRs): HC-FR1 having the amino acid sequence of SEQ ID NO:53 HC-FR2 having the amino acid sequence of SEQ ID NO:59 HC-FR3 having the amino acid sequence of SEQ ID NO:66 HC-FR4 having the amino acid sequence of SEQ ID NO:71. 4. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises: a VL region having the following framework regions (FRs): LC-FR1 having the amino acid sequence of SEQ ID NO:104 LC-FR2 having the amino acid sequence of SEQ ID NO:110 LC-FR3 having the amino acid sequence of SEQ ID NO:120 LC-FR4 having the amino acid sequence of SEQ ID NO:125. 5. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171. 6. The antigen-binding molecule according to claim 1, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177. 7. A nucleic acid, or a plurality of nucleic acids, encoding an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises: (i) a heavy chain variable (VH) region having the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:45 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region having the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SEQ ID NO:92 LC-CDR3 having the amino acid sequence of SEQ ID NO:95. 8. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises: a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83. 9. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises: a VH region having the following framework regions (FRs): HC-FR1 having the amino acid sequence of SEQ ID NO:53 HC-FR2 having the amino acid sequence of SEQ ID NO:59 HC-FR3 having the amino acid sequence of SEQ ID NO:66 HC-FR4 having the amino acid sequence of SEQ ID NO:71. 10. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises: a VL region having the following framework regions (FRs): LC-FR1 having the amino acid sequence of SEQ ID NO:104 LC-FR2 having the amino acid sequence of SEQ ID NO:110 LC-FR3 having the amino acid sequence of SEQ ID NO:120 LC-FR4 having the amino acid sequence of SEQ ID NO:125. 11. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171. 12. The nucleic acid or plurality of nucleic acids according to claim 7, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177. 13. A cell comprising a nucleic acid, or a plurality of nucleic acids, encoding an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises: (i) a heavy chain variable (VH) region having the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:45 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region having the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SEQ ID NO:92 LC-CDR3 having the amino acid sequence of SEQ ID NO:95. 14. The cell according to claim 13, wherein the antigen-binding molecule comprises: a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83. 15. The cell according to claim 13, wherein the antigen-binding molecule comprises: a VH region having the following framework regions (FRs): HC-FR1 having the amino acid sequence of SEQ ID NO:53 HC-FR2 having the amino acid sequence of SEQ ID NO:59 HC-FR3 having the amino acid sequence of SEQ ID NO:66 HC-FR4 having the amino acid sequence of SEQ ID NO:71. 16. The cell according to claim 13, wherein the antigen-binding molecule comprises: a VL region having the following framework regions (FRs): LC-FR1 having the amino acid sequence of SEQ ID NO:104 LC-FR2 having the amino acid sequence of SEQ ID NO:110 LC-FR3 having the amino acid sequence of SEQ ID NO:120 LC-FR4 having the amino acid sequence of SEQ ID NO:125. 17. The cell according to claim 13, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171. 18. The cell according to claim 13, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177. 19. A method of treating a cancer in a subject, comprising administering to a subject a therapeutically effective amount of an antigen-binding molecule that specifically binds to HER3, wherein the antigen-binding molecule comprises: (i) a heavy chain variable (VH) region having the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:45 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region having the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SEQ ID NO:92 LC-CDR3 having the amino acid sequence of SEQ ID NO:95. 20. The method according to claim 19, wherein the antigen-binding molecule comprises: a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83. 21. The method according to claim 19, wherein the antigen-binding molecule comprises: a VH region having the following framework regions (FRs): HC-FR1 having the amino acid sequence of SEQ ID NO:53 HC-FR2 having the amino acid sequence of SEQ ID NO:59 HC-FR3 having the amino acid sequence of SEQ ID NO:66 HC-FR4 having the amino acid sequence of SEQ ID NO:71. 22. The method according to claim 19, wherein the antigen-binding molecule comprises: a VL region having the following framework regions (FRs): LC-FR1 having the amino acid sequence of SEQ ID NO:104 LC-FR2 having the amino acid sequence of SEQ ID NO:110 LC-FR3 having the amino acid sequence of SEQ ID NO:120 LC-FR4 having the amino acid sequence of SEQ ID NO:125. 23. The method according to claim 19, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171. 24. The method according to claim 19, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177. 25. The method according to claim 19, wherein the cancer is selected from: a cancer comprising cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, breast carcinoma, ductal carcinoma, gastric cancer, gastric carcinoma, gastric adenocarcinoma, colorectal cancer, colorectal carcinoma, colorectal adenocarcinoma, head and neck cancer, squamous cell carcinoma of the head and neck (SCCHN), lung cancer, lung adenocarcinoma, squamous cell lung carcinoma, ovarian cancer, ovarian carcinoma, ovarian serous adenocarcinoma, kidney cancer, renal cell carcinoma, renal clear cell carcinoma, renal cell adenocarcinoma, renal papillary cell carcinoma, pancreatic cancer, pancreatic adenocarcinoma, pancreatic ductal adenocarcinoma, cervical cancer, cervical squamous cell carcinoma, skin cancer, melanoma, esophageal cancer, esophageal adenocarcinoma, liver cancer, hepatocellular carcinoma, cholangiocarcinoma, uterine cancer, uterine corpus endometrial carcinoma, thyroid cancer, thyroid carcinoma, pheochromocytoma, paraganglioma, bladder cancer, bladder urothelial carcinoma, prostate cancer, prostate adenocarcinoma, sarcoma and thymoma. With regards to claims 41-43, the US Patent does not claim additionally administering trastuzumab or docetaxel to treat cancer. Aurisicchio teaches monoclonal antibodies comprising VH and VL domains that bind to HER3 extracellular epitopes, including epitopes comprising instant SEQ ID NO:230 (PNPNQ), such as epitope CFGPNPNQ (SEQ ID NO: 38), FGPNPNQC (SEQ ID NO: 39), GPNPNQCC (SEQ ID NO: 40), CFGPNPNQC (SEQ ID NO: 46), FGPNPNQCC (SEQ ID NO: 47), and CFGPNPNQCC (SEQ ID NO: 53) (p. 22-23; Figure 10). Aurisicchio teaches nucleic acids encoding the antibodies and transfecting cells to express and produce the antibodies (Examples 9, 11, and 12). Aurisicchio teaches administering the antibodies to subjects to treat cancer including pancreatic cancer and breast cancer (Examples 6-8). Aurisicchio teaches administering the antibodies in combination with HERCEPTIN™ (trastuzumab) anti-HER2 antibody to enhance treatment of cancer (Example 8). Aurisicchio suggests treating cancer with chemotherapeutics (p. 3) and suggests combining the HER3 antibody with an anti-neoplastic agent (p. 34). Schoebert also teaches producing therapeutic monoclonal antibodies against the HER3 extracellular domain. Schoebert also teaches compositions comprising the antibodies, nucleic acids encoding the antibodies (p. 4, 20-22, 38), and routine methods of making the antibodies by immunization of mammals, isolation of hybridoma cells producing the antibodies, isolating antibody clones from phage display, sequencing the antibodies, and transfecting cells to express the antibodies (p. 29-33; Example 1). Schoebert teaches methods of treating cancer in a subject by administering the anti-HER3 antibody in combination with known anti-cancer agents, including docetaxel trastuzumab, and cetuximab, and treating breast and pancreatic cancer (p. 5, 22-29, 44; Example 9; claims 44-53). It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. 7. Claims 24-43 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 11,208,498, in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming a method of treating the same cancer instantly claimed comprising administering an antigen-binding molecule comprising VH and VL domains that comprise the same CDR sequences instantly claimed, thereby rendering obvious HER3 antigen-binding molecule of instant claims 24-27 and methods of treating cancer of instant claims 36-40. 1. A method of treating a cancer in a subject, wherein the cancer comprises cells having a mutation resulting in increased expression of a ligand for HER3, wherein the method comprises administering a therapeutically or prophylactically effective amount of an antigen-binding molecule which is capable of binding to HER3 to the subject, and wherein the antigen-binding molecule comprises: (i) a heavy chain variable (VH) region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:43 HC-CDR2 having the amino acid sequence of SEQ ID NO:46 HC-CDR3 having the amino acid sequence of SEQ ID NO:51; and (ii) a light chain variable (VL) region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:91 LC-CDR2 having the amino acid sequence of SEQ ID NO:94 LC-CDR3 having the amino acid sequence of SEQ ID NO:99. 2. The method according to claim 1, wherein the ligand for HER3 comprises an amino acid sequence having at least 60% sequence identity to the EGF-like domain of an NRG. 3. The method according to claim 1, wherein the mutation results in increased expression of the EGF-like domain of an NRG at the cell surface. 4. The method according to claim 1, wherein the cancer comprises cells having an NRG gene fusion. 5. The method according to claim 4, wherein the NRG gene fusion is selected from CLU-NRG1, CD74-NRG1, DOC4-NRG1, SLC3A2-NRG1, RBPMS-NRG1, WRN-NRG1, SDC4-NRG1, RAB2IL1-NRG1, VAMP2-NRG1, KIF13B-NRG1, THAP7-NRG1, SMAD4-NRG1, MDK-NRG1, TNC-NRG1, DIP2B-NRG1, MRPL13-NRG1, PARP8-NRG1, ROCK1-NRG1, DPYSL2-NRG1, ATP1B1-NRG1, CDH6-NRG1, APP-NRG1, AKAP13-NRG1, THBS1-NRG1, FOXA1-NRG1, PDE7A-NRG1, RAB3IL1-NRG1, CDK1-NRG1, BMPRIB-NRG1, TNFRSF10B-NRG1, MCPH1-NRG1 and SLC12A2-NRG2. 6. The method according to claim 4, wherein the NRG gene fusion is selected from CLU-NRG1, CD74-NRG1, SLC3A2-NRG1 or VAMP2-NRG1. 7. The method according to claim 1, wherein the cancer comprises cells expressing HER3. 8. The method according to claim 1, wherein the cancer derives from the lung, breast, head, neck, kidney, ovary, pancreas, prostate, uterus, gallbladder, colon, rectum, bladder, soft tissue or nasopharynx. 9. The method according to claim 1, wherein the cancer is selected from lung cancer, non-small cell lung cancer, lung adenocarcinoma, invasive mucinous lung adenocarcinoma, lung squamous cell carcinoma, breast cancer, breast carcinoma, breast invasive carcinoma, head and neck cancer, head and neck squamous cell carcinoma, renal cancer, renal clear cell carcinoma, ovarian cancer, ovarian serous cystadenocarcinoma, pancreatic cancer, pancreatic adenocarcinoma, pancreatic ductal adenocarcinoma, prostate cancer, prostate adenocarcinoma, endometrial cancer, uterine carcinosarcoma, gallbladder cancer, cholangiocarcinoma, colorectal cancer, bladder cancer, urothelial bladder cancer, sarcoma, soft tissue sarcoma, neuroendocrine tumor and neuroendocrine tumor of the nasopharynx. 10. The method according to claim 1, wherein the cancer is selected from lung cancer, non-small cell lung cancer, lung adenocarcinoma, invasive mucinous lung adenocarcinoma and lung squamous cell carcinoma. 11. The method according to claim 1, wherein the antigen-binding molecule comprises: (i) a VH region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:41 HC-CDR2 having the amino acid sequence of SEQ ID NO:45 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a VL region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:88 LC-CDR2 having the amino acid sequence of SEQ ID NO:92 LC-CDR3 having the amino acid sequence of SEQ ID NO:95. 12. The method according to claim 1, wherein the antigen-binding molecule comprises: a VH region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:36; and a VL region comprising an amino acid sequence having at least 70% sequence identity to the amino acid sequence of SEQ ID NO:83. 13. The method according to claim 1, wherein the antigen-binding molecule comprises: a VH region incorporating the following framework regions (FRs): HC-FR1 having the amino acid sequence of SEQ ID NO:53 HC-FR2 having the amino acid sequence of SEQ ID NO:59 HC-FR3 having the amino acid sequence of SEQ ID NO:66 HC-FR4 having the amino acid sequence of SEQ ID NO:71. 14. The method according to claim 1, wherein the antigen-binding molecule comprises: a VL region incorporating the following framework regions (FRs): LC-FR1 having the amino acid sequence of SEQ ID NO:104 LC-FR2 having the amino acid sequence of SEQ ID NO:110 LC-FR3 having the amino acid sequence of SEQ ID NO:120 LC-FR4 having the amino acid sequence of SEQ ID NO:125. 15. The method according to claim 1, wherein the antigen-binding molecule comprises a heavy chain comprising the amino acid sequence of SEQ ID NO:171. 16. The method according to claim 1, wherein the antigen-binding molecule comprises a light chain comprising the amino acid sequence of SEQ ID NO:177. The US Patent does not claim nucleic acids encoding the antibody, cells expressing the antibody, and additionally administering trastuzumab or docetaxel to treat cancer. Aurisicchio and Schoebert teach as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the US Patent. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. 8. Claims 24-43 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 11,780,933 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. Although the claims at issue are not identical, they are not patentably distinct from each other because the US Patent is claiming an antigen-binding molecule comprising a VH and VL region comprising all of the same CDR sequences instantly claimed that bind to HER3 epitope comprising SEQ ID NOs:230 and 231, nucleic acid encoding the antigen-binding molecule, a cell expressing the antigen-binding molecule, and method of treating cancer in a subject comprising administering the antigen-binding molecule, wherein the cancer includes cancer comprising cells expressing an EGFR family member, a cancer comprising cells expressing HER3, a solid tumor, breast cancer, and more, rendering obvious instant claims 24-40. With regards to claims 41-43, the US Patent does not claim additionally administering trastuzumab or docetaxel to treat cancer. Aurisicchio and Schoebert teach as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the US Patent. One would have been motivated to and have a reasonable expectation of success to because: (1) the US Patent claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. 9. Claims 24-43 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3, 4, 7, 8, 11-13, 15, 19, 21, 23-30 of copending Application No. 18/683,155 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. The copending application claims a method of treating HER3-associated cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is a solid tumor, breast cancer, gastric cancer, pancreatic cancer, and more; wherein the HER3 antibody is 10D1F or comprises a VH and VL as follows: (a) (i) a heavy chain variable (VH) region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:40 HC-CDR2 having the amino acid sequence of SEQ ID NO:43 HC-CDR3 having the amino acid sequence of SEQ ID NO:48; and (ii) a light chain variable (VL) region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:66 LC-CDR2 having the amino acid sequence of SEQ ID NO:69 LC-CDR3 having the amino acid sequence of SEQ ID NO:74; or (b) (i) a heavy chain variable (VH) region incorporating the following CDRs: HC-CDR1 having the amino acid sequence of SEQ ID NO:38 HC-CDR2 having the amino acid sequence of SEQ ID NO:42 HC-CDR3 having the amino acid sequence of SEQ ID NO:45; and (ii) a light chain variable (VL) region incorporating the following CDRs: LC-CDR1 having the amino acid sequence of SEQ ID NO:63 LC-CDR2 having the amino acid sequence of SEQ ID NO:67 LC-CDR3 having the amino acid sequence of SEQ ID NO:70; wherein SEQ ID NOs:38, 42, 45, 63, 67, and 70 are 100% identical to instant CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95, respectively; wherein the VH comprises SEQ ID NO:33 and VL comprises SEQ ID NO:58 that are 100% identical to instant SEQ ID NOs:36 and 83, respectively. The copending application claims treating the same cancer population instantly claimed by administering the same HER3 antibody comprising the same CDR and VH and VL sequences. The method of the copending application renders obvious the instant HER3 antibody itself. Therefore, the copending claims overlap in scope with, and render obvious instant claims 24-27 and 36-40. The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel. Aurisicchio and Schoebert teach as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. This is a provisional nonstatutory double patenting rejection. 10. Claims 24-43 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 4, 7, 9, 17, 18, 22, 24, 26, 30-32, 34-37, 39, 42, 46 and 47 of copending Application No. 18/688,576 in view of WO 2008/100624, Schoebert et al. The copending application claims a HER3 antigen-binding molecule comprising VH and VL CDR SEQ ID NOs:43, 46, 51, 91, 94, and 99 that are identical to the same instant SEQ ID NOs; or comprising CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95 that are identical to the same instant SEQ ID NOs; a method of treating cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is breast, gastric, pancreatic cancer and more; and wherein the composition is administered in combination with cetixumab or trastuzumab. The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering docetaxel. Schoebert teaches as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Schoebert teaches and demonstrates that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer in combination with other anticancer agents; (2) Schoebert suggests combining anti-cancer agents with HER3 antibody for the treatment of cancer, and (3) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. This is a provisional nonstatutory double patenting rejection. 11. Claims 24-43 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-30 of copending Application No. 18/403,476 in view of in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. The copending application claims an antibody binding to HER3 that comprises CDR SEQ ID NOs:38, 42, 45, 63, 67, 70, that are 100% identical to instant SEQ ID NOs:41, 45, 48, 63, 67, and 70; and comprises VH and VL SEQ ID NOs:33 and 58, that are 100% identical to instant VH and VL SEQ ID NOs:36 and 83; methods of treating cancer comprising administering the antibody, wherein the cancer is cancer cells comprising cells expressing EGFR family member, breast cancer, gastric cancer, pancreatic cancer, and more cancers. Therefore, the copending claims overlap in scope with, and render obvious, the instantly claimed antibody and method of treating cancer. The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel. Aurisicchio and Schoebert teach as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. This is a provisional nonstatutory double patenting rejection. 12. Claims 24-43 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3-16 of copending Application No. 19/301,118 in view of WO 2012/059224, Aurisicchio, published May 2012, and WO 2008/100624, Schoebert et al. The copending application claims a method of treating cancer in a subject comprising administering to the subject an antigen-binding molecule which binds to HER3; wherein the cancer is a lung cancer, breast cancer, pancreatic cancer, and more; wherein the HER3 antibody is comprises a VH and VL comprising CDR SEQ ID NOs: 43, 46, 51, 91, 94, and 99 that are 100% identical to the instantly claimed CDR sequences; or comprising CDR SEQ ID NOs:41, 45, 48, 88, 92, and 95 that are 100% identical to the instantly claimed CDR sequences; wherein the VH comprises SEQ ID NO:36 and VL comprises SEQ ID NO:83 that are 100% identical to instant SEQ ID NOs:36 and 83. The copending application claims treating the same cancer population instantly claimed by administering the same HER3 antibody comprising the same CDR and VH and VL sequences. The method of the copending application renders obvious the instant HER3 antibody itself. Therefore, the copending claims overlap in scope with, and render obvious instant claims 24-27 and 36-40. The copending application does not claim a nucleic acid encoding the antibody, cell expressing the antibody, or the method of treating cancer further comprising administering trastuzumab or docetaxel. Aurisicchio and Schoebert teach as set forth above. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to make nucleic acids encoding the antibody and cells expressing the antibody of the copending application. One would have been motivated to and have a reasonable expectation of success to because Aurisicchio and Schoebert teach and demonstrate that production and isolation of nucleic acid sequences encoding HER3 antibodies for the expression in cells to produce antibodies is routine and conventional. It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to administer trastuzumab or docetaxel in the method of treating cancer claimed by the copending application. One would have been motivated to and have a reasonable expectation of success to because: (1) the copending application claims administering their HER3 antibody to treat cancer; (2) Aurisicchio and Schoebert suggest combining anti-cancer agents with HER3 antibody for the treatment of cancer, (3) Aurisicchio demonstrates that trastuzumab combined with anti-HER3 antibody improved therapeutic efficacy of cancer; and (4) Schoebert teaches docetaxel is a known, established chemotherapeutic for treatment of cancer and suggests combining it with anti-HER3 antibody therapy. This is a provisional nonstatutory double patenting rejection. Response to Arguments 13. Applicants argue the pending claims are amended and request Examiner to withdraw or reevaluate the rejections in response to the 35 USC 103 rejection. Applicants argue that Examiner’s rationale for obviousness is not necessarily applicable to the amended claims. 14. The arguments have been considered but are not persuasive. Applicants presented no specific arguments as to why the US Patents and copending applications now fail to render obvious the instantly claimed invention as amended. The double patenting rejections above take into consideration the current claim amendments and are maintained. 15. All other objections and rejections recited in the Office Action mailed March 24, 2026 are hereby withdrawn. The claims/specification objections are withdrawn in view of amendments spelling out the amino acid sequences of SEQ ID NOs:92-94. The rejection of claims under 35 U.S.C. 102(a)(1) as being anticipated by Boyd-Kirkup et al (Proceedings of the American Association for Cancer Research Annual Meeting, 2017: 2017 April 1-5; Washington DC. Philadelphia (PA): AACR; Cancer Research, 2017; 77(13 Suppl); Abstract 24) is withdrawn in view of arguments that the disclosed HMBD001 antibody is not publicly available (enabled) and the antibody is not disclosed or determined to bind HER3 epitopes SEQ ID NOs:230 and 231. The rejection of claims under 35 U.S.C. 102(a)(1) as being anticipated by Thakker et al (European Journal of Cancer, November 13, 2018; 103S1; e36-e37; Poster Session; abstract 87) and rejection of claims under 35 U.S.C. 103 as being obvious over Thakker are both withdrawn in view of the Boyd-Kirkup declaration filed under 37 CFR 1.130 stating the exception under 102(b)(1)(A) and disqualifying Thakker as prior art. The rejection of claims under 35 U.S.C. 102(a)(1) as being anticipated by WO 2012/059224, Aurisicchio and rejection of claims under 35 U.S.C. 103 as being obvious over Aurisicchio are withdrawn in view of claim amendments requiring the antigen-binding molecule bind to HER3 regions comprising SEQ ID NO:230 and SEQ ID NO:231. Aurisicchio does not teach or suggest their antibodies bind to both sequence regions of HER3. 16. Conclusion: No claim is allowed. Conclusion 17. THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a). A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action. 18. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LAURA B GODDARD whose telephone number is (571)272-8788. The examiner can normally be reached Mon-Fri, 7am-3:30pm. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. 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If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /Laura B Goddard/Primary Examiner, Art Unit 1642