Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of the species G166-S114 charge pair mutation in the reply filed on 04/14/2026 is acknowledged.
Application Status
Claims 1-22 are pending and examined on the merits herein.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 2 and 4-5 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 2 recites “a Fc region (containing a CH2 and CH3 regions)” in options (a)-(c). The use of parentheses in the instant claim renders the claim indefinite as the limitations in the parentheses are not defining the term in front of the parentheses and it is therefore unclear whether the limitation in the parentheses are a required part of the claimed invention.
Claim 4 recites “(a) a negatively charged amino acid (D or E)” and “(b) a positively charged amino acid (K or R).” The use of parentheses in the instant claim renders the claim indefinite as the limitations in the parentheses are not defining the term in front of the parentheses and it is therefore unclear whether the limitation in the parentheses are a required part of the claimed invention
Claim 5 recites “wherein the CH1 and CL regions of one of the two arms comprise amino acid substitutions at an amino acid residue corresponding to the amino acid position of SEQ ID NO: 17, 18, 19, or 20 for CH1 and SEQ ID NO: 21 or 22 for CL; wherein the amino acid substitution in the CH1 and CL regions are selected from (1) K133C and C220X in CH1, and F209C and C214X in CL; (2) R133C and C131X in CH1, and F209C and C214X in CL; (3) R133C and C131X in CH1, and V209C or C214X in CL; or (4) K133C and C220X in CH1, and V209C or C214X in CL; wherein X is selected from S, A or G.” The reference SEQ ID NOs do not comprise the length, in total residues, for which the claimed amino acid substitution are referencing. For example, SEQ ID NO: 17 is 103 residues in total length; none of SEQ ID NOs: 17-20, referring to the CH1 domain, have more than 105 total residues, as listed. Thus, the required amino acid substitution cannot occur at residues 133 or 220 of SEQ ID NOs: 17-20, as those residues are not defined in the listed sequences. Similarly, SEQ ID NOs: 21 and 22, referring to the CL domain, have no more than 107 total residues as listed. Thus, the amino acid substitution cannot occur at residues 209 or 214, as those residues are not defined in the sequences. The specifications disclose that antibodies comprising a K133 and F209 the CH1 region were produced, and thus the substitutions within the CH1 domains are functional (see Table 2, Fig. 2). However, claim 5 fails to particularly point out and distinctly claim the subject matter of the invention, as the numbering system seems to include more than the total residues of any one of SEQ ID NOs: 17-22. Thus, it is unclear where the numbering system begins, or more particularly, which amino acid residues of the CH1 domain of SEQ ID NOs: 17-20, or the CL domain of SEQ ID NOs: 21-22, the claim is referring to. That is, it is unclear to the skilled artisan which substituted amino acid residues, within SEQ ID NOs: 17-20, would read on the limitations of instant claim 5. As the metes and bounds of the claim are unclear, claim 5 is rejected for indefiniteness.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-3 and 10-22 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Li (US 2023/0089926 A1; PTO-892).
The applied reference has a common assignee and inventor with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed in the reference and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement.
Regarding claims 1-3, Li teaches an isolated multi-specific antibody or antigen-binding fragment thereof, wherein the multi-specific antibody or antigen-binding fragment thereof is a bispecific antibody or antigen-binding fragment comprising a first antigen-binding arm (Ab1) and a second antigen-binding arm (Ab2), wherein Ab1 and/or Ab2 comprise a substituted amino acid that is conjugated to a FA (claims 1, 11-12), wherein the first antigen-binding arm (Ab1) comprises H1 and L1 and a second antigen-binding arm (Ab2) comprises H2 and L2, wherein
(a) H1 and H2 each comprises a CH1 region of human IgG1, IgG2, IgG3, or IgG4; and
(b) L1 and L2 each comprises a CL region of a human kappa light chain or a human lambda light chain;
wherein H1L1 and H2L2 each comprise a charge pair selected from the group consisting of the following amino acid substitutions:
(1) G166D/E in CH1 of H1 and S114K/R in CL of L1, respectively, and G166K/R in CH1 of H2 and S114D/E in CL of L2, respectively;
(2) T187D/E in CH1 of H1 and D/N170K/R in CL of L1, respectively, and T187K/R in CH1 of H2 and D/N170D/E in CL of L2, respectively;
(3) S131D/E in CH1 of H1 and P119K/R in CL of L1, respectively, and S131K/R in CH1 of H2 and P119D/E in CL of L2, respectively;
(4) A129D/E in CH1 of H1 and S121K/R in CL of L1, respectively, and A129K/R in CH1 of H2 and S121D/E in CL of L2, respectively;
(5) K/R133D/E in CH1 of H1 and K207K/R in CL of L1, respectively, and K/R133K/R in CH1 of H2 and K207D/E in CL of L2, respectively;
(6) K/R133D/E in CH1 of H1 and I/L117K/R in CL of L1, respectively, and K/R133K/R in CH1 of H2 and I/L117D/E in CL of L2, respectively;
(7) K/R133D/E in CH1 of H1 and F/V209K/R in CL of L1, respectively, and K/R133K/R in CH1 of H2 and F/V209D/E in CL of L2, respectively;
(8) G166D/E in CH1 of H2 and S114K/R in CL of L2, respectively, and G166K/R in CH1 of H1 and S114D/E in CL of L1, respectively (claim 17).
Regarding claims 10-11 and 13, the copending claims teach The isolated bi specific antibody or antigen-binding fragment thereof of claim 12, wherein Ab I binds an immune cell modulator (ICM) (claim 13), wherein the ICM is CD3 (claim 14), the isolated bispecific antibody or antigen-binding fragment thereof of claim 12, wherein Ab2 binds a tumor-associated antigen (TAA) (claim 15), wherein the TAA is DLL3 (claim 16).
Regarding claims 12 and 14, Li teaches the isolated bispecific antibody or antigen binding fragment thereof comprising 1) a first antigen-binding arm (Abl) comprising a VH region having the polypeptide sequence of SEQ ID NO: 15, a VL region having the polypeptide sequence of SEQ ID NO: 17, a CHI region having [[a]] the polypeptide sequence of SEQ ID NO: 16, and a CL region having the polypeptide sequence of SEQ ID NO: 18; 2) a first antigen-binding arm (Abl) comprising a VH region having the polypeptide sequence of SEQ ID NO: 19 (claim 18). SEQ ID NO: 19, 16, 17 and 18 having 100% sequence identity to the instant claimed SEQ ID NO: 9, 10, 11 and 12 respectively.
Regarding claim 14, Li teaches the isolated bispecific antibody or antigen-binding fragment thereof of claim 18, wherein the second antigen-binding arm (Ab2) comprises a VH region having the polypeptide sequence of SEQ ID NO:23, a VL region having the polypeptide sequence of SEQ ID NO:25, a CHI region having the polypeptide sequence of SEQ ID NO:24, and a CL region having the polypeptide sequence of SEQ ID NO:26 (claim 19). SEQ ID NO: 23-26 have 100% sequence identity to the instant claimed SEQ ID NO: 13-16 respectively.
Regarding claim 15, Li teaches an isolated nucleic acid encoding the isolated antibody or antigen-binding fragment thereof of claim 1 (claim 27).
Regarding claim 16, Li teaches a vector comprising the isolated nucleic acid of claim 27 (claim 28).
Regarding claim 17, Li teaches an isolated host cell comprising the vector of claim 28 (claim 29).
Regarding claim 18, Li teaches a pharmaceutical composition comprising the isolated antibody or antigen-binding fragment thereof of claim of 1, and a pharmaceutically acceptable carrier (claim 30).
Regarding claims 19-20, Li teaches a method of treating a cancer in a subject in need thereof, the method comprising administering to the subject the pharmaceutical composition of claim 30 (claim 31), wherein the cancer is selected from the group consisting of a lung cancer, a gastric cancer, an esophageal cancer, a bile duct cancer, a cholangiocarcinoma, a colon cancer, a hepatocellular carcinoma, a renal cell carcinoma, a bladder urothelial carcinoma, a metastatic melanoma, a breast cancer, an ovarian cancer, a cervical cancer, a head and neck cancer, a pancreatic cancer, a glioma, a glioblastoma, and other solid tumors, and a non-Hodgkin's lymphoma (NHL), an acute lymphocytic leukemia (ALL), a chronic lymphocytic leukemia (CLL), a chronic myelogenous leukemia (CML), a multiple myeloma (MM), an acute myeloid leukemia (AML), and other liquid tumors (claim 32).
Regarding claim 21, Li teaches a method of producing the isolated antibody or antigen-binding fragment thereof of claim 1, the method comprising culturing a cell comprising a nucleic acid encoding the antibody or antigen-binding fragment thereof under conditions to produce the antibody or antigen-binding fragment thereof, and recovering the antibody or antigen-binding fragment thereof from the cell or culture (claim 33).
Regarding claim 22, Li teaches a method of producing a pharmaceutical composition comprising the isolated antibody or antigen-binding fragment thereof of claim 1, the method comprising combining the antibody or antigen-binding fragment thereof with a pharmaceutically acceptable carrier to obtain the pharmaceutical composition (claim 35).
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Li (US 2023/0089926 A1; PTO-892) as applied to claims 1-3 and 10-22 above, and further in view of Dillon (mAbs, 9(2), 213–230; PTO-892).
The teachings of Li regarding claims 1-3 and 10-22 are detailed above.
Li does not teach that the VL region of L1 have a Q39E and a Q38K substitution respectively and the VL region of L2 have a Q39K and a Q38E substitution mutation respectively.
Dillon teaches that bispecific IgG production in single host cells has been a much sought-after goal to support the clinical development of these complex molecule (abstract). Dillon further teaches that for efficient orthogonal Fab pairing changes, it can be advantageous to combine variable and constant domain mutations such as a conserved hydrogen bond between the variable domains involving VH Q39 and VL Q38 (page 218, col 1, para 2) and further that as these residues are distal to the complementary-determining regions (CDRs), little effect upon antigen binding affinity was seen (table 4). Dillon further teaches that these positions minimize LC homodimer and improve orthogonal Fab designs for single-cell BsIgG (page 218, col 1, para 2). Dillon further teaches that the variant, VL Q38E, negatively affected antibody assembly (Fig. 2D) but that this assembly defect was rescued with the VH Q39K variant (page 218, col 1, para 2).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the instant application to add charge pair mutations in the VL region of the bispecific as taught by Dillon to the bispecific antibody with engineered charge pair mutations in the constant regions as taught by Li. The ordinary artisan would have been motivated to do so because Li teaches that it is advantageous to combine variable and constant domain mutations such as a conserved hydrogen bond between the variable domains involving VH Q39 and VL Q38 to support bispecific IgG production in single host cells. The ordinary artisan has a reasonable expectation of success to add Q39E and Q38K mutations in the VL of L1 and L2 to improve bispecific antibody production in a single cell.
The rationale to apply a technique taught by the prior art as improving the therapeutic and production characteristics of a similar construct is to predictably obtain an improvement to the second construct and is consistent with the exemplary rationales provided by the Supreme Court in KSR International Co. v. Teleflex Inc., 82 USPQ2d 1385, 1395-97 (2007) and discussed in M.P.E.P. § 2143. For these reasons, the invention as a whole would have been prima facie obvious to one ordinary skill in the art before the effective filing date of the claimed invention.
Claims 6-9 are rejected under 35 U.S.C. 103 as being unpatentable over Li (US 2023/0089926 A1; PTO-892) as applied to claims 1-3 and 10-22 above, and further in view of Wang (WO 2019/217145 A1; PTO-892) and Wang hereafter “Zou” for clarity of the record (WO 2019/173420 A1; PTO-892).
The teachings of Li regarding claims 1-3 and 10-22 are detailed above.
Li does not teach that the ICM target is CD47 or that the TAA is CLDN18.2.
Regarding claims 6 and 8, Wang teaches that an anti-CD47 antibody can be used to induce macrophage-mediated phagocytosis of cancer cells that express both a TAA and CD47 (para 0031). Wang further teaches an isolated anti-CD47 monoclonal antibody or antigen-binding fragment thereof comprising a humanized heavy chain variable region of an anti-CD47 monoclonal antibody and a humanized light chain variable region of an anti-DLL3 monoclonal antibody, wherein the anti-CD47 monoclonal antibody or antigen-binding fragment thereof comprises: (e) a heavy chain variable region having the polypeptide sequence of SEQ ID NO: 176, and a light chain variable region having the polypeptide sequence of SEQ ID NO: 172 (claim 9). SEQ ID NO: 176 has 100% sequence identity to the instant claimed SEQ ID NO: 1 and SEQ ID NO: 172 has 100% sequence identity to the instant claimed SEQ ID NO: 2.
Regarding claims 7 and 9, Zou teaches that CLDN18.2 is an ideal target for precision-guided, anti-cancer biologies to CLDN18.2-positive tumors, as CLDN18.2 is not expressed in any normal tissue other than the differentiated gastric epithelial cells, which are unreachable by large molecule compounds administrated intravenously (para 0005). Zou further teaches an isolated monoclonal antibody or antigen-binding fragment thereof wherein the antibody or antigen-binding fragment thereof specifically binds claudin 18.2 (CLDN18.2), preferably human CLDN18.2 (claim 1), wherein the isolated humanized antibody or antigen-binding fragment thereof comprises: (k) a heavy chain variable region having the polypeptide sequence of SEQ ID NO: 151, and a light chain variable region having the polypeptide sequence of SEQ ID NO: 153 (claim 8). SEQ ID NO: 151 and 153 have 100% sequence identity to the instant claimed SEQ ID NO: 3 and 4 respectively.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the instant application to use CD47 as the ICM as taught by Wang and CLDN18.2 as taught by Zou in the bispecific antibody with engineered charge pair mutations in the constant regions as taught by Li. The ordinary artisan would have been motivated to do so because the engineered charge pairs in the constant region of the bispecific can be applied to any ICM/ TAA targets to improve immunotherapy production, Wang teaches that an anti-CD47 antibody can be used to induce macrophage-mediated phagocytosis of cancer cells and Zou teaches that CLDN18.2 is an ideal target for precision-guided, anti-cancer biologies to CLDN18.2-positive tumors. The ordinary artisan has a reasonable expectation of success use CD47 x CLDN18.2 to produce a bispecific immunotherapy with engineered charge pairs in the constant domain.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-3 and 10-22 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1, 11-19, 27-33, and 35 of copending Application No. 17/760,394 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claims 1-3, the copending claims teach an isolated multi-specific antibody (claim 11 and 1), wherein the multi-specific antibody is a bispecific antibody (claim 12), wherein the first antigen-binding arm (Abl) comprises HI and LI and a second antigen-binding arm (Ab2) comprises H2 and L2, wherein
(a) HI and H2 each comprises a CHI region of human IgGl, IgG2, IgG3, or IgG4; and
(b) LI and L2 each comprises a CL region of a human kappa light chain or a human lambda light chain;
wherein HILI and H2L2 each comprise a charge pair selected from the group consisting of the following amino acid substitutions:
(1) Gl66D/E in CHI of HI and S114K/R in CL of LI, respectively, and Gl66K/R in CHI of H2 and SI 14D/E in CL ofL2, respectively;
(2) Tl87D/E in CHI of HI and DINI 70K/R in CL of LI, respectively, and Tl87K/R in CHI ofH2 and DINI 70D/E in CL ofL2, respectively;
(3) Sl31D/E in CHI of HI and Pl 19K/R in CL of LI, respectively, and Sl31K/R in CHI of H2 and Pl 19D/E in CL ofL2, respectively;
(4) Al29D/E in CHI of HI and Sl21K/R in CL of LI, respectively, and Al29K/R in CHI of H2 and Sl21D/E in CL ofL2, respectively;
(5) K/R133D/E in CHI of HI and K207K/R in CL of LI, respectively, and K/R133K/R in CHI ofH2 and K207D/E in CL ofL2, respectively;
(6) K/R133D/E in CHI of HI and I/LI l 7K/R in CL of LI, respectively, and K/R133K/R in CHI ofH2 and I/LI l 7D/E in CL ofL2, respectively;
(7) K/R133D/E in CHI of HI and F/V209K/R in CL of LI, respectively, and K/R133K/R in CHI ofH2 and F/V209D/E in CL ofL2, respectively;
(8) Gl66D/E in CHI ofH2 and S114K/R in CL ofL2, respectively, and Gl66K/R in CHI of HI and SI 14D/E in CL of LI, respectively (claim 17).
Regarding claims 10-11 and 13, the copending claims teach The isolated bi specific antibody or antigen-binding fragment thereof of claim 12, wherein Ab I binds an immune cell modulator (ICM) (claim 13), wherein the ICM is CD3 (claim 14), the isolated bispecific antibody or antigen-binding fragment thereof of claim 12, wherein Ab2 binds a tumor-associated antigen (TAA) (claim 15), wherein the TAA is DLL3 (claim 16).
Regarding claims 12 and 14, the copending claims teach the isolated bispecific antibody or antigen binding fragment thereof comprising 1) a first antigen-binding arm (Abl) comprising a VH region having the polypeptide sequence of SEQ ID NO: 15, a VL region having the polypeptide sequence of SEQ ID NO: 17, a CHI region having [[a]] the polypeptide sequence of SEQ ID NO: 16, and a CL region having the polypeptide sequence of SEQ ID NO: 18; 2) a first antigen-binding arm (Abl) comprising a VH region having [[a]] the polypeptide sequence of SEQ ID NO: 19 (claim 18). SEQ ID NO: 19, 16, 17 and 18 having 100% sequence identity to the instant claimed SEQ ID NO: 9, 10, 11 and 12 respectively.
Regarding claim 14, the copending claims teach he isolated bispecific antibody or antigen-binding fragment thereof of claim 18, wherein the second antigen-binding arm (Ab2) comprises a VH region having the polypeptide sequence of SEQ ID NO:23, a VL region having the polypeptide sequence of SEQ ID NO:25, a CHI region having the polypeptide sequence of SEQ ID NO:24, and a CL region having the polypeptide sequence of SEQ ID NO:26 (claim 19). SEQ ID NO: 23-26 have 100% sequence identity to the instant claimed SEQ ID NO: 13-16 respectively.
Regarding claim 15, the copending claims teach an isolated nucleic acid encoding the isolated antibody or antigen-binding fragment thereof of claim 1 (claim 27).
Regarding claim 16, the copending claims teach A vector comprising the isolated nucleic acid of claim 27 (claim 28).
Regarding claim 17, the copending claims teach An isolated host cell comprising the vector of claim 28 (claim 29).
Regarding claim 18, the copending claims teach A pharmaceutical composition comprising the isolated antibody or antigen-binding fragment thereof of claim of 1, and a pharmaceutically acceptable carrier (claim 30).
Regarding claims 19-20, the copending claims teach A method of treating a cancer in a subject in need thereof, the method comprising administering to the subject the pharmaceutical composition of claim 30 (claim 31), wherein the cancer is selected from the group consisting of a lung cancer, a gastric cancer, an esophageal cancer, a bile duct cancer, a cholangiocarcinoma, a colon cancer, a hepatocellular carcinoma, a renal cell carcinoma, a bladder urothelial carcinoma, a metastatic melanoma, a breast cancer, an ovarian cancer, a cervical cancer, a head and neck cancer, a pancreatic cancer, a glioma, a glioblastoma, and other solid tumors, and a non-Hodgkin's lymphoma (NHL), an acute lymphocytic leukemia (ALL), a chronic lymphocytic leukemia (CLL), a chronic myelogenous leukemia (CML), a multiple myeloma (MM), an acute myeloid leukemia (AML), and other liquid tumors (claim 32).
Regarding claim 21, the copending claims teach A method of producing the isolated antibody or antigen-binding fragment thereof of claim 1, the method comprising culturing a cell comprising a nucleic acid encoding the antibody or antigen-binding fragment thereof under conditions to produce the antibody or antigen-binding fragment thereof, and recovering the antibody or antigen-binding fragment thereof from the cell or culture (claim 33).
Regarding claim 22, the copending claims teach A method of producing a pharmaceutical composition comprising the isolated antibody or antigen-binding fragment thereof of claim 1, the method comprising combining the antibody or antigen-binding fragment thereof with a pharmaceutically acceptable carrier to obtain the pharmaceutical composition (claim 35).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
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/AMBER K FAUST/Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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