Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
2. Applicant’s amendment filed on 12/22/2025 is acknowledged.
3. Claims 1, 15-20, 26, 30, 32, 38, 44-47, 50, 54, 56 and 58-59 are pending.
4. Applicant’s election without traverse of Group I, claims 1, 15-20, 56 and 58-59 in the reply filed on 12/22/2025 is acknowledged. The Examiner has withdrawn the species election.
5. Claims 26, 30, 32, 38, 44-47, 50 and 54 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 12/22/2025.
6. Claims 1, 15-20, 56 and 58-59 are under consideration for their full scope.
7. Applicant’s IDS documents filed on 07/23/2024 and 12/22/2025 have been considered.
8. The disclosure is objected to because of the following informalities:
The two sequences on pages 5-6 in paragraph [0027] are missing their sequence identifiers.
Appropriate correction is required.
9. 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.
10. Claims 1, 15-20, 56 and 58-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-58 of U.S. Patent No.9,334,332 (PTO-892; Reference A). Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-58, and particularly claims 19 and 38-57 are directed to:
an antibody that binds to KIT which comprises SEQ ID NO:18 of instant claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of instant claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of instant claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of instant claim 59.
The reference also claims wherein the antibody comprises an Fc region of a human IgG1 (reference claim 28 and 37); which is a monoclonal antibody (reference claim 8); which is an antigen-binding fragment or a Fab fragment (reference claim 9); which is a bispecific antibody or antigen-binding fragment thereof (reference claim 10); which is fused to a heterologous polypeptide (reference claim 11); and which is a conjugate linked to an agent (reference claim 12).
The reference sequences and SEQ ID NOs are identical to those the instant application.
The reference teachings anticipate the claimed invention.
11. Claims 1, 15-20, 56 and 58-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8 of U.S. Patent No.9,605,081 (PTO-892; Reference B) in view of U.S. Patent 9,334,332 (PTO-892; Reference A). Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-58, and particularly claims 19 and 38-57 are directed to nucleic acids encoding the following:
an antibody that binds to KIT which comprises SEQ ID NO:18 of instant claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of instant claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of instant claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of instant claim 59.
The reference sequences and SEQ ID NOs are identical to those the instant application.
The claimed invention differs from the prior art in the recitation of the antibodies; and wherein the antibody comprises an Fc region of a human IgG1; which is a monoclonal antibody; which is an antigen-binding fragment or a Fab fragment; which is a bispecific antibody or antigen-binding fragment thereof; which is fused to a heterologous polypeptide; and which is a conjugate linked to an agent of instant claims 15-20.
U.S. Patent 9,334,332 has been discussed supra.
It would have been obvious to one of ordinary skill in the art at the time of invention to have produced the antibody which is encoded by the nucleic acids of U.S. Patent 9,605,081. It would have been obvious in view of the teachings of U.S. Patent 9,334,332 to make an antibody wherein the antibody comprises an Fc region of a human IgG1 (reference claim 28 and 37); which is a monoclonal antibody (reference claim 8); which is an antigen-binding fragment or a Fab fragment (reference claim 9); which is a bispecific antibody or antigen-binding fragment thereof (reference claim 10); which is fused to a heterologous polypeptide (reference claim 11); and which is a conjugate linked to an agent (reference claim 12).
From the combined teachings of the reference, it is apparent that one of ordinary skill in the art would have had a reasonable expectation of success in producing the claimed invention. Therefore, the invention as a whole was prima facie obvious to one of ordinary skill in the art at the time the invention was made, as evidenced by the reference, especially in the absence of evidence to the contrary.
12. Claims 1, 15-20, 56 and 58-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No.10,184,007 (PTO-892; Reference C). Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-20, are directed to a method of administering or contacting a cell with:
an antibody that binds to KIT which comprises SEQ ID NO:18 of instant claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of instant claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of instant claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of instant claim 59.
The reference also claims wherein the antibody comprises an Fc region of a human IgG1 (reference claim 9); which is a monoclonal antibody (reference claim 10); which is an antigen-binding fragment or a Fab fragment (reference claim 11); which is a bispecific antibody or antigen-binding fragment thereof (reference claim 12); which is fused to a heterologous polypeptide (reference claim 13); and which is a conjugate linked to an agent (reference claim 14).
The reference sequences and SEQ ID NOs are identical to those the instant application.
The reference teachings anticipate the claimed invention.
13. Claims 1, 15-20, 56 and 58-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-22 of U.S. Patent No.10,781,267 (PTO-892; Reference D). Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-22, are directed to a method of administering:
an antibody that binds to KIT which comprises SEQ ID NO:18 of instant claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of instant claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of instant claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of instant claim 59.
The reference also claims wherein the antibody comprises an Fc region of a human IgG1 (reference claim 8); which is a monoclonal antibody (reference claim 9); which is an antigen-binding fragment or a Fab fragment (reference claim 10); which is a bispecific antibody or antigen-binding fragment thereof (reference claim 11); which is fused to a heterologous polypeptide (reference claim 12); and which is a conjugate linked to an agent (reference claim 13).
The reference sequences and SEQ ID NOs are identical to those the instant application.
The reference teachings anticipate the claimed invention.
14. Claims 1, 15-20, 56 and 58-59 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No.11,891,452 (PTO-892; Reference E). Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-20, are directed to a method of administering:
an antibody that binds to KIT which comprises SEQ ID NO:18 of instant claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of instant claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of instant claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of instant claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of instant claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of instant claim 59.
The reference also claims wherein the antibody comprises an Fc region of a human IgG1 (reference claim 9); which is a monoclonal antibody (reference claim 10); which is an antigen-binding fragment or a Fab fragment (reference claim 11); which is a bispecific antibody or antigen-binding fragment thereof (reference claim 12); which is fused to a heterologous polypeptide (reference claim 13); and which is a conjugate linked to an agent (reference claim 14).
The reference sequences and SEQ ID NOs are identical to those the instant application.
The reference teachings anticipate the claimed invention.
15. 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.
16. Claims 1, 15-20, 56 and 58-59 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.
Applicant is in possession of: antibodies which bind to KIT and which comprise all 6 CDRs of the Hum1-Hum20 antibodies disclosed in Table 4 (comprising a variable heavy chain of SEQ ID NOs 2-6 and a variable light chain of SEQ ID NOs 7-10).
Applicant is not in possession of: antibodies which bind to KIT that comprise variants of the 6 CDRS of the Hum1-Hum20 antibodies disclosed in Table 4 (comprising a variable heavy chain of SEQ ID NOs 2-6 and a variable light chain of SEQ ID NOs 7-10); and antibodies that comprise less than all 6 CDRs of the Hum1-Hum20 antibodies disclosed in Table 4 of claims 1, 56, 58-59 and claims dependent thereupon.
The specification describes the Hum1-Hum20 antibodies disclosed in Table 4 comprising a variable heavy chain of SEQ ID NOs 2-6 and a variable light chain of SEQ ID NOs 7-10.
The specification has not adequately described:
an antibody that binds to KIT which comprises SEQ ID NO:18 of claim 1
an antibody that binds to KIT which comprises SEQ ID NO:58 of claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:63 of claim 56;
an antibody that binds to KIT which comprises SEQ ID NO:72 of claim 56;
an antibody that binds to KIT which comprises SEQ ID NOs 16-19 and 21 of claim 58;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21 and 56-58 of claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 56, 59 and 61-63 of claim 59;
an antibody that binds to KIT which comprises SEQ ID NOs 19, 21, 58 and 64-65 of claim 59; and
an antibody that binds to KIT which comprises SEQ ID NOs 66, 68 and 70-72 of claim 59.
The claims encompass antibodies with variants of the recited amino acid sequences. The claims recite variable region sequences containing amino acids not found in the Hum1-Hum20 antibodies that were actually produced in the specification which actually binds KIT. The skilled artisan cannot envision all the antibody and method possibilities recited in the instant claims.
Consequently, conception cannot be achieved until a representative description of the structural and functional properties of the claimed invention has occurred, regardless of the complexity or simplicity of the method.
The specification must set forth the structural features that allow one of ordinary skill in the art to identify and produce the recited antibodies. In the instant case, definition by function does not suffice to define the genus because it is only an indication of what the antibodies do, rather than what they are.
It is well established in the art that it is highly unpredictable which changes in amino acid sequence can be made in complementarity determining regions (CDRs) of a parental antibody such that the derived antibody retains the binding specificity and affinity of the parent antibody. The art of Mariuzza et al. (PTO-892; Reference U) reviews the structural basis of antigen-antibody recognition and teaches that a naturally occurring antibody comprises light and heavy chains. The antigen-combining site of an antibody is a three-dimensional structure, which fully comprises six "complementarity-determining regions" (CDRs), three each from the light and heavy chains. The amino acid sequences of the CDRs are hypervariable, as the amino acid residues contained within the CDRs determine much of antibody's antigen-binding specificity. Of the amino acid residues of the antibody contacting the antigen, six are within the light chain, nine are within the heavy chain, and two are within the constant or nearly constant "framework" regions (In particular, whole document). As such, one of skill in the art would not know which of the recited antibody variants would have the claimed function of binding to KIT because it is the 6 CDRs together which determine the antibody's antigen-binding specificity.
It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. MacCallum, et al. (PTO-892; Reference V) analyzed many different antibodies for interactions with antigen and state that although CDR3 of the heavy and light chain dominate, a number of residues outside the standard CDR definitions make antigen contacts (see page 733, right column) and non-contacting residues within the CDRs coincide with residues as important in defining canonical backbone conformations (see page 735, left column). De Pascalis, et al.
(PTO-892; Reference W) demonstrate that grafting of the CDRs into a human framework was performed by grafting CDR residues and maintaining framework residues that were deemed essential for preserving the structural integrity of the antigen binding site (see page
3079, right column). Although abbreviated CDR residues were used in the constructs, some residues in all 6 CDRs were used for the constructs (see page 3080, left column). Thus it is unpredictable as to what amino acids can be changed in the original intact antibodies disclosed in the specification wherein the antibodies would still function. Thus, the skilled artisan cannot envision the detailed structure of the encompassed invention and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation.
It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function.
As evidenced by the art of Goel et al. (IDS filed on 07/23/2024; Reference C132), Kahn et al. (PTO-892; Reference X) and Poosarla et al. (PTO-892; Page 2; Reference U), antibody specificity for a particular antigen does not correlate with any particular structure for the antibodies themselves. It was well known to those skilled in the art at the time the invention was made that minor structural differences among structurally related antibodies or compositions thereof could result in substantially different binding activities. Given the lack of guidance in the specification, it is unpredictable which antibodies with which structures would exhibit the recited functions. The specification does not disclose a correlation between the structure of the antibodies themselves and their function of binding KIT such that a skilled artisan would have known what antibody structures possess the claimed functions.
The specification does not disclose a correlation between the antibody structure and the function of binding KIT such that a skilled artisan would have known what antibody variants possess the claimed function. "Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features" Ex parte Kubin (83 U.S.P.Q.2d 1410 (BPAI 2007)), at page 16. In this instant case, Applicants have not provided the requisite identifying structural features of the antibodies encompassed. "Without a correlation between structure and function, the claim does little more than define the claimed invention by function" supra, at page 17.
U.S. Court of Appeals for the Federal Circuit recently decided Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017) which concerned adequate written description for claims drawn to antibodies. The Federal Circuit explained in Amgen that when an antibody is claimed,
35 U.S.C. § 112(a) requires adequate written description of the antibody itself. Amgen, 872 F.3d at 1378-79. The Amgen court expressly stated that the so-called "newly characterized antigen"
test, which had been based on an example in USPTO-issued training materials and was noted in dicta in several earlier Federal Circuit decisions, should not be used in determining whether there is adequate written description under 35 U.S.C. § 112(a) for a claim drawn to an antibody. Citing its decision in Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co. , the court also stressed that the "newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. Amgen, 872
F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345
(Fed. Cir. 2010). In view of the Amgen decision, adequate written description of a newly\ characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional. Id.
The specification does not provide adequate written description of the claimed invention.
The legal standard for sufficiency of a patent's (or a specification's) written description is whether that description "reasonably conveys to the artisan that the inventor had possession at that time of the. . .claimed subject matter", Vas-Cath, Inc. V. Mahurkar, 19 U.S.P.Q.2d 1111
(Fed. Cir. 1991). In the instant case, the specification does not convey to the artisan that the applicant had possession at the time of invention of the claimed invention.
Adequate written description requires more than a mere statement that it is part of the invention and a reference to a potential method of isolating it. In the instant application, the amino acid sequence itself or isolated protein is required. See Fiers v. Revel, 25 USPQ 2d 1601 at 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Lts., 18 USPQ2d 1016. In view of the aforementioned problems regarding description of the claimed invention, the specification does not provide an adequate written description of the invention claimed herein.
See The Regents of the University of California v. Eli Lilly and Company, 43 USPQ2d 1398,
1404-7 (Fed. Cir. 1997). In University of California v. Eli Lilly and Co., 39 U.S.P.Q.2d 1225
(Fed. Cir. 1995) the inventors claimed a genus of DNA species encoding insulin in different vertebrates or mammals, but had only described a single species of cDNA which encoded rat insulin. The court held that only the nucleic acids species described in the specification (i.e. nucleic acids encoding rat insulin) met the description requirement and that the inventors were not entitled to a claim encompassing a genus of nucleic acids encoding insulin from other vertebrates, mammals or humans, id. at 1240. The Federal Circuit has held that if an inventor is "unable to envision the detailed constitution of a gene so as to distinguish it from other materials.
. .conception has not been achieved until reduction to practice has occurred", Amgen, Inc. v.
Chugai Pharmaceutical Co, Ltd., 18 U.S.P.Q.2d 016 (Fed. Cir. 1991). Attention is also directed to the decision of The Regents of the University of California v. Eli Lilly and Company (CAFC,
July 1997) wherein is stated: "The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 222 USPQ 369, 372-373 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.").
Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material. Thus, as we have previously held, a cDNA is not defined or described by the mere name "cDNA," even if accompanied by the name of the protein that it encodes, but requires a kind of specificity usually achieved by means of the recitation of the sequence of nucleotides that make up the cDNA." See
Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606.
As such, there is insufficient written description of the required kind of structure identifying information about the corresponding makeup of the claimed antibodies to demonstrate possession.
17. No claim is allowed.
18. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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January 27, 2026
/Nora M Rooney/
Primary Examiner, Art Unit 1641