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 .
Election/Restrictions
Applicant’s election without traverse of Group I and species which is a-b (CCR8) in the reply filed on 10/22/2025 is acknowledged.
Due to an obvious typographical error, Group I should have included claims 1, 3, 4, 7, 8, 15-18 and 26, while Group II should have included claims 18-25. Because the first method of use of Group I was “a method of using the polypeptide for immunization to make an antibody thereto” and Group II was “a method of obtaining an antibody by using the polypeptide to pan an antibody library”, claims 19-21, which are all drawn to panning an antibody library (part (b) of claim 18), should have been part of Group II instead of Group I.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
The antibody CDR sequences in Tables 7.1, 7.2 b, and 7.3 do not have sequence identifiers.
Also, peptide sequences in Table 10.1.3.1 (p. 235), fall under the requirements for identification by sequence identifier, with sulfation indicated according to the key in Appendix F of 37 CFR 1.821 and 1.822 (MPEP 2422(I)).
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Specification
All references to location in the specification are in reference to the clean substitute specification filed 12/22/2022.
The disclosure is objected to because of the following informalities:
1) The specification refers to Example 5 in three locations (p. 69, 78 and 221), but there is no Example 5.
2) It is noted that the statement added by preliminary amendment (12/22/2022) to be the first paragraph of the specification and entitled “Sequence Listing Submission” was not required because the CRF was an official part of the international application and Sequence Listing was part of the PCT application which serves as a basis for this national stage filing (see MPEP 2422.03(I) and see form PTO-1390, transmittal letter concerning submission under 35 USC 371 dated 12/22/2022). However, in view of the inclusion of the information and incorporation thereof, the file name and size (not the creation date) must be corrected as set forth below:
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Appropriate correction is required.
Trade Name or a Mark
The use of the term “Tween” (p. 223, paragraph beginning line 20), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Abstract
Applicant is reminded of the proper content of an abstract of the disclosure.
A patent abstract is a concise statement of the technical disclosure of the patent and should include that which is new in the art to which the invention pertains. The abstract should not refer to purported merits or speculative applications of the invention and should not compare the invention with the prior art.
If the patent is of a basic nature, the entire technical disclosure may be new in the art, and the abstract should be directed to the entire disclosure. If the patent is in the nature of an improvement in an old apparatus, process, product, or composition, the abstract should include the technical disclosure of the improvement. The abstract should also mention by way of example any preferred modifications or alternatives.
Where applicable, the abstract should include the following: (1) if a machine or apparatus, its organization and operation; (2) if an article, its method of making; (3) if a chemical compound, its identity and use; (4) if a mixture, its ingredients; (5) if a process, the steps.
Extensive mechanical and design details of an apparatus should not be included in the abstract. The abstract should be in narrative form and generally limited to a single paragraph within the range of 50 to 150 words in length.
See MPEP § 608.01(b) for guidelines for the preparation of patent abstracts.
The instant abstract refers to the purported merit of the generated antibodies with “other favorable properties”. Also, it is over 200 words in length.
Claim Objections
Claim 26 is objected to because of the following informalities: In claim 26 in “a HCDR3 region comprising between 10 and 34% of tyrosine and/or between 2 and 20% of histidine,” use of “of” before the amino acid name does not contribute to the claim’s clarity. It is suggested that, for example, “of tyrosine” be replaced with “tyrosine residues” and the same for “of histidine” (see p. 7, line 29, e.g., for basis).
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 26 and dependent claims 3, 4, 7, 8 and 16-18 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 1 recites the broad recitation at “least two” (in reference to sulfated tyrosines), and the claim also recites “all” which is the narrower statement of the range/limitation. The claim(s) are considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims. If at least two tyrosines are sulfated, then this encompasses all tyrosines being sulfated.
Regarding claim 26, the phrase "preferably" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 26 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 26 depends from claim 18, which is drawn to a method of obtaining or generating an antibody or fragment thereof that specifically binds the isolated polypeptide or conjugate thereof of claim 1 by immunizing a suitable animal with the isolated polypeptide or conjugate, generating hybridoma cells from the immunized animal, screening antibodies produced by the hybridoma cells of an antibody that specifically binds to the isolated polypeptide or conjugate thereof, and isolating the antibody. Claim 18 also recites the antibody may be obtained by panning an antibody library with the isolated polypeptide or conjugate. While the method of immunization was well-known and it was recognized by those skilled in the art that it could be practice with most polypeptides or conjugates thereof, the antibody product is particular to the antigen and animal immunized. The specification states (end of Example.3) that “In summary, antibodies specifically recognizing human CC chemokine receptors are rare for some members of this target class. The low rates are in line with results from further commercially available antibodies sold for human chemokine receptors.” The instant specification describes panning of phage display libraries to obtain the antibody (e.g., Examples 6-8). It also describes a limited number of antibodies obtained by the panning method. Only two antibodies binding specifically only to sulfated mouse CCR8 (end of Example 8) and a small number of antibodies binding sulfated human and/or cynomolgus CCR8 (Tables 10.1.3.1. and 10.2.1) were identified. There is insufficient disclosure to show the inventors were in possession of a method of claim 18 wherein the antibodies obtained thereby had one or more properties of claim 26, especially for those properties which have a narrower breadth, e.g., cross reactive for a human and cynomolgus seven transmembrane receptor and is a non-internalizing antibody. The skilled artisan could not readily envision the encompassed antibodies of claim 26 and would not on the basis of sequence have been able to distinguish an antibody that did or did not meet the limitations of claim 26. As stated in MPEP 2163(I)(A), “An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function.“ While the inventors recognized that heavy chain variable region CDR3 (HCDR) in the antibodies binding human CCR8 had a substantially higher number of tyrosine residues than would be expected for a random fully human HCDR3 of the same length (Example 9, p. 231, lines 6-11), this does not give a description of the light chain CDRs or HCDR1 or -2, or even what other amino acids in addition to the tyrosines and in what positions they can occur in HCDR3 in combination with the other CDRs to be part of an antibody that binds the sulfated polypeptide of claim 1. Claim 26 puts limitations on the antibody produced by the method for which the specification does not provide written description commensurate in scope with the genus of antibodies encompassed.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111 (Fed. Cir. 1991), clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116).
With the exception of the antibodies meeting the limitations of claim 26 which are disclosed in the specification, the skilled artisan cannot envision the detailed chemical structure of the encompassed polynucleotides, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016 (Fed. Cir. 1991). Applicant has not disclosed relevant identifying characteristics, such as structure or other physical and/or chemical properties common to all encompassed antibodies, sufficient to show possession of the claimed genus, i.e., a structure-function correlation. Mere idea or function is insufficient for written description; isolation and characterization at a minimum are required. A description of what a material does, rather than what it is, usually does not suffice. Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483 (BPAI 1993). In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence.
Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. § 112 is severable from its enablement provision (see page 1115).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 3, 4, 7, 8, 16-18 and 26 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 31, 38-41 and 51-54 of copending Application No. 18/666,512 (‘512, reference application) in view of Hoffhines et al. (J. Biol. Chem. 281(49):37877-37887, 2006, cited in the IDS filed 2/3/2023) and Bunschoten et al. (Chem. Commun. 21:2999-3001, 2009, cited in the IDS filed 2/3/2023).
Although the claims at issue are not identical, they are not patentably distinct from each other because both applications recite a sulfated polypeptide or conjugate thereof comprising a TRD of CCR8 and comprising one of sequences SEQ ID NO:43-48, wherein: in SEQ ID NO:46 or SEQ ID NO:47, at least two or all of Y3, Y15 and Y17 have been sulfated, or in SEQ ID NO:48, at least two or all of Y3, Y14 and Y15 have been sulfated (instant claim 1 and claims 41 and 54 of ‘512). SEQ ID NO:43-45 are comprised by SEQ ID NO:46-48, respectively. These sequences are identical between the two applications, including the substitution of the cysteine between the TRD and LID (represented by Xaa, which can be any amino acid). Both recite an antibody that binds the polypeptide or conjugate thereof, including an antibody that binds human CCR8 or that is cross reactive and binds one or both of mouse and cynomolgus CCR8 (claims 31, 38-40, 51-53 of ‘512, and instant claim 26). ‘512 does not claim wherein the antibody is generated or obtained by any particular method or the polypeptide or conjugate to which the antibody binds is immobilized.
Hoffhines et al. teaches a method of generating antibodies that binds sulfated proteins by panning a single chain Fv (scFv) phagemid library. The target protein was immobilized for this purpose (p. 37878, paragraph bridging cols. 1-2).
Bunschoten et al. teaches a method of synthesizing specifically sulfated G protein-coupled receptor peptides, including the N-terminal peptide of the C5a receptor that comprises two tyrosine residues (p. 2999).
It would have been obvious to the artisan of ordinary skill before the effective filing date of the instant application to have immobilized the sulfated CCR8 TRD-containing polypeptide, e.g., of SEQ ID NO:46, in order to use it in a method of panning a phagmid antibody display library to obtain antibodies that bound the sulfated polypetide, as taught for a different sulfated polypeptide by Hoffhines et al. Additionally, it would have been obvious wherein the polypeptide or polypeptide of the conjugate was synthesized as a sulfated polypeptide by the method of Bunschoten et al., which was successful for an N-terminal tyrosine-containing portion of a similarly structured receptor, i.e., a seven-transmembrane receptor.
This is a provisional nonstatutory double patenting rejection.
Prior Art
The prior art made of record and not relied upon is considered pertinent to Applicant's disclosure.
US 2021/0238292 A1 (cited in the IDS filed 02/03/2023; [0373]) teaches antibodies generated to the N-terminal fragment of human CCR8 wherein the cysteine at position 25 was mutated to serine to prevent disulfide bonding. The CCR8 conjugate was used for antibody panning and had an N-terminal CCR8 sequence identical to of instant SEQ ID NO:46, followed by a 6xHis tag, linker and mouse IgG2a-Fc (CCR8-ECD-Fc; Table 4). US 2021/0238292 is excepted as prior art under 102(b)(2) because it has an effective filing date less than a year before the instant application and an identical inventive entity.
Barrington et al. (J. Biol. Chem. 291(31):16208-16220, 2016, cited in the IDS filed 2/3/2023) showed that for CCR8, disruption by amino acid substitution of the natural CKR disulfide bridge between amino acids C25 and C272 did not affect cell surface expression levels, while disruption of the C106-C183 bridge reduced surface expression by up to 6-fold (Fig. 1B and p. 16209, col. 1, fourth paragraph). Ligand CCL1 cannot activate the receptor when either disulfide bridge is absent (p. 16210, col. 1, first paragraph). Barrington et al. provides no motivation or suggestion to have a sulfated CCR8 polypeptide or conjugate according to the instant claims wherein C25, i.e., the cysteine between the TRD and LID domain, is removed or altered to a different amino acid.
Gutierrez et al. (J. Biol. Chem. 279(15:14726-14733, 2004, cited in the IDS filed 2/3/2023) teaches chemokine receptor CCR8 binds CCL1 ligand and has a potential role in allergic inflammation, atherogenesis, can act as an HIV coreceptor and is a target of some virally encoded cytokines (p. 14726, col. 2, first full paragraph). Using mouse CCR8 (mCCR8) it was shown that post-translational modification led to sulfation of tyrosines at positions 14 and 15 and decrease ligand CCL1 binding (p. 14730, first and second full paragraphs). “All together, the results show that tyrosine sulfation in the CCR8 N-terminal domain is important for full activity of this chemokine receptor,…” (p. 14726, col. 2, second full paragraph). mCCR8 was produced recombinantly (paragraph bridging pp. 14726-14727). Sulfation was accomplished by incubation of the protein with [35S]sulfate (p. 14729, col. 1, third paragraph). Through amino acid mutation analysis, it was determined that tyrosines 14 and 15 were normally sulfated in mCCR8 (paragraph bridging cols. 1-2 of p. 14729). This reference supports the obviousness of having a polypeptide comprising at least two tyrosine substitutions in the TRD of CCR8, but is silent with respect to changing or deleting the cysteine between the TRD or LID domain.
Jen et al. (Biochem. 48(23):5332-5338, 2009, cited in the IDS filed 2/2/2023) teaches posttranslational sulfation synthesized N-terminal domain-derived peptides of CCR5 and CCR8 by tyrosylprotein sulfotransferase-2 (TPST-2), followed by separation of products by RP-HPLC and mass spectrometry analysis (Abstract and Experimental Procedures). The human CCR5 peptides analyzed were N-terminal amino acids 1-18 or 2-18 (Fig. 1). The mouse CCR8 (mCCR8) peptide comprised amino acids 2-17 (p. 533, col. 1, second paragraph). Treatment with TPST-2 generated a mixture of sulfated forms. It was found that for mCCR8 Tyr 3, Tyr14 and Tyr15 are sulfated (p. 5335, col. 1). Jen et al. did not include a LID domain or change or delete a cysteine immediately after the TRD, which comprises amino acids 1-18.
US 20090220486 A1 and related US 20080274100, both cited in the IDS filed 02/03/2023, teaches in paragraph [0044] CCR5 sulfation and activity. In paragraphs [0130]-[0142] antibodies to sulfated proteins are taught. Paragraph [0185] suggests using sulfated CCR8 to make antibodies. Antibodies were identified by biopanning for antibodies (e.g., [0185] and [0198]-[0202]. The sulfated peptides were synthetic ([0333]). There references are silent with respect to changing or deleting the cysteine between the TRD or LID domain.
Examiner’s Comment
While the prior art (see above) individually teaches sulfated CCR peptides comprising the TRD and LID domain, as well as the cysteine between the two domains (C25 for CCR8), neither the prior art nor the knowledge generally available to the artisan of ordinary skill before the effective filing date of the invention provides a nexus for combining with the same polypeptide, the sulfation as required by claims as well as the deletion of substitution of the intervening cysteine. As a result, at least the elected species of claim 1 is free of the prior art.
Conclusion
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Claire Kaufman
/Claire Kaufman/
Primary Examiner, Art Unit 1674
January 24, 2026