DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 05 November 2025 has been entered.
Election/Restrictions
Claims 1-8 and 16-19 are pending. Claims 1-8 remain withdrawn as being directed to the non-elected invention as previously noted on the record. Newly added claim 19 is directed to an invention not elected in response to restriction requirement of 12/07/2023, therefore claim 19 is withdrawn.
Claim Status
Claims 9-15 are cancelled. Claims 1-8 and 16-19 as filed on 05 November 2025 are pending. Claims 1-8 and 19 are withdrawn. Claims 16-18 are under examination.
Rejections/Objections Withdrawn
Notice of sequence deficiency is withdrawn. Examiner notes Applicant response in Remarks dated 11/05/2025 in particular the bottom of page 5 as numbered by applicant and page 6 as numbered by applicant. Applicant cites MPEP 2422 Appendix E and MPEP 2431.
Rejection Maintained – Rejection Amendment Necessitated by Applicant Amendment of Claims
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.
Claims 16-18 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.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or it may be satisfied by the disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
Scope of the Claimed Genus
Claims 16-18 are product claims to antibody-drug conjugates.
Claims 16-18 recite a genus of antibodies that bind caprin-1 protein which are conjugated to an antitumor agent from any of several species, wherein caprin-1 is expressed on the surface of a cancer cell. The antibody can be from any source (human, mouse, rabbit, canine, equine, llama, recombinant, etc.) and no limitations are placed on the structure of the binding portion of the antibodies.
The conjugation of an antibody to an antitumor agent does not provide any sequence or structure of the antibody.
Summary of Species Disclosed in the original specification
The specification discloses that, in contrast to prior teachings, caprin-1 can be expressed on the surface of certain tumor cells and further that some, but not all, antibodies specific for caprin-1 will bind caprin-1 on the surface of those cells and mediate ADCC activity. E.g. Specification at [0007]-[0008] and Example 4 at [0181]-[0184].
Caprin-1 from several species had been sequenced and is reported in the Specification as, for example, SEQ ID NOS: 2 (human), 6 (canine), 16 (cow), 18 (horse), 20 (mouse), 30 (chicken). E.g., [0163] and sequence listing. The dog, cow, horse, mouse, and chicken CAPRIN-1 sequences are all at least about 80% identical to human CAPRIN-1. The specification shows that caprin-1 mRNA is expressed in normal testis and in breast, brain, leukemia, lung, and esophageal cancer cell lines. E.g., Fig. 1; [0165]. Surface caprin-1 expression was detected by antibody staining of human [0169] and canine [0170] breast cancer tissue, in human brain tumors [0171], and in human metastatic breast cancer [0172].
At [0166], the Specification describes a polyclonal antibody that was raised by immunizing a rabbit with the caprin-1 peptide of SEQ ID NO: 37. That peptide comprises the sequence “RNLEKKKGKLDDYQ,” which is residues 66-79 of instant SEQ ID NO: 2 (human caprin-1). The polyclonal antibody binds caprin-1 on the surface of various cancer cells. E.g., [0167]. The polyclonal antibody also mediated antibody dependent cellular cytotoxicity against caprin-1-expressing cancer cells in Example 2. [0173]-[0175].
The specification in Example 4 also describes eleven mouse monoclonal antibodies (named monoclonal antibody #1 to #11) that bind an epitope within the partial human caprin-1 sequence of SEQ ID NO: 136. SEQ ID NO: 136 is a 58 amino acid segment of the human caprin-1 sequence, spanning residues 240-297 of SEQ ID NO: 2. [0203]. Antibodies that bind SEQ ID NO: 136 also bind caprin-1 on the surface of cancer cells. E.g., [0184], [0193]. Mouse monoclonal antibodies that bind the human caprin-1 protein of SEQ ID NO: 2 are described in Example 4. [0181]-[0184]. The antibodies bound caprin-1 on the surface of various tumor cells. E.g. [0193]. The antibodies exhibited ADCC against a panel of human cancer cell lines that express caprin-1. [0194], [0195]. Growth of a caprin-1-expressing tumor in a mouse model could also be inhibited by the antibodies. E.g. [0196]-[0198] and Fig 6.
State of the Relevant Art
As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure of each monoclonal antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (Of Record) (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1).
While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule”, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7). Further, the skilled artisan has long recognized that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al., Proc. Nat’l Acad. Sci. USA, 79:1979-83 (1982) (PTO-892). Rudikoff teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. E.g., Abstract. Similarly, Brown et al., J. Immunol., 156(9):3285-91 (1996) (PTO-892), teach that although a single amino acid change in CDR2 of heavy chain of a particular antibody was tolerated, the antibody lost binding upon introduction of two amino acid changes in the same region. Brown, p. 3290 and Tables 1 and 2. Table 1 of Brown shows that even a conservative substitution does not ensure that functionality of the antibody is retained. These older citations are supported my more recent discoveries of why these substitutions change antibody activity. Marvin et. al., Biochemistry, 42(23):7077-7083 (2003) (“Marvin” PTO-892) teaches that changes to the heavy and light chains altered binding affinity (Table 2) with changes to the CDR having large impacts but the changes with the largest impact were from residues in the CDR, but not from ones interfacing with the antigen ( Page 7081 in col 1 “Conclusions and Discussion” and Page 7082 in Figure 4).
In general, absent at least the conserved structure of the CDRs of the heavy chain and light chain of an antibody, the skilled artisan generally would not be able to visualize or otherwise predict an antibody with a particular set of functional properties would look like structurally.
The presence of an antitumor agent conjugated to the antibody does not inform the structure of the antibody. Antibody-drug conjugates have selective binding to target cells for use in therapy for diseases including cancer where the selective binding comes from the antibody of the ADC (Kovtun et. al. Cancer Res (2006). 66(6):3214-3221 (2006) (PTO-892) (page 3214 in col 1 in par 2).
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that 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.
The specification does not provide a representative number of species. While applicant provides eleven mouse monoclonal antibodies and a polyclonal antisera, those species are but a small portion of the extremely large number of potential members of the claimed genus. All of the mouse antibodies bind within a particular defined region of the extracellular domain of the caprin-1 protein identified by SEQ ID NO: 136. But the caprin-1 protein, and even the extracellular domain of the caprin-1 protein, contains additional epitopes where antibodies can bind, even when caprin-1 is considered from only one species, such as the human caprin-1 protein of SEQ ID NO: 2. The antibodies encompassed by the claims can be from any of a number of species. Antibodies to any given antigen can be produced from such diverse species as human, mouse, rabbit, and llama, as well as recombinantly. And as was well-known in the art, the structure each antibody uses to bind its particular epitope on an antigen is distinct and is formed by a recombination event that results in high variability at the amino acid sequence level even when the same antigen is bound by different antibodies from the same source. E.g., Edwards et al, J Mol Biol 334:103-118 (2003) (OF RECORD); see also Marchalonis et al., Dev & Comp Immunol 30:223-247 (2006) (OF RECORD), summarized in Abstract and Conclusion. Accordingly, a disclosure of eleven mouse monoclonal antibodies that all bind within the same region of human caprin-1 cannot be considered representative of antibodies to epitopes on caprin-1 generally, even if the claim were limited to human caprin-1. Further, mouse antibodies cannot be considered representative of antibodies from other sources, whether human, llama, recombinant phage, or some other antibody source.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. To meet this requirement in the instant case, the specification must describe structural features that the skilled artisan as of the effective filing date would have expected to convey the claimed binding activity.
In the instant case, the specification does not describe a substantial structure that is shared by the members of the genus and that would allow others to visualize the genus. Neither is a structural core described that would be expected to correlate with the claimed function of binding caprin-1 on the surface of a cancer cell, as recited in claim 9. The structure of an antibody that provides function are the CDRs. By not defining the CDRs applicant has not provided a structure with a known function and the art shows that variation of the CDR sequences changes their function so the teaching of a single antibody CDRs does not provide structure/function for another set of CDRs.
Conclusion
In 2017, the Federal Circuit emphasized that antibody claims do not merit special exemption from the law governing written description. In particular, the Federal Circuit rejected the notion that a disclosure can provide written description support for a claimed antibody simply by describing the target to which the antibody binds. Amgen Inc., v. Sanofi, LLC, 872 F.3d. 1367, 1378 (Fed. Cir. 2017) (finding that the “newly characterized antigen test” which “allow[ed] patentees to claim antibodies by describing . . . the antigen” to which they bind “flouts basic legal principles of the written description requirement.”). Accordingly, in order to provide written description for the claimed genus of antibodies, the Specification must disclose “either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, at 1350.
Because the specification does not describe either identifying characteristics of the genus or a representative number of species falling within the genus, the disclosure is not sufficient to show that applicant was in possession of the genus as broadly claimed.
Applicant Arguments
Applicant argues the requirements of “antibody-tumor agent conjugate that binds to a CARPIN-1 protein” and “to deliver the antitumor agent to the CARPIN-1 expressing cancer cells” provides one with skill in the art that the claims are not directed to an antibody.
Applicant argues that the case Amgen cited in the rejection is not applicable to claims 16-18.
Applicant lists the following differences between the pending claims and Amgen:
Amgen claims are to a monoclonal antibody that binds PCSK9. The legal issue is whether the functional definition without structural disclosure and lack of representative species and structural predictability was sufficient to satisfy the written description requirement. Applicant points to Example 1 which was an experiment of a polyclonal antibody that binds to CAPRIN-1 on cancer cells. Applicant argues these are experimental results for a core delivery mechanism of a claimed therapeutic system and demonstrates that CARPIN-1-targeting delivery platform can transport conjugated agents to cancer cells.
Applicant argues the amended claims are to a therapeutic system comprising an antibody a drug and delivery. Applicant argues the claims are to a therapeutic system with the following functions: recognition, therapeutic action, and delivery mechanism.
Applicant argues the claims are not to a composition but to a functional system and the claims as amended are not to an antibody but “how to deliver the drug”.
Applicant argues Ariad: applicant argues Aria is not applicable as Ariad was claiming an antibody which Ariad only disclosed the antigen in the specification. Applicant argues the pending claims are to a drug delivery system.
Applicant argues the ADC of the invention has the activity of binding CARPIN-1 to deliver its payload. Applicant argues this requires no further definition and specifically argues CDRs are not required.
Applicant argues the claims do not require a representative species because representative species are required in cases of structural unpredictability.
Applicant argues the claim is not a genus claim as it is to a conjugate system and not a genus of antibodies. Applicant argues the boundaries of the claimed conjugate are clearly defined by target specificity, conjugation chemistry, and ADC technology constraints.
Applicant argues Amgen is not applicable because Amgen was related to antibodies while the claims are to antibody-drug conjugates.
Applicant argues the AbbVie case is not related because the case was to pure antibodies regarding technical constraints, unpredictable diversity, and representativeness while the instant claims are to a drug delivery system which are predictable and constrained by the ADC platform.
Applicant argues other patents which have issued without written description rejections in U.S. Patents: 12,274,745 B2 and 11,814,428, B2.
Applicant argues claim 19 to a method using the agent of claim 19 in a method of treatment would not be a claim to an antibody.
Response to Arguments
Applicant's arguments filed 05 November 2025 have been fully considered but they are not persuasive.
The claims elected by applicant are product claims. The term “delivery system” does not appear in the claims and if they were in the claims would not provide structure for the antibody-drug conjugate the applicant is claiming. An antibody-drug conjugate comprises an antibody conjugated to a drug. One of skill in the art knows the varying structures of an antibody which are represented by but not limited to Figure 1 of Almagro. The addition of an antitumor agent to an antibody is also known in the art as shown by Kovtun. The addition of further components to an antibody does not change the reality of an antibody. An antibody binds it antigen based on its CDRs which are generally present in the variable heavy and variable light domains as explained in the above 112(a) rejection. As taught by Kovtun, the specificity and binding activity of the antibody is the reason to create an ADC it does not inform one of skill in the art of the structure of the antibody or change the way an antibody works based on its CDRs. The written description of an antibody product claim requires the recitation of the structure that provides its function which remains its six CDRs.
An antibody is functional just as an ADC is functional. A claim providing the function of binding a target does not provide structure for an antibody whether it is naked or conjugated to a drug. This is supported by the teachings cited in the 112(a) rejection. The written description rejection relates to the antibody in the ADC only being described by its antigen which makes the analysis based on Amgen, AbbVie, and Ariad applicable.
An ADC relies on the antibody binding activity which comes from its CDRs making the CDRs within an ADC just as unpredictable as a genus of antibodies.
Regarding issued patents cited by applicant, the examiner takes no position on other patent examinations either completed or ongoing. The examiner is not familiar with the specifics of any other patent application.
Claim 19 is withdrawn for being directed to an invention other than the one elected previously and the claim has not been examined or rejected and no response will be given to the arguments related to claim 19.
Rejections Maintained
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.
Applicant presented a single argument to double patenting rejections. The response to arguments to all double patenting rejections are after the last rejection in this section.
Claims 16-18 are rejected on the ground of nonstatutory double patenting as being unpatentable over:
claims 1-9 of US9,180,187 (IDS);
claims 1-15 of US9,180,188 (IDS);
claims 1-15 of US9,181,334 (IDS);
claims 1-18 of US9,181,348 (IDS);
claims 1-20 of US9,260,513 (IDS);
claims 1-20 of US9,266,958 (IDS);
claims 1-20 of US9,273,128 (IDS);
claims 1-20 of US9,273,130 (IDS);
claims 1-19 of US9,416,193 (IDS);
claims 1-19 of US9,428,581 (IDS);
claims 1-13 of US9,573,993 (IDS);
claims 1-24 of US9,862,774 (IDS);
Although the claims at issue are not identical, they are not patentably distinct from each other because each patent contains claims that recite antibodies as antibody drug conjugates (either antibody per se or the antibody used in a method of treating/detecting) that are species within the scope of the genus of antibodies recited in each of the instant claims. And while some of the issued claims do not expressly recite that the antibody binds caprin-1 expressed on the surface of a cancer cell, that property is inherently present in the patented antibodies. Therefore the claims are not patentably distinct.
Claims 16-18 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 12274745. Although the claims at issue are not identical, they are not patentably distinct from each other.
The patent recites CARPIN-1 binding polyclonal antibodies in an antibody-drug conjugate wherein in the drug is an immune activator (claims 1-4). The patent recites the antibody is monoclonal or polyclonal (claim 4) and further teaches it is humanized or chimeric (claim 5).
Claims 16-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14 of copending Application No. 18688106 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites CARPIN-1 binding polyclonal antibodies in an antibody-drug conjugate wherein in the drug is an immune activator (claims 1-4). The reference application recites the antibody is human, humanized, chimeric, or a single chain antibody (claim 6).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 16-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of copending Application No. 18873798 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites CARPIN-1 binding polyclonal antibodies in an antibody-drug conjugate wherein in the drug is an immune activator (claims 1-4). The reference application recites the antibody is monoclonal or polyclonal (claim 3) and human, humanized, chimeric, or a single chain antibody (claim 6).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 16-18 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of copending Application No. 19079803 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites CARPIN-1 binding polyclonal antibodies in an antibody-drug conjugate wherein in the drug is an immune activator (claims 1-4). The reference application recites the antibody is monoclonal or polyclonal (claim 3) and human, humanized, chimeric, or a single chain antibody (claim 6).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Applicant Arguments
Applicant requests the rejections be held in abeyance until allowable subject matter is found.
Response to Arguments
Claims continue to be rejected under 35 U.S.C. 112(a) and the current double patenting rejections are maintained.
Conclusion
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/F.E./Examiner, Art Unit 1643
/Meera Natarajan/Primary Examiner, Art Unit 1643