DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant amendments to the claims and arguments filed on May 18, 2026, and July 9, 2026, have been received and entered. Claims 37 and 42 have been amended, while claims 84-97 are newly added. Claims 1-36, 38-41, 43-83 have been canceled. The Barnes’s declaration filed on May 18, 2026m have been received and considered. The declaration will be discussed in detail below as it applies to the rejection. The Claims 37, 42, 84-96 and 97 are pending in the instant application.
Election/Restrictions
Applicant's election with traverse of claims 37-40, 42 (group II) in the reply filed on September 4, 2025, was acknowledged. The requirement was deemed proper and is therefore made FINAL for the reasons discussed in non-Final office action mailed on December 18, 2025.
Claims 37, 42, 84-96 and 97 are under consideration.
Priority
This application is 371 of PCT/US2020/065450 filed on 12/17/2020, which claims priority from US provisional application no 62/949,707 filed on 12/18/2019.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 09/22/2022 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner.
Maintained -Claim Rejections - 35 USC § 112-in modified form- necessitated by amendments
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 37, 42, 84-96 and 97 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a transgenic mouse whose genome comprises in its germline: (i) a homozygous immunoglobulin heavy chain (IgH) locus comprising (i) a plurality of human heavy chain leader/V gene segments at an endogenous IgH locus, upstream of an endogenous constant (C) region, wherein each of the human heavy chain leader/V gene segments comprises the same first leader peptide-encoding sequence, and further wherein no additional human heavy chain leader N gene segments are present in the genome of the transgenic mouse other than the plurality of human heavy chain leader N gene segments comprising the same first leader peptide-encoding sequence and (ii) a homozygous immunoglobulin kappa light chain (IgH) locus comprising (i) a plurality of human kappa light chain leader/V gene segments at an endogenous Ig kappa light chain locus, upstream of an endogenous kappa constant (C) region, wherein each of the human kappa light chain leader/V gene segments comprises the same the same second leader peptide-encoding and further wherein no additional human light chain leader N gene segments are present in the genome of the transgenic mouse other than the plurality of human light chain leader N gene segments comprising the same second leader peptide-encoding sequence.,
wherein said transgenic mouse is functional to express chimeric immunoglobulin heavy and kappa light chain polypeptide, and wherein said transgenic mouse is capable of producing an antibody comprising a chimeric Ig heavy/kappa light chain variable region following immunization with an antigen,
does not reasonably provide enablement for a mouse with no phenotype or using any other heavy/light chain leader peptide-encoding sequence showing contemplated biological activity to make and use the invention. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Applicant’s arguments that claims have been limited to a transgenic mouse rather than a nonhuman animal and thereby obviating the rejection. Applicants assert that Claiming prophetically is permitted and does not by itself indicate a lack of enablement. M.P.E.P. $608.01(p) and $2166.02. Applicants provide herewith the Declaration of Ralston M. Barnes, Ph.D. (the "Barnes Declaration"). Paragraph 13 of the Declaration introduces as Exhibit B thereto a poster presented at a Keystone Conference titled "Antibodies as Drugs: Innovative Formats, Design and Engineering" in February 2025. The poster describes the creation and testing of transgenic mice of the present invention. The methods described herein generated viable mice with normal B cell development (Figure 5) and robust production of high affinity antibodies (Figures 6 and 7). Using these mice, a single primer set was able to recover full naïve repertoire, ensuring sequence diversity among antibodies obtained. These results demonstrate that the transgenic mice described in the application are competent to produce antibodies with the desired recovery of antibodies across germlines. Applicants’ arguments have been fully considered but are not found persuasive.
In response, it is relevant to note that none of the claims recite any resulting phenotype and therefore, one of skill in the art would not know how to use the mouse encompassed by the claims without a phenotype (emphasis added). The claims broadly recite a mouse whose genome comprises immunoglobulin heavy chain (IgH) locus comprising a plurality of human heavy chain leader/V gene segments at an endogenous IgH locus, upstream of an endogenous constant (C) region, wherein each of the human heavy chain leader/V gene segments comprises the same first leader peptide-encoding sequence, a immunoglobulin kappa light chain (IgH) locus comprising (i) a plurality of human kappa light chain leader/V gene segments at an endogenous Ig kappa light chain locus, upstream of an endogenous kappa constant. The independent claims fails to specify any specific common leader sequence for human heavy chain variable gene segment and/or a specific common leader sequence for a plurality of human kappa light chain variable gene segment resulting in a specific phenotype to make and use the invention.
The specification prophetically contemplates providing a mouse with a humanized heavy chain immunoglobulin locus for use in producing human antibodies, wherein the humanized heavy chain immunoglobulin locus comprises a plurality of human heavy chain leader/V gene segments all comprising the same leader peptide-encoding sequence. The specification discloses that the heavy chain leader peptide-encoding sequence for IGHV 3-23 (SEQ ID NOs: 16 and 136), which encode SEQ ID NO: 86, are selected for heavy chains in the methods, constructs and mice of the present invention, as was light chain leader peptide-encoding sequence for IGKV 3-20 (SEQ ID NOs: 49 and 137), which encode SEQ ID NO: 112 (see para. 103). Example 2 selection of heavy and light chain V gene segments. The specification teaches the heavy chain leader peptide-encoding sequence for IGHV 3-23 (SEQ ID NOs: 16 and 136), which encode SEQ ID NO: 86, were selected for heavy chains in the methods, constructs and mice of the present invention, as was light chain leader peptide-encoding sequence for IGKV 3-20 (SEQ ID NOs: 49 and 137), which encode SEQ ID NO: 112. The disclosure of instant specification is prophetic and there is no evidence on record that a transgenic nonhuman animal comprising a plurality of human heavy/light chain leader/V gene segments with the identical leader sequence can be even generated that is capable of mounting a normal immune response upon immunization to make and use the invention,
The Barnes’s declaration (para. 13) in part relying on the poster presentation showing transgenic mice described in the application are competent to produce antibodies with the desired recovery of antibodies across germlines is not found fully persuasive. Figure 2 of the declaration explicitly reported selecting common leader for IgH and IgK chains to overcome errors that are introduced during the multiplex PCR using degenerate primers. In the instant case, claims are not limited to any specific universal common leader for IgH and Igk chain that would allow the repertoire sequence recovery with single primer set as exemplified in the poster. The art teaches a single-nucleotide polymorphisms in gene leader regions are position-sensitive and can functionally reverse or alter downstream variable gene expression, thereby impacting how the gene is regulated or produces protein (see Zhu et al Journal of Genetics and Genomics 48 (2021) 936-945, abstract and page 938, col. ,2, last para and page 939, col. 1). One of skill in the art would have to perform undue experimentation to optimize a specific combination of plurality of human heavy/light chain leader / and V gene segments to make and use the mouse, without reasonable expectation of success. In this context, a careful evaluation of the content of the declaration in part relying on poster exhibiting that leader sequence and conditions used in the compare the steps, materials (specific universal leader sequences), and conditions used in the experiments of the declaration with those disclosed in the application are not commensurate in scope. The declaration (poster) reported a high-throughput in vivo antibody recovery and analysis is a key method in binder that shows single primer set recovers full naïve repertoire in common leader mice have normal B cell development (see fig. 4). It is further disclosed that immunization of common leader mice induces robust antibody production. This is further evidenced by the teaching of instant specification that describes evaluating a panel of leader peptides for efficiency of recombinant protein expression by pairwise evaluation of heavy chain and light chain leader combinations alongside control leaders, including osteonectin (SEQ ID NO: 117), which is frequently used for this purpose. This initial evaluation allowed suboptimal leaders to exclude and to select leader candidates that would be sufficient for in vitro expression (see example 2). These assertions clearly suggest that not any and all the leader sequence could be used for pairwise combinations for heavy and light chain leader sequences of the panel to drive expression of the plurality of any two or more heavy and light chain gene segment as broadly recited in the claims for the a specific phenotype. In fact, specification teaches
“the panel of was further refined following initial functional screening by in vitro expression. These criteria included an evaluation of the complexity and length of the genomic sequence to determine if it would accommodate engineering across multiple variable genes for inclusion in transgenic constructs. An exome blast confirmed that the sequences used for primer design would be unique across the mouse transcript and support specificity. Functional liabilities in the recombinant setting were considered as well to further refine criteria for high-value leaders. For instance, leader sequences were also 5 eliminated if they include a downstream methionine residue, such as IGKV 1-9 (SEQ ID NO: 97) and IGKV 1-39 (SEQ ID NO: 104), to avoid its use as a cryptic translation start site. In addition, the sequences of potential amplification primers for use with the leader peptide-encoding sequences were analyzed for undesirable secondary structure and sequence liabilities that would impact the ability to design high-performing PCR strategies. These 10 included primer sequences immediately adjacent to the variable domain framework near the 3' region of the leader, which is a strategic region for supporting full-length variable domain sequencing since more 5' regions would create longer sequences to resolve by sequencing. Based on the considerations above, the heavy chain leader peptide-encoding sequence for IGHV 3-23 (SEQ ID NOs: 16 and 136), which encode SEQ ID NO: 86, were selected for 15 heavy chains in the methods, constructs and mice of the present invention, as was light chain leader peptide-encoding sequence for IGKV 3-20 (SEQ ID NOs: 49 and 137), which encode SEQ ID NO: 112. In a preferred embodiment the genomic leader peptide-encoding sequences of IGHV 3-23 (SEQ ID NO: 136) and IGKV 3-20 (SEQ ID NO: 137) are used for heavy and light chain V gene segments, respectively.” (example 2 of the specification).
In the instant case, claims lack specificities in terms of common leader sequence utilized to make common leader mice for a specific combination of human heavy and/or light chain V gene segment showing a specific phenotype. The specification teaches many of the common leader sequences require an evaluation of the complexity and length of the genomic sequence to determine if it would accommodate across the mouse transcript and support specificity. The claims merely require a common leader sequence without specifying any specific group of common leader sequence that would enable the claimed mouse for producing antibodies in response to an antigen. MPEP 2164.05(a) states “While a later dated publication cannot supplement an insufficient disclosure in a prior dated application to make it enable, an applicant can offer the testimony of an expert based on the publication as evidence of the level of skill in the art at the time the application was filed. Gould v. Quigg, 822 F.2d 1074, 1077, 3 USPQ2d 1302, 1304 (Fed. Cir. 1987). In the instant case, it is unclear if the common leader sequence used in the post filing poster is same as one disclosed in the instant application. Absent any specific common leader sequence and/or specific heavy and light chain V gene segment resulting phenotype of the claimed mouse, it would have required undue experimentation to predict the results achieved in any mouse comprising and expressing any human IgH/L, the levels of the transgene product, the consequences of that product, and therefore, the resulting phenotype upon antigen challenge. An artisan would have to perform undue experimentation to make and use the invention without reasonable expectation of success.
Therefore, in view of the fact patterns of the instant case, and the ground of rejection outlined by the examiner, applicants' arguments are not compelling and do not overcome the rejection of record.
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.
Claims 37 and 42 remain rejected under 35 U.S.C. 103 as being unpatentable over Murphy (PNAS, 2014, 111, 14, 5153-5158, IDS)/Buelow et al (WO2005007696, dated 01/27/2005, IDS), Campbell et al (Molecular Immunology, 1992, 193-203) as evidenced by Song (WO2014058389, dated 4/17/2014, IDS) and Grawunder (US20060052585, dated 3/9/2006).
Claim interpretation: Claims as presented neither require any specific phenotype nor any specific sequence for the first and second leader peptide encoding sequence, therefore claims are interpreted as any leader sequence that is based on leader primers designed that could be used to amplify diverse human Ig VH gene segment that are conserved across plurality of V gene segments without any specific phenotype. Instant rejection is applied to the breadth of the claim and not to a mouse using specific common leader sequence and specific heavy/light chain V gene segment showing any specific phenotype.
With respect to claims 37, Murphy teaches a transgenic mouse whose genome comprises a i) a homozygous immunoglobulin heavy chain (IgH) locus comprising (i) a plurality of human heavy chain leader/V gene segments at an endogenous IgH locus, upstream of an endogenous constant (C) region, and (ii) a homozygous immunoglobulin kappa light chain (IgH) locus comprising (i) a plurality of human kappa light chain leader/V gene segments at an endogenous Ig kappa light chain locus, upstream of an endogenous kappa constant (C) region (see fig. 1). It is relevant to note that Murphy teaches replacement of entire mouse endogenous heavy/kappa light chain gene segment with corresponding human heavy/light chain variable gene segment upstream of endogenous constant region.
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Further, Murphy teaches 3 constant specific primers paired with pooled leader primers for each family of human variable regions for both the heavy chain and kappa light chain that are separately used to produce the purified product that is cloned using TOPO cloning system. Murphy teaches each sequence was assembled into contigs and aligned to human Ig sequences using the IMGT V-Quest (2) search function. Murphy further teaches these sequences are compared with germ-line sequences for somatic hypermutation and recombination junction analysis (see supplementary information, page, 1, col. 1, last para. to col. 2). Likewise, Buelow teaches a transgenic mouse (see page whose genome comprises a whose genome comprises a i) a homozygous immunoglobulin heavy chain (IgH) locus comprising (i) a plurality of human heavy chain leader/V gene segments at an endogenous IgH locus, upstream of an endogenous constant (C) region, and (ii) a homozygous immunoglobulin kappa light chain (IgH) locus comprising (i) a plurality of human kappa light chain leader/V gene segments at an endogenous Ig kappa light chain locus, upstream of an endogenous kappa constant (C) region (see example 10-11: figures 1, 4, 5,6 and 10).
Murphy/Buelow teaches different leader sequences linked to the human heavy/light chain V gene segments. Murphy differs from claimed invention by not disclosing wherein each of the human heavy/kappa chain leader/V gene segments comprises the same first/second leader peptide-encoding sequence.
Before the effective filing date of instant application, it was generally known in art that leader sequence-based primers could be used to amplify diverse human Ig VH gene segment since leader sequences are conserved across variable gene families than internal FR region. This would allow broader and less biased detection of rearranged V genes. Campbell designed a set of six, non-degenerate oligonucleotide primers, corresponding to the 5' leader regions of each of the six human VH gene families. The references provide a general strategy for family specific polymerase chain reaction amplification using these primers and a conserved 3' primer corresponding to frame work3, JH, or constant region. This strategy is used to isolate and sequence novel human germline VH genes belonging to the VH2 and VH4 families. Campbell shows that targeting the leader region facilitates broad repertoire of germline VH gene segment (see entire abstract). Song provided requisite heavy chain and light chain leader sequence by identifying several highly conserved amino acids sequence for heavy chain and light chain leader sequence (see claim 9 and 21 of ‘389). Campbell and Song differs from claimed invention by not disclosing/demonstrating using common leader exon, located 5' of each VH, DJH and VLJL gene segments.
Grawunder cures deficiency by disclosing a vector comprising human IgH and IgL chains containing all the coding regions and control elements for human antibody expression. It is disclosed that the coding regions for the variable domains contain a common leader exon, located 5' of each VH, DJH and VLJL rearranged exon (FIG. 15) (limitation of claim 38, 40) that is required for the proper transport of IgH and IgL chains through the endoplasmatic reticulum, the trans Golgi network and eventually to the cell surface (see para. 312).
Therefore, it would have been prima facie obvious for a person of ordinary skill in the art to combine the teachings of prior art to modify the transgenic mouse of Murphy/Buelow by substituting different leader sequences linked to the human heavy/light chain V gene segments with common leader exon, located 5' of each of the heavy/light chain variable gene segment as suggested in Grawunder and Song by using the leader sequence-based primers to amplify diverse human Ig VH/VL gene segment disclosed in Campbell, as instantly claimed, with a reasonable expectation of success, to produce transgenic mouse that facilitates broad repertoire of germline VH gene segment, before the effective filing date of instant application. Said modification amounting to combining prior art elements according to known methods to yield predictable results. One of ordinary skill in the art would be motivated use a common leader sequence that are conserved across variable gene families than internal FR region because this would allow broader and less biased detection of rearranged V genes (See Campbell). Other limitations of using first leader encoding sequence that is different from a second leader encoding sequence (limitation of claim 42) would be obvious modification as to design common leader sequences that are conserved across variable gene families of human heavy and kappa light chain variable gene segment respectively and therefore different between the distinct heavy and light chain gene families. Absent evidence of any superior result or use of any specific common leader sequence, one of skill in the art would have been expected to have a reasonable expectation of success because prior art successfully used a common leader exon, located 5' of each heavy and/or light chain variable gene segment for proper transport of IgH and IgL chains that is eventually expressed to the cell surface. It should be noted that the KSR case forecloses the argument that a specific teaching, suggestion, or motivation is required to support a finding of obviousness See the recent Board decision Ex parte Smith, --USPQ2d--, slip op. at 20, (Bd. Pat. App. & Interf. June 25, 2007) (KSR, 82 USPQ2d at 1396) (http: www. uspto.gov/web/offices/dcom/bpai/prec/fd071925.pdf).
Response to arguments
Applicants disagree with the rejection in part relying on Barnes Declaration describing that the use of six distinct primers to amplify all families of heavy chain V gene regions would lead to at least six different sequences, and that even within each family there would be hybridization efficiency differences that would give rise to biased recovery of the type avoided by the present invention. If Campbell et al. is being cited as providing an alternative to the claimed transgenic animals where a bundle of primers is used to clone antibodies out of a transgenic animal, rather than engineering the transgenic animal to allow use of a single primer for all antibodies, then it misses the point of the invention. If it is being cited as a method of cloning individual V gene regions with a common leader peptide-encoding sequence in tandem, for example for use in constructing a mouse of the present invention, it cannot do so since the primers are inherently variable in sequence and at any rate span only a small portion of the complete leader peptide-encoding sequence. Song, which appears to be WO 2014/058389, merely discloses design of optimal signal sequences for use in expression and manufacturing of antibodies. It does not relate to transgenic animals, or genetic constructs for generation of human antibodies from an unrearranged genomic locus of human variable domain regions in a mouse. See paragraph 10 of the Barnes Declaration. Song, which appears to be WO 2014/058389, merely discloses design of optimal signal sequences for use in expression and manufacturing of antibodies. It does not relate to transgenic animals, or genetic constructs for generation of human antibodies from an unrearranged genomic locus of human variable domain regions in a mouse. Grawunder et al. to amplify rearranged antibody variable domain sequences to clone out individual V gene regions, Paragraphs 11 and 12 of the Barnes Declaration explain that the degenerate leader-sequence based primers used in Grawunder et al. would not generate cloned sequence with a common leader, and would in fact retain most if not all of the sequence variability in the leader peptide-encoding sequence that the present invention avoids. Applicants assert that Grawunder et al. is apparently referring to the fact that all expressed V gene segments must be preceded by an exon encoding the N terminus of the leader peptide, with sufficient sequence homology between V gene segments that priming can be achieved using one or several degenerate primers. But as outlined in the Barnes Declaration (paragraphs 11 and 12), amplification using such primers cannot generate different V gene segments having identical upstream leader peptide-encoding sequences. Campbell et al. and/or Grawunder et al. are cited to suggest mechanisms of amplifying V gene region sequences for cloning in tandem to form an unrearranged human immunoglobulin locus for introduction into mice, such amplification would not give rise to the common (same) leader sequence for all V gene regions of the present invention. Applicants’ arguments have been fully considered but are not found persuasive.
In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Applicants have further engaged in selective reading of the teachings of Campbell and/or Grawunder to formulate the grounds for teaching away. It should be noted that the ultimate goal of instant application pertains to overcome bias issue by engineering human heavy and/or light chain V gene segments so that each segment in a given chain that shares the same leader peptide-encoding sequence. This would allow amplification of variable regions with a single forward primer to improve uniformity in rearrangement, expression, and secretion instead of a mixture as encountered in prior art. In the instant case, independent claim 32 is broad. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., single primer/common leader sequence to produce for all antibodies or genetic constructs for generation of human antibodies from an unrearranged genomic locus of human variable domain regions in a mouse or any use of the mouse ) are not recited in the rejected independent claim. Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). In the instant case, claim 31, neither recites a specific common leader sequence to produce all antibodies nor does the claim recite human antibodies from an unrearranged genomic locus of plurality of human variable domain regions in a mouse. The term V gene segment recited in the claim could be broadly interpreted to encompass rearranged heavy chain variable region, wherein the V segment could be derived as germline V segment but ultimately included as part of rearranged VDJ sequence. As previously indicated, it is Song who describes compiling antibody signal peptides from public data, clustered them by similarity, and selecting and using representative heavy- and light-chain leaders to measure secretion to identify the best-performing combinations (para. 63-64). To the extent, Grawunder teaches coding regions for the variable domains need to contain a common leader exon, located 5' of each VHDJH and VLJ.L rearranged exon (FIG. 15), which is required for the proper transport of IgH and IgL chains through the endoplasmatic reticulum, the trans golgi network and eventually to the cell surface, it is applicable to the rejection. This recitation suggests that prior art explicitly contemplates multiple VDJ/VJ rearrangements could use the same leader exon instead of having separate leader sequence for every possible rearrangement (see para. 316). The term V gene segment could be interpreted as the rearranged heavy chain variable gene region Absent any requirement of any specific common leader sequence or any resulting phenotype, Grawunder and Song cures the deficiency in Murphy coding regions for the variable domains need to contain a common leader exon, located 5' of each for heavy chain V gene segment and light chain V gene segment, with reasonable expectation of success.
Examiner’s note: Applicant’s representative is requested to contact Examiner to resolve the pending issues to overcome the obviousness rejection.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ANOOP K. SINGH whose telephone number is (571)272-3306. The examiner can normally be reached Monday-Friday, 8AM-5PM.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Peter Paras can be reached at (571)272-4517. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ANOOP K SINGH/Primary Examiner, Art Unit 1632
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