DETAILED ACTION
Notice of Pre-AIA or AIA Status
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Applicant’s species election without traverse of
(i) an anti-Nectin-4 antibody comprising:
a. heavy chain CDRs: H1 SEQ ID NO: 1 wherein X1 is M (AKA SEQ ID NO: 7), H2 SEQ ID NO: 2, and H3 SEQ ID NO: 3 wherein X2 is M and X3 is K (AKA SEQ ID NO: 11) and
b. light chain CDRs: L1 SEQ ID NO: 4 wherein X4 is R and X5 is E (AKA SEQ ID NO: 13), L2 SEQ ID NO: 5, and L3 SEQ ID NO: 6 wherein X6 is F and X7 is P (AKA SEQ ID NO: 15);
(ii) an anti-CD3 antigen binding site comprising: L4 SEQ ID NO: 44, L5 SEQ ID NO: 45, L6 SEQ ID NO: 46 wherein X11 is G, X12 is P, X13 is K, X14 is Q (AKA SEQ ID NO: 52), L7 SEQ ID NO: 47 wherein X15 is D (AKA SEQ ID NO: 55), L8 SEQ ID NO: 48, and L9 SEQ ID NO: 49;
(iii) the agent of the immunoconjugate is an auristatin; and
(iv) immune checkpoint PD-1
in the reply filed on 2/17/2026 is acknowledged.
3. Claims 1-25 and 27-50 are pending. Claim 26 is canceled. Claims 33 and 34 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 2/17/2026.
4. Claims 1-25, 27-32 and 35-50 are under examination.
Information Disclosure Statement
5. The information disclosure statements (IDS) submitted on 12/16/2022, 10/31/2024, 11/6/2024, 12/5/2024, 7/2/2025, 8/7/2025 and 1/13/2026 have been considered by the examiner.
Replacement Sequence Listing
6. Applicant’s submission of a replacement sequence listing is acknowledged. The replacement sequence listing has been entered.
Drawings
7. Replacement of drawings in compliance with 37 CFR 1.84 and 37 CFR1.121(d) are required. The drawings submitted are not acceptable because:
The drawings are not incompliance with 37 CFR1.84 because Fig. 31 contains figure, or view numbers that have incorrect orientation. Reference characters, sheet numbers, and view numbers must be oriented in the same direction as the view. See 37 CFR1.84(p)(1).
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:
8. Specific deficiency – Nucleotide and/or amino acid sequences appearing in the drawings are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). See Fig. 33A and 33B. Sequence identifiers for nucleotide and/or amino acid sequences must appear either in the drawings or in the Brief Description of the Drawings.
Required response – Applicant must provide:
Replacement and annotated drawings in accordance with 37 CFR 1.121(d) inserting the required sequence identifiers;
AND/OR
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers into the Brief Description of the Drawings, 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
9. The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code, see paragraph [0320] for example. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Claim Objections
10. Claims 12-13, 17-18, 28-29, 46 and 48-50 are objected to because of the following informalities:
(i) Claims 12 and 17 are objected to for reciting “each said region independently having at least 80% identity to a combination of amino acid sequences…”.
Claims 13 and 18 are objected to for reciting “each said region independently having at least 80 identity to a pair of amino acid sequences…”.
Claim 48 is objected to for reciting “each said region independently having at least 90% identity to a combination of amino acid sequences…”.
Claim 49 is objected to for reciting “each said region independently having at least 90% identity to a pair of amino acid sequences…”.
Claims 12-13, 17-18, and 48-49 are objected to because each region (VH or VL) cannot have at least 80% to a combination or a pair of VH and VL amino acid sequences.
(ii) Claim 13 is further objected to for reciting “at least 80 identity”. Claim 13 should be amended to recite “at least 80% identify”.
(iii) Claims 28 and 29 are objected to for reciting “or antibody fragment” as this limitation is already in base claim (claim 19).
(iv) Claims 46 and 50 are objected to for omitting a subject to be treated.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
11. 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.
12. Claims 20, 23-25 and 27 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.
(i) Claims 20 and 27 are indefinite for reciting “at a value of a condition”. The specification does not specifically define “a value of a condition”. The specification gives one example of a condition: pH. Other than pH, the specification does not teach the metes and bounds of a value of a condition. Therefore, the metes and bounds of the claimed invention cannot be determined and the claims are indefinite.
(ii) Claims 23-25 and 27 are indefinite for the following reasons:
Claim 23 recites: “having at least 70% of the antigen binding activity at pH 6.0 as compared to the same antigen binding activity of a parent antibody or antibody fragment from which the antibody or antibody fragment is evolved, at pH 6.0”.
Claim 24 recites “having less than 50% of the antigen binding activity at pH 7.4 as compared to a same antigen binding activity of a parent antibody or antibody fragment from which the antibody or antibody fragment is evolved, at pH 7.4”.
Claim 25 recites “wherein the antigen binding activity is binding to Nectin-4 protein, as measured by an ELISA assay”.
The meaning of the term “antigen binding activity” is unclear. It may be interpreted as binding affinity as evidenced by claim 20, or EC50 value (which measures the concentration of an antibody required to induce a 50% response). Furthermore, a parent antibody or antibody fragment is not limited to BAP-143 wildtype. In the absence of a clear definition of “antigen binding activity” and “a parent antibody or antibody fragment”, the metes and bounds of the claimed invention cannot be determined and the claims are indefinite.
Claim Rejections - 35 USC § 112
13. 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.
14. Claims 1-25, 27-32 and 35-50 are rejected under 35 U.S.C. 112, 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(s), at the time the application was filed, had possession of the claimed invention.
The claims are rejected because the specification does not adequately describe all the species encompassed by the genus of anti-Nectin-4 antibodies and the genus of anti-CD3 antibodies.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., high affinity, neutralization activity, competing with a reference antibody for binding), “[c]laiming antibodies with specific properties, e.g., an antibody that binds to human TNF-α with A2 specificity, can result in a claim that does not meet written description even if the human TNF-α protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011).
“[A] sufficient description of a genus . . . requires the disclosure of 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, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the 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 to provide a "representative number” of species.
The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. For antibodies, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor, 97 USPQ2d at 1875 (“[T]he application only provides amino acid sequence information (a molecular description of the antibody) for a single mouse variable region, i.e., the variable region that the mouse A2 antibody and the chimeric antibody have in common. However, the mouse variable region sequence does not serve as a stepping stone to identifying a human variable region within the scope of the claims.”). A chimeric antibody shares the full heavy and light chain variable regions with the corresponding mouse antibody; that is, the structure shared between a mouse and chimeric antibody would generally be expected to conserve the antigen binding activity.
Lastly, even if a selection procedure is disclosed that was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad, 94 USPQ2d at 1167; Centocor at 1876 (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”)
Independent claim 1 is drawn to an isolated polypeptide that binds to Nectin-4 comprising a heavy chain variable region including three complementarity determining regions (CDRs) having sequences H1, H2, and H3, wherein:
the H1 sequence is GFTFSSYNX1N (SEQ ID NO: 1);
the H2 sequence is ISSSSSTIYYADSVKG (SEQ ID NO: 2); and
the H3 sequence is AYYYGX2DX3 (SEQ ID NO: 3);
wherein X1 is M or D; X2 is M or D; X3 is V or K, and a light chain variable region including three CDRs having sequences L1, L2, and L3, wherein:
the L1 sequence is X4ASQGISGWX5A (SEQ ID NO: 4);
the L2 sequence is AASTLQS (SEQ ID NO: 5); and
the L3 sequence is QQANSX6PX7T (SEQ ID NO: 6),
wherein X4 is R or H; X5 is L or E; X6 is F or E; and X7 is P or D, and with the proviso that X1,X2, X3, X4, X5, X6 and X7 cannot simultaneously be, M, M, V, R, L, F and P, respectively and with the proviso that the heavy and light chain variable regions cannot be a combination of SEQ ID NOS: 18 and 31 or a combination of SEQ ID NOS: 18 and 56.
Claim 2 is drawn to the isolated polypeptide of claim 1, further comprising six anti-CD3 complementarity determining regions L4, L5, L6, L7, L8, and L9, wherein:
the L4 sequence is GFTFNTYAMN (SEQ ID NO: 44),
the L5 sequence is RIRSKYNNYATYYADSVKD (SEQ ID NO: 45),
the L6 sequence is HX11NFX12NSX13VSWFX14Y (SEQ ID NO: 46),
the L7 sequence is RSSTGAVTTSNYX15N (SEQ ID NO: 47),
the L8 sequence is GTNKRAP (SEQ ID NO: 48), and
the L9 sequence is ALWYSNLWV (SEQ ID NO: 49),
wherein X11 is G or S, X12 is G or P, X13 is Y or K, X14 is A or Q and X15 is A or D.
Claim 1 encompasses 127 antibodies (2x1x(2x2)x(2x2)x1x(2x2)=128 -1 due to the proviso). The antibodies are required to have a function of binding to Nectin-4. Dependent claims 20-22 further require the antibodies to have higher binding activity (including higher binding affinity to Nectin-4 or lower EC50) at a value of a condition (including pH value) in a tumor microenvironment in comparison with a different value of the same condition that occurs in a non-tumor microenvironment. Claims 23-25 and 27 require the antibody to have certain specific binding activity as compared to a parental antibody at a value of condition (including different pH value).
The specification discloses twelve antibodies that can bind Nectin-4, see paragraph [0332] reproduced below:
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623
708
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However, there is no evidence indicating all the 127 antibodies can in fact bind Nectin-4.
Regarding claim 20, the specification does not disclose an anti-Nectin-4 antibody having higher binding affinity to Nectin-4 at a value of a condition (including pH value) in a tumor microenvironment in comparison with a different value of the same condition that occurs in a non-tumor microenvironment. The specification does not disclose measuring antibody binding affinity. The specification only discloses measuring EC50 at pH 6 and pH 7.4. The specification does not disclose a value of a condition other than pH 6 and pH 7.4.
ELISA assay (e.g. Tables 1 and 2, reproduce below) shows 5 antibodies having a lower EC50 at pH 6 in comparison with pH 7.4.
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313
564
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228
438
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FACS (e.g. Table 6 and Table 10, reproduced below) shows 10 antibodies having a lower EC50 at pH 6 in comparison with pH 7.4.
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161
660
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192
640
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Regarding claim 27, it appears that the ratio at least about 1.5:1 refers to the ratio of pH 7.4/pH 6.0, not pH 6/pH 7.4 as evidenced by Tables 1, 2, 6 and 10 above.
Based on ELISA and FACS, it appears that not all 12 disclosed antibodies have the function defined by claims 20-25 and 27. Without further testing, one of ordinary skill in the art would not be able to identify from the 127 antibodies, the antibodies that can bind Nectin-4, much less the antibodies having the functions recited in the claims 20-25 and 27.
Claim 2 encompasses 32 antibodies (1x1x(2x2x2x2)x2x1x1] with a function of binding to CD3.
The specification does not disclose an anti-CD3 antibody having defined 6 CDR sequences.
Therefore, the written description for anti-Nectin-4 and anti-CD3 antibodies is not commensurate in scope with the claims.
The CDR sequences (SEQ ID NOs: 1, 3, 4, 6, 46 and 47) recited in the claims appear to be consensus sequences that were generated by aligning CDR sequences from different antibodies. Therefore, the claims encompass a genus of antibodies that are formed by random combination of CDRs of different antibodies. It is unpredictable which antibodies among the claimed antibodies are in fact have the claimed function. Although the specification discloses 12 anti-Nectin-4 antibodies, these 12 antibodies cannot be a representative number of the species for the genus of 127 antibodies. There is no disclosure of a correlation between structure and function. Although one of ordinary skill in the art can envision each possible CDR sequence, one of ordinary skill in the art can't identify without further testing the antibodies which have the claimed function. The specification only discloses a correlation between the Nectin-4 binding function and each of the 12 disclosed antibodies. However, such correlation is not present when the CDR sequences of these antibodies are modified.
The state of the prior art is such that it is well established in the art that the formation of an intact antigen-binding site of antibodies generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs or hypervariable regions, 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 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 (Almagro et. al., Front. Immunol. 2018; 8:1751, see Section “The IgG Molecule” in paragraph 1 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).
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 Herold et al. Herold et al. (Sci Rep. 2017 Sep 25;7(1):12276) performed single- and double-point mutations in exemplary antibodies and found that a single point mutation in the VH CDR region can completely abolish antigen binding (Page 8, Paragraph 1, Line 11). Murphy et al. (Journal of Immunological Methods, Vol. 463, Pg. 127-133, 2018), teach that altering amino acid D92 in the complementarity determining region light chain region 3 (CDRL3) of single chain fragment variable (scFv) 2G1 obliterates its capacity to bind to microcystin-leucine-arginine (MC-LR)(Page 130, Section 3.2, paragraph 2) and changing phenylalanine at position 91 to tyrosine caused an increased in binding to MC-LR, compared to the parent clone (Page 131, Column 1, Paragraph 2). The alterations in binding that were observed in these two variants demonstrate the highly influential role of CDRL3 in binding MC-LR. Thus, the state of the art recognized that it would be highly unpredictable that a specific antibody comprising less than all six CDRs of a parental antibody with a desired specificity would retain the antigen-binding function of the parental antibody. Thus, the minimal structure which the skilled artisan would consider predictive of the function of binding the antigen of the parental donor antibody includes six CDRs (i.e. VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and VL CDR3) from parental donor antibody in the context of framework sequences which maintain their correct spatial orientation and have the requisite binding function of the parental donor antibody. One of ordinary skill in the art could not predictably extrapolate the teachings in the specification, limited to antibodies that comprise all six CDRs of a parental donor antibody that binds antigen to antibodies that comprise fewer than all six CDRs from the parental donor antibody, wherein the antibodies retain the antigen specificity of the parental donor antibody. In cases involving unpredictable factors, such as most chemical reactions and physiological activity, more may be required. In re Fisher, 427 F.2d 833, 839, 166 USPQ 18, 24 (CCPA 1970) (contrasting mechanical and electrical elements with chemical reactions and physiological activity). See also In re Wright, 999 F.2d 1557, 1562, 27 USPQ2d 1510, 1513 (Fed. Cir. 1993); In re Vaeck, 947 F.2d 488, 496, 20 USPQ2d 1438, 1445 (Fed. Cir. 1991). One of skill in the art would neither expect nor predict the appropriate functioning of the antibodies as broadly as is claimed. There is no disclosure of a correlation between structure and function that would allow those of skill in the art to recognize other members of the claimed genus from the disclosure. Accordingly, the skilled artisan would not recognize that applicants were in possession of the invention as broadly claimed at the time the application was filed.
Conclusion
15. No claims are allowed. The elected anti-Nectin-4 antibody is free of prior art.
16. Any inquiry concerning this communication or earlier communications from the examiner should be directed to HONG SANG whose telephone number is (571)272-8145. The examiner can normally be reached Monday-Friday 8am-5pm.
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/HONG SANG/Primary Examiner, Art Unit 1646