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 .
DETAILED ACTION
Applicant’s response filed on 07/23/2026 is duly acknowledged.
Claims 1-23 as currently amended/presented are pending in this application.
Claims 13-23 (nonelected inventions of Groups II-III) remain withdrawn.
Claims 1-12 (elected invention of Group I, taken as without traverse; directed to “A mesoporous silica binding peptide…”), as currently amended/presented have been examined on their merits in this action hereinafter.
Priority
This application gets the effective filing date of 06/21/2023.
Claim Objections- Withdrawn
In view of applicant’s amendment to claim 7, the claim objection as previously made by the examiner, has now been withdrawn.
Claim Rejections - 35 USC § 112 – Withdrawn
In view of applicant’s amendment to claims 1, 5 and 6, the 112b rejection of claims 1-12 as previously made by the examiner, has been withdrawn.
Claim Rejections - 35 USC § 102 - Withdrawn
In view of applicant’s amendment to claim 1, the 102(a)(1) rejection of record over the cited prior art of Shimojo et al (JP 2013151454 A), as previously made by the examiner, has been withdrawn.
Claim Rejections - 35 USC § 103- Withdrawn
In view of applicant’s amendment to claim 1, the 103(a) rejection of claims 5 and 6 as previously made by the examiner has been withdrawn.
However, the following contains new grounds of objection/rejection over pending claims as currently amended by the applicants:
Claim Rejections - 35 USC § 112 – New Grounds
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 5, 6 and 11 (as presented) are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claims 1, 5 and 11 recite the following:
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It is to be noted that instant claim 1 (from which both claims 5 and 11 indirectly or directly depend from) has now been amended to delete the SEQ ID NOs: 1 and 11 from the Markush group as claimed (which now represents only “SEQ ID NOS: 2-10 and 12-16”). However, instant claims 5 and 11 still require the limitations of “the mesoporous silica binding peptides of SEQ ID NOS: 1-16” (see claim 5, for instance), which does not appear to further limit the scope of the product as presented in amended claim 1. Similar issue is pertinent to instant claim 11, as currently presented. Since, dependent claim 6 directly depends from claim 5 (which fails to further limit the product of claim 1, as amended), it has also been rejected for the same reasons of record, as discussed above.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. Appropriate correction is required.
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Claim Rejections - 35 USC § 102 - New Grounds
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1 and 7-11 (as amended/presented) are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Inoue (2015; NPL cited as ref. [U] on PTO 892 form).
Claim 1 as amended has been reproduced hereinbelow:
“1 (currently amended) A mesoporous silica binding peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 2-10 and 12-16, wherein such peptides are not in the form of a naturally occurring protein sequence.”
See also limitations of dependent claims 7-11, as presented by applicants.
Inoue (2015), while teaching peptide useful in biosensor for detecting target raw materials such as metals including titanium and compounds thereof (see entire disclosure for Accession NO: BBY97722 attached), disclose a non-natural, synthetic, titanium metal binding peptide that comprises amino acid sequence having 100% identity to instantly claimed SEQ ID NO: 2 (regarding instant claim 1) as reproduced herein below (a 16 amino acid peptide designated as SEQ ID NO: 74):
SEQ ID NO: 2 (Instant claim 1- A_GenSeq database result)
BBY97722
ID BBY97722 standard; peptide; 16 AA.
XX
AC BBY97722;
XX
DT 18-JUN-2015 (first entry)
XX
DE Titanium-binding peptide (Ti3) SEQ ID NO:74.
XX
KW analyte detection; biosensor; heavy metal; protein detection;
KW recombinant protein.
XX
OS Synthetic.
XX
CC PN JP2015082985-A.
XX
CC PD 30-APR-2015.
XX
CC PF 25-OCT-2013; 2013JP-00222610.
XX
PR 25-OCT-2013; 2013JP-00222610.
XX
CC PA (AJIN ) AJINOMOTO KK.
XX
CC PI Inoue I;
XX
DR WPI; 2015-271232/36.
XX
CC PT New peptide useful in biosensor for detecting target raw material,
CC PT preferably titanium metal or titanium compound, and electronic devices
CC PT and implants, e.g. semiconductor memory and solar cell.
XX
CC PS Example 3; SEQ ID NO 74; 117pp; Japanese.
XX
CC The invention relates to a novel peptide used in a biosensor for
CC detecting a target raw material, preferably titanium metal or titanium
CC compound. The peptide comprises an amino acid sequence formula of SEQ ID
CC NO: 1-2 (see BBY97649-BBY97650). The invention further claims: a fusion
CC protein comprising the peptide; a multimer of fusion protein; a complex
CC of multimer; a polynucleotide encoding the fusion protein; an expression
CC vector comprising the polynucleotide; a transformant comprising the
CC expression vector; and a method of screening the peptide. The peptide is
CC also used in electronic devices and implants, preferably semiconductor
CC memory and solar cell. The peptide has the ability to firmly attach to a
CC target raw material. The present sequence is a titanium-binding peptide
CC obtained by a modified phage display method and is used in the biosensor
CC for detecting a target raw material.
XX
SQ Sequence 16 AA;
Query Match 100.0%; Score 72; Length 16;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KSLSRHDHIHHH 12
||||||||||||
Db 1 KSLSRHDHIHHH 12
The limitations of “mesoporous silica binding” is taken as an inherent functional feature of the peptide which would necessarily be the same, as the disclosed 12 AA peptide by Inoue has the same structural feature and/or the same amino acid sequence as recited in instantly amended claim 1, SEQ ID NO: 2; i.e. “KSLSRHDHIHHH”.
Regarding instant claim 11, the metal-binding peptide disclosed by Inoue 2015 has an amino acid sequence of SEQ ID NO: 2, as recited in instant claim 1, as currently amended.
The limitations of instant claims 7-10, as currently recited (wherein “the mesoporous silica to which the peptide [[is]] binds consists essentially of silicon and oxygen”; “wherein the mesoporous silica to which the peptide binds is a clay that comprises on a molar basis, 20% to 35% silicon and 60% to70% oxygen”; “wherein the clay further includes on a molar basis, up to 10% of at least one trace metal selected from the group consisting of aluminium, calcium, gold, iron, magnesium, potassium, sulphur and thallium”; and “wherein the clay further comprises up to 6% aluminium”) mainly characterize the “mesoporous silica” to which the claimed peptide binds (taken herein as inherent functional property limitations), and do not specifically further define and/or provide structural distinction other than the amino acid sequence for the peptides already recited in terms of SEQ ID NOs: 1-16 of instant claim 1, and therefore, have been taken to be met by the specific disclosure from Inoue, as discussed above.
As per MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. In re American Academy of Science Tech Center, F.3d, 2004 WL 1067528 (Fed. Cir. May 13, 2004)(The USPTO uses a different standard for construing claims than that used by district courts; during examination the USPTO must give claims their broadest reasonable interpretation.). This means that the words of the claim must be given their plain meaning unless applicant has provided a clear definition in the specification. In re Zletz, 893 F.2d 319, 321, 13 USPQ2d 1320, 1322 (Fed. Cir. 1989).
Claim Rejections - 35 USC § 103 – New Grounds
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-11 (as currently amended/presented) are rejected under 35 U.S.C. 103 as being unpatentable over Inoue (2015; NPL cited as ref. [U] on PTO 892 form) taken with Shimojo et al (JP 2013151454 A; NPL previously made of record), and Monthony et al (WO 2009/073977 A1; FOR previously made of record).
Claims 1, 5 and 6, as currently amended have been reproduced below:
“1 (currently amended) A mesoporous silica binding peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 2-10 and 12-16, wherein such peptides are not in the form of a naturally occurring protein sequence.”
“5. (currently amended) The mesoporous silica binding peptide of claim 4 wherein the linker peptide sequence is SGGGCGPXGPC (SEQ ID NO: 17) where X is a place holder for any of the mesoporous silica binding peptides of SEQ ID NOS: 1-16 having 8 to 18 residues.”
“6. (currently amended) The mesoporous silica binding peptide of claim 5 wherein the mesoporous silica binding peptide is fused to the C-terminus of the heterologous protein.”
See also limitations of dependent claims 2-4 and 7-11 as currently presented (see also 112d rejection as discussed above).
Inoue (2015), while teaching peptide useful in biosensor for detecting target raw materials such as metals including titanium and compounds thereof (see entire disclosure for Accession NO: BBY97722 attached), disclose a non-natural, synthetic, titanium metal binding peptide that comprises amino acid sequence having 100% identity to instantly claimed SEQ ID NO: 2 (regarding instant claim 1) as reproduced herein below (a 16 amino acid peptide designated as SEQ ID NO: 74):
SEQ ID NO: 2 (Instant claim 1- A_GenSeq database result)
BBY97722
ID BBY97722 standard; peptide; 16 AA.
XX
AC BBY97722;
XX
DT 18-JUN-2015 (first entry)
XX
DE Titanium-binding peptide (Ti3) SEQ ID NO:74.
XX
KW analyte detection; biosensor; heavy metal; protein detection;
KW recombinant protein.
XX
OS Synthetic.
XX
CC PN JP2015082985-A.
XX
CC PD 30-APR-2015.
XX
CC PF 25-OCT-2013; 2013JP-00222610.
XX
PR 25-OCT-2013; 2013JP-00222610.
XX
CC PA (AJIN ) AJINOMOTO KK.
XX
CC PI Inoue I;
XX
DR WPI; 2015-271232/36.
XX
CC PT New peptide useful in biosensor for detecting target raw material,
CC PT preferably titanium metal or titanium compound, and electronic devices
CC PT and implants, e.g. semiconductor memory and solar cell.
XX
CC PS Example 3; SEQ ID NO 74; 117pp; Japanese.
XX
CC The invention relates to a novel peptide used in a biosensor for
CC detecting a target raw material, preferably titanium metal or titanium
CC compound. The peptide comprises an amino acid sequence formula of SEQ ID
CC NO: 1-2 (see BBY97649-BBY97650). The invention further claims: a fusion
CC protein comprising the peptide; a multimer of fusion protein; a complex
CC of multimer; a polynucleotide encoding the fusion protein; an expression
CC vector comprising the polynucleotide; a transformant comprising the
CC expression vector; and a method of screening the peptide. The peptide is
CC also used in electronic devices and implants, preferably semiconductor
CC memory and solar cell. The peptide has the ability to firmly attach to a
CC target raw material. The present sequence is a titanium-binding peptide
CC obtained by a modified phage display method and is used in the biosensor
CC for detecting a target raw material.
XX
SQ Sequence 16 AA;
Query Match 100.0%; Score 72; Length 16;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KSLSRHDHIHHH 12
||||||||||||
Db 1 KSLSRHDHIHHH 12
The limitations of “mesoporous silica binding” is taken as an intrinsic functional feature of the claimed peptide which would necessarily be the same, as the disclosed titanium metal-binding peptide by Inoue has the same structural features and/or comprises the same amino acid sequence as recited in instantly amended claim 1, SEQ ID NO: 2; i.e. “KSLSRHDHIHHH”.
Regarding instant claim 11, the metal-binding peptide disclosed by Inoue 2015 has an amino acid sequence of SEQ ID NO: 2, as recited in instant claim 1, as currently amended.
The limitations of instant claims 7-10, as currently recited (wherein “the mesoporous silica to which the peptide [[is]] binds consists essentially of silicon and oxygen”; “wherein the mesoporous silica to which the peptide binds is a clay that comprises on a molar basis, 20% to 35% silicon and 60% to70% oxygen”; “wherein the clay further includes on a molar basis, up to 10% of at least one trace metal selected from the group consisting of aluminium, calcium, gold, iron, magnesium, potassium, sulphur and thallium”; and “wherein the clay further comprises up to 6% aluminium”) mainly characterize the “mesoporous silica” to which the claimed peptide binds (taken herein as intrinsic functional property), and do not specifically further define and/or provide structural distinction other than the amino acid sequence for the peptides already recited in terms of “SEQ ID NOs: 2-10 and 12-16” of instant claim 1, and therefore, have been taken to be met by the specific disclosure from Inoue, as discussed above.
However, the limitations of dependent claims 2-6 as currently presented have not been specifically exemplified by the disclosure from Inoue 2015, as discussed above.
Shimojo et al (2013; all citations per English translation previously made of record) disclose a peptide having an amino acid sequence (designated as SEQ ID NO: 11; WAGAKRLVLRRE; see p. 4, 4th paragraph; and claims, for instance) which is 100% identical to the peptide having SEQ ID NO: 1 disclosed as non-natural, silica binding peptide by the applicants on record; see homology below with the 12 AA peptide disclose with Accession Number BAQ44713):
SEQ ID NO: 1 (A_Genseq database)
BAQ44713
ID BAQ44713 standard; peptide; 12 AA.
XX
AC BAQ44713;
XX
DT 12-SEP-2013 (first entry)
XX
DE Gold (Au)-binding AuBP1 peptide, SEQ ID 11.
XX
KW diagnostic test; gold carrier; immunosensor.
XX
OS Unidentified.
XX
CC PN JP2013151454-A.
XX
CC PD 08-AUG-2013.
XX
CC PF 25-JAN-2012; 2012JP-00013115.
XX
PR 25-JAN-2012; 2012JP-00013115.
XX
CC PA (JAAT ) JAPAN ATOMIC ENERGY AGENCY.
CC PA (UYKY-) UNIV KYUSHU.
XX
CC PI Shimojo K, Naganawa H, Goto M, Kamiya N;
XX
DR WPI; 2013-M22265/55.
XX
CC PT Gold carrier useful in kit, immune sensor and immune marker for
CC PT inspecting disease, comprises immobilized protein comprising peptide and
CC PT protein having gold binding ability.
XX
CC PS Disclosure; SEQ ID NO 11; 49pp; Japanese.
XX
CC The present invention relates to a novel gold carrier comprising an
CC immobilized protein, where the protein is a fusion protein of a peptide
CC and a protein having gold binding ability. Also described are: (1) a
CC method for manufacturing the gold carrier, which involves immobilizing
CC the protein in the gold carrier; and (2) a method for detecting to-be-
CC measured substance in a test sample, involves reacting the gold carrier
CC and the test sample, and specifically detecting interaction between the
CC gold carrier and the to-be-measured substance in the test sample. The
CC gold carrier is useful in a kit, an immune sensor and in immune marker
CC for inspecting disease. The present sequence is a gold (Au)-binding AuBP1
CC peptide, used in the construction of gold carrier of the invention.
XX
SQ Sequence 12 AA;
Query Match 100.0%; Score 62; Length 12;
Best Local Similarity 100.0%;
Matches 12; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 WAGAKRLVLRRE 12
||||||||||||
Db 1 WAGAKRLVLRRE 12
The limitations of “mesoporous silica binding” is taken as an intrinsic functional feature of the peptide which would necessarily be the same, as the disclosed 12 AA peptide from Shimojo et al has the same structural feature or the same amino acid sequence of SEQ ID NO: 1 in the instant disclosure of record.
Regarding instant claim 2, Shimojo et al disclose that the aforementioned peptide is fused to a termini (i.e. N- or C-terminal fusion protein) of a heterologous protein (see Abstract, and p. 4, 5th paragraph, for instance) such as an antibody-binding protein (see p. 2, 3rd paragraph; for instance); wherein (regarding instant claims 3-4) the peptide is fused to the C-terminus of the heterologous protein (see for instance, p.6, Example 1 disclosing a fusion protein, albeit to a different peptide as an example, designated as “A3 peptide” that is fused to the C-terminus of the heterologous ZZ domain of protein A (designated as “ZZ-Trx-A3”) via a linking “protecting protein” such as thioredoxin (Trx; taken herein as a “linker peptide sequence”; it is noted that the term “linker peptide sequence” has not been specifically defined by applicants on record; see instant disclosure, SPEC, p. [0015], [0017], for instance). Regarding instant claim 11, the peptide disclosed by Shimojo et al has an amino acid sequence that consists of SEQ ID NO: 1 disclosed by the applicants on record.
The limitations of instant claims 7-10, as currently recited (wherein “the mesoporous silica to which the peptide [[is]] binds consists essentially of silicon and oxygen”; “wherein the mesoporous silica to which the peptide binds is a clay that comprises on a molar basis, 20% to 35% silicon and 60% to70% oxygen”; “wherein the clay further includes on a molar basis, up to 10% of at least one trace metal selected from the group consisting of aluminium, calcium, gold, iron, magnesium, potassium, sulphur and thallium”; and “wherein the clay further comprises up to 6% aluminium”) mainly characterize the “mesoporous silica” to which the claimed peptide binds (taken herein as intrinsic functional property limitations), and do not specifically further define and/or provide structural distinction other than the amino acid sequence for the peptides already recited in terms of SEQ ID NOs: 1-16, and therefore, have also been taken to be met and/or obviated by the specific disclosure from Shimojo et al, as discussed above.
However, the specific linker peptide limitations of instant claims 5 and 6 (as reproduced above) have not been taught and/or disclosed by the cited prior art references of Inoue 2015 when taken with the disclosure from Shimojo et al, as discussed above.
Monthony et al (2009), while teaching polypeptides modified by protein trans-splicing technology (see Title, Abstract, and Fig. 1AB, and Example 1 on p. 26-27, for instance), disclose the use of peptide linkers including 7 amino acid peptide sequence SGGGCGP designated as SEQ ID NO: 11 (see p. 21, 2nd paragraph; Example 1 on p. 27, for instance) that can provide spacing as well as means for functional derivatization such as PEGylation (see p. 27, 2nd paragraph, for instance) and can be positioned at the C-terminus of a given target protein such as a maltose binding protein (MBP; see Fig. 11, for instance) for modifying the target proteins. Monthony et al also disclose several benefits of such peptide linker/spacer, in addition to its use in trans-splicing reaction, such as for site-specific PEGylation wherein glycine (G) residues are to provide some spaces around the cysteine, and the proline (P) residue is thought to minimize degradation by carboxyl peptidases (i.e. provide stability for the fusion protein; see p. 27, 2nd paragraph, for instance).
Thus, given the detailed disclosure for metal-binding peptides from Inoue 2015 in combination with the disclosure from Shimojo et al as discussed above, to a person of ordinary skill in the art before the effective filing date of this invention, it would have been obvious to include such peptide linkers at the C-terminus of a heterologous protein that can be further employed for accommodating a desired peptide sequence of limited length, including the metal-binding peptides as disclosed by both Inoue 2015 and Shimojo et al (including peptides such as SEQ ID NOs: 2 and 1, respectively; as specifically discussed above). Since, the techniques for such bio-molecular manipulations for making heterologous fusion proteins have already been disclosed in the cited prior art of Monthony et al, such modifications to incorporate the desired linker peptide at the C-terminus of heterologous proteins (such as MBP as demonstrated by Monthony et al), would have been obvious and/or fully contemplated by an artisan of ordinary skill in the art, at least for the disclosed benefits of flexibility and advantages as already eluded by Monthony et al (see detailed teachings above), unless evidence/data provided on record to the contrary (which is currently lacking; see instant specification, [0042], for instance).
Thus, the claim as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the invention as claimed.
Allowable Subject Matter
Claim 12 is objected to as being dependent upon a rejected base claim, but appears to be free of prior art issues, and would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Examiner’s Response to Applicant’s Arguments
Applicant’s arguments filed on 07/23/2026 (see REM, p. 5) with respect to claim(s) of record as currently amended, have been considered but are moot in view of the new grounds of objections/rejections made in this office action, as discussed in detail above.
Conclusion
NO claims are currently allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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 SATYENDRA K. SINGH whose telephone number is (571)272-8790. The examiner can normally be reached M-F 8:00- 5:00.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LOUISE W HUMPHREY can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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SATYENDRA K. SINGH
Primary Examiner
Art Unit 1657
/SATYENDRA K SINGH/Primary Examiner, Art Unit 1657
Prosecution Insights