DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03/31/2026 has been entered.
Priority
The present application was filed as a proper National Stage (371) entry of PCT Application No. PCT/EP2019/077971, filed 10/15/2019. Acknowledgement is also made of applicant’s claim for foreign priority under 35 U.S.C. 119(a)-(d) to Application No. EP182000435.8, filed on 10/15/2018 in Europe.
Status of the claims
Claims 1, 3-9, and 16-19 are pending, claims 2, 10-15 are cancelled. Claims 1, and 8-9 are amended. Claims 17-19 are new. Claims 1, 3-9, and 16-19 are examined below.
Withdrawn Rejections
After further consideration, the rejection of claims 1, 3-9, and 16 under 35 U.S.C. 112(a) has been withdrawn.
The rejection of claims 8 and 9 under 35 U.S.C. 112(b) has been withdrawn due to the amendment of the claim.
Withdrawn Objections
The objection to the drawings has been withdrawn because the conditions for accepting color drawings and black and white photographs have been satisfied.
Claim Interpretation
The following is a quotation of 35 U.S.C. 112(f):
(f) Element in Claim for a Combination. – An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
The following is a quotation of pre-AIA 35 U.S.C. 112, sixth paragraph:
An element in a claim for a combination may be expressed as a means or step for performing a specified function without the recital of structure, material, or acts in support thereof, and such claim shall be construed to cover the corresponding structure, material, or acts described in the specification and equivalents thereof.
The claims in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be understood by one of ordinary skill in the art. The broadest reasonable interpretation of a claim element (also commonly referred to as a claim limitation) is limited by the description in the specification when 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is invoked.
As explained in MPEP § 2181, subsection I, claim limitations that meet the following three-prong test will be interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph:
(A) the claim limitation uses the term “means” or “step” or a term used as a substitute for “means” that is a generic placeholder (also called a nonce term or a non-structural term having no specific structural meaning) for performing the claimed function;
(B) the term “means” or “step” or the generic placeholder is modified by functional language, typically, but not always linked by the transition word “for” (e.g., “means for”) or another linking word or phrase, such as “configured to” or “so that”; and
(C) the term “means” or “step” or the generic placeholder is not modified by sufficient structure, material, or acts for performing the claimed function.
Use of the word “means” (or “step”) in a claim with functional language creates a rebuttable presumption that the claim limitation is to be treated in accordance with 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph. The presumption that the claim limitation is interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is rebutted when the claim limitation recites sufficient structure, material, or acts to entirely perform the recited function.
Absence of the word “means” (or “step”) in a claim creates a rebuttable presumption that the claim limitation is not to be treated in accordance with 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph. The presumption that the claim limitation is not interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, is rebutted when the claim limitation recites function without reciting sufficient structure, material or acts to entirely perform the recited function.
Claim limitations in this application that use the word “means” (or “step”) are being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, except as otherwise indicated in an Office action. Conversely, claim limitations in this application that do not use the word “means” (or “step”) are not being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, except as otherwise indicated in an Office action.
Claim 19 recites “a means for binding the C-peptide variant to form an antibody ligand complex”. Regarding the “means for binding the C-peptide variant”, the regarding structure is described in the specification, for example at page 2, lines 9-11, as an antibody directed against C-peptide. Further, the claim recites that “mixing the ligand with a means for binding” forms “an antibody ligand complex” further identifying the “means for binding” as an antibody. In view of the specification and the claim, the “means for binding” is interpreted as an antibody.
If applicant does not intend to have this/these limitation(s) interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph, applicant may: (1) amend the claim limitation(s) to avoid it/them being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph (e.g., by reciting sufficient structure to perform the claimed function); or (2) present a sufficient showing that the claim limitation(s) recite(s) sufficient structure to perform the claimed function so as to avoid it/them being interpreted under 35 U.S.C. 112(f) or pre-AIA 35 U.S.C. 112, sixth paragraph.
Claim Objections
Claim 17 is objected to because of the following informalities: Claim 17, line 12 recites “selected from the group consisting of:”. This sentence fragment appears to be a typographical error. Appropriate correction is required.
Claim Rejections - 35 USC § 103
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.
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, 3-9, 16, and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Ligler et al., US 5,354,654, granted 10/11/1994 (PTO-892, 06/14/2024) in view of Ngo (2005) “Ligand Displacement Immunoassay”, Analytical Letters, 38, 7, pages 1057-1069 (IDS 04/12/2021) and Wahren et al., WO2005118638A1 (PTO-892, 01/09/2024).
Regarding claim 1, 3-5, 16, and 19, Ligler teaches a method comprising a displacement assay comprising binding a labelled ligand or a labelled receptor to an immobilized receptor or ligand to obtain an immobilized ligand-receptor complex (Ligler, especially at column 3, lines 16-39) for biomolecules including C-peptide (Ligler, column 6, line 10; claim 15). Ligler further teaches that the ligand-receptor pair may comprise antibody-antigen or hapten (Ligler, column 5, lines 32-35), meaning that the immobilized ligand-receptor complex is an antibody-ligand-complex as claimed instantly (see also claim 13).
Ligler further teaches that the labelled ligand or receptor may be the identical molecule as the analyte or may be structurally distinct from the analyte, so long as it and the analyte both bind specifically to the immobilized receptor or ligand (Ligler, column 7, lines 23-29).
Ligler further teaches that the sample containing the analyte is passed through a column containing a labelled ligand-immobilized receptor complex and the amount of labelled ligand displaced by the analyte is detected in the liquid phase exiting the column (Ligler, column 10, lines 9-15). This allows indication of the presence of the target analyte, which again may be C-peptide (see also column 10, lines 34-41).
Ligler does not teach that the ligand has a lower affinity to the anti-C-peptide antibody than wild type C-peptide. Ligler further fails to teach that the ligand is a C-peptide variant of the wild-type C-peptide of SEQ ID No: 1 comprising the amino acids between positions 8-17 of SEQ ID NO:1, and comprising a substituted amino acid at 12 (L) as recited in instant claims 1 and 19.
Ligler further fails to teach that the substituted amino acid is substituted by C or P (instant claim 3) or that 1 to 20 amino acids are deleted at the C- and/or N-terminus (instant claim 4).
Ligler further fails to teach that the ligand comprises SEQ ID NO: 6 (instant claim 5) or that the amino acid 12(L) is substituted by C (instant claim 16).
Ngo teaches that in displacement assays, the antibody with the highest binding constant may not be the best for an assay with greatest sensitivity, because it makes the displacement of labeled antigen to the antibody by analyte antigens much more difficult and requires higher concentrations of antigen, rendering the assay less sensitive (Ngo, page 1060, lines 9-15). Ngo further teaches that antibodies with weaker affinity for the labeled antigens can be used or cross -reactive antibodies can be used that have greater affinity with analyte antigens than with the labeled antigens (Ngo, page 1060, lines 16-21).
Wahren teaches providing modified variants or analogues of C-peptide which have been modified to increase the in vivo half-life of C-peptide so as to provide a longer-lasting and more efficacious therapeutic agent, because a treatment with longer lasting action can be administered less often and would be of great clinical importance and utility (Wahren, page 7, see paragraph 1). Wahren further teaches that human C-peptide is a 31 amino acid peptide having the following sequence: EAEDLQVGQVELGGGPGAGSLQPLALEGSLQ (SEQ ID No: 1 of Wahren), the sequence being identical to that of SEQ ID No: 1 of the present application (Wahren, page 4, 3rd paragraph). Wahren further teaches that C-peptide is known to have a relatively short half-life. Wahren teaches that the peptides may be in their native form or may be truncated (e.g. from the N- or C-terminus or both (instant claim 4; Wahren, page 9, lines 9-15). As such Wahren teaches a C-peptide variant, wherein amino acids 1-20 are deleted at the C- and/or N-terminus as recited in claim 4 of the present application. Wahren teaches that the substituted acid can be one of the well-known 20 conventional amino acids, comprising Cysteine (C) (instant claims 3, 5, and 16; Wahren, page 11, lines 14-16). Wahren teaches that the analogue may be modified at any one or combination of the leucine residues at positions 5, 12, 21, 24, 26, or 30 (12(L), instant claims 3, 5, and 16; Wahren, page 19, see 4th paragraph, lines 1-3; claims 1 and 6-9). Wahren teaches that C-peptide starts to degrade in as little as 15-20 minutes in an in vitro assay (Wahren, page 33, lines 6-9). Wahren teaches that C-peptide analogues show increased half-life of 20-35% in the in vitro assay (Wahren, page 37, see 2nd paragraph). Wahren teaches that it is important that the C-peptide analogues retain C-peptide activity (Wahren , page 15, 2nd paragraph, lines 1-2) and that affinity tests based on measurements of protein binding may be used as activity tests of C-peptide (Wahren , page 17, lines 10-12).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Ligler of detecting analyte in the liquid phase exiting the column, with the method of Ngo, measuring the concentration of the displaced labeled antigen, because by measuring the displaced antigens and using a standard calibration curve, one can determine the concentration of the antigens in the test sample.
The artisan would have had a reasonable expectation of success in determining the amount of displaced ligand as evidenced by Ligler’s Figures 1-2 by using the measurement method of Ngo, because Ngo uses a displacement assay as taught by Ligler and Ligler shows that the assay was sensitive to changes in target analyte concentration (see Figures 1-2 of Ligler).
It would have further been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Ligler in view of Ngo, a displacement assay for the detection of C-peptide, wherein the ligand and the analyte both bind specifically to an immobilized antibody and the antibody binds with greater affinity to the analyte then the ligand, to arrive at the claimed C-peptide ligand with a substitution of the leucine residue at position 12 with cysteine, because Wahren teaches that the C-peptide analogues can be modified at any one or combination of the leucine residues at positions 5, 12, 21, 24, 26, or 30 and that the substitutions can be one of the well-known 20 conventional amino acids. Specifically, the combination would have been an obvious matter of selecting a substitution from the finite list of suitable alternatives, to arrive at a peptide comprising the C-peptide of SEQ ID No: 6, which is amino acids 8-17 of SEQ ID NO. 1 with a substitution of L(12) to C (SEQ ID No: 6 being applicant’s elected species), as claimed. See MPEP 2143 (I)(E). The ordinary artisan would have been motivated to do so, because of the teaching of Wahren that a substitution of the leucine residues, including the leucine residue at position 12 increases the stability of the C-peptide analogue and that the substitution comprises one of the well-known 20 amino acids, which include cysteine. Wahren teaches increased stability in an in vitro assay, while the native C-peptide starts being degraded within only 15-20 min.
The ordinary artisan would have a reasonable expectation of success, because Ligler teaches a method of detecting C-peptide in a displacement assay, where the displaced ligand can be structurally distinct form the analyte, for example C-peptide, as long as it binds specifically to the immobilized receptor and Wahren teaches modified C-peptide variants that retain affinity in a protein binding assay.
Regarding claim 6, Ligler teaches a labelled ligand or a labelled receptor in an immobilized ligand-receptor complex (Ligler, column 3, lines 37-40).
Regarding claim 7, Ligler teaches the label can be a fluorophore, a chromophore, a radiolabel, a metal colloid, an enzyme, or a chemiluminescent or bioluminescent molecule (Ligler, column 7, lines 39-42).
Regarding claims 8 and 9, Ligler and the cited art above teach a method comprising a displacement assay substantially as claimed.
Ligler teaches a support for the immobilized receptor or ligand that may be composed of glass, silicon, quartz, paper, nitrocellulose, or polymers (Ligler, column 8, lines 4-6). Ligler further teaches that the ligand-receptor pair may comprise antibody-antigen or hapten (Ligler, column 5, lines 32-35). Ligler further teaches that a labelled ligand or a labelled receptor is bound to an immobilized receptor (instant claim 8) or an immobilized ligand (instant claim 9; Ligler, column 4, lines 21-35). Ligler further teaches that the sample containing the analyte is passed through a column containing a labelled ligand-immobilized receptor complex and the amount of labelled ligand displaced by the analyte is detected in the liquid phase exiting the column (Ligler, column 10, lines 9-15). Ligler further teaches detecting biomolecules including C-peptide (Ligler, column 6, line 10).
Ligler fails to teach determining the amount of displaced ligand.
Ngo teaches that the presence of antigens in a test sample will displace the bound labeled antigens from the immobilized antibodies and that the amount of displaced labeled antigens is proportional to the amount of antigens present in the sample. Ngo further teaches that by measuring the concentration of labeled antigens displaced and using a standard calibration curve, the concentration of the antigens in the test sample can be determined (Ngo, page 1057, ‘Introduction’, lines 3-8).
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Ligler of detecting analyte in the liquid phase exiting the column, with the method of Ngo, measuring the concentration of the displaced labeled antigen, because by measuring the displaced antigens and using a standard calibration curve, one can determine the concentration of the antigens in the test sample.
The ordinary artisan would have had a reasonable expectation of success in determining the amount of displaced ligand as evidenced by Ligler’s Figures 1-2, which show that the assay was sensitive to changes in target analyte concentration.
Claims 17 and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Ligler et al. in view of Ngo et al. and Wahren et al., WO2005118638A1 (PTO-892, 01/09/2024) and further in view of Möhlig et al. Predictors of abnormal glucose metabolism in women with polycystic ovary syndrome. European journal of endocrinology. 2006 Feb;154(2):295-301.
Regarding claims 17 and 18, Ligler teaches a method comprising a displacement assay comprising binding a labelled ligand or a labelled receptor to an immobilized receptor or ligand to obtain an immobilized ligand-receptor complex (Ligler, especially at column 3, lines 16-39) for biomolecules including C-peptide (Ligler, column 6, line 10; claim 15). Ligler further teaches that the ligand-receptor pair may comprise antibody-antigen or hapten (Ligler, column 5, lines 32-35), meaning that the immobilized ligand-receptor complex is an antibody-ligand-complex as claimed instantly (see also claim 13).
Ligler further teaches that the labelled ligand or receptor may be the identical molecule as the analyte or may be structurally distinct from the analyte, so long as it and the analyte both bind specifically to the immobilized receptor or ligand (Ligler, column 7, lines 23-29).
Ligler further teaches that the sample containing the analyte is passed through a column containing a labelled ligand-immobilized receptor complex and the amount of labelled ligand displaced by the analyte is detected in the liquid phase exiting the column (Ligler, column 10, lines 9-15). This allows indication of the presence of the target analyte, which again may be C-peptide (see also column 10, lines 34-41).
Ligler does not teach that the ligand has a lower affinity to the anti-C-peptide antibody than wild type C-peptide. Ligler further fails to teach that the ligand is a C-peptide variant of the wild-type C-peptide of SEQ ID No: 1 comprising the amino acids between positions 8-17 of SEQ ID NO:1, and comprising a substituted amino acid at 12 (L). Ligler further fails to teach that the antibody directed against C-peptide is selected from a group comprising or is the antibody PEP-001.
Ngo teaches that in displacement assays, the antibody with the highest binding constant may not be the best for an assay with greatest sensitivity, because it makes the displacement of labeled antigen to the antibody by analyte antigens much more difficult and requires higher concentrations of antigen, rendering the assay less sensitive (Ngo, page 1060, lines 9-15). Ngo further teaches that antibodies with weaker affinity for the labeled antigens can be used or cross -reactive antibodies can be used that have greater affinity with analyte antigens than with the labeled antigens (Ngo, page 1060, lines 16-21).
Wahren teaches providing modified variants or analogues of C-peptide which have been modified to increase the in vivo half-life of C-peptide so as to provide a longer-lasting and more efficacious therapeutic agent, because a treatment with longer lasting action can be administered less often and would be of great clinical importance and utility (Wahren, page 7, see paragraph 1). Wahren further teaches that human C-peptide is a 31 amino acid peptide having the following sequence: EAEDLQVGQVELGGGPGAGSLQPLALEGSLQ (SEQ ID No: 1 of Wahren), the sequence being identical to that of SEQ ID No: 1 of the present application (Wahren, page 4, 3rd paragraph). Wahren further teaches that C-peptide is known to have a relatively short half-life. Wahren teaches that the analogue may be modified at any one or combination of the leucine residues at positions 5, 12, 21, 24, 26, or 30 (12(L), Wahren, page 19, see 4th paragraph, lines 1-3; claims 1 and 6-9). Wahren teaches that C-peptide starts to degrade in as little as 15-20 minutes in an in vitro assay (Wahren, page 33, lines 6-9). Wahren teaches that C-peptide analogues show increased half-life of 20-35% in the in vitro assay (Wahren, page 37, see 2nd paragraph). Wahren teaches that it is important that the C-peptide analogues retain C-peptide activity (Wahren , page 15, 2nd paragraph, lines 1-2) and that affinity tests based on measurements of protein binding may be used as activity tests of C-peptide (Wahren , page 17, lines 10-12).
Möhlig teaches that clone PEP-001 is a mouse monoclonal anti-human C-peptide antibody.
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Ligler of detecting analyte in the liquid phase exiting the column, with the method of Ngo, measuring the concentration of the displaced labeled antigen, because by measuring the displaced antigens and using a standard calibration curve, one can determine the concentration of the antigens in the test sample.
The artisan would have had a reasonable expectation of success in determining the amount of displaced ligand as evidenced by Ligler’s Figures 1-2 by using the measurement method of Ngo, because Ngo uses a displacement assay as taught by Ligler and Ligler shows that the assay was sensitive to changes in target analyte concentration (see Figures 1-2 of Ligler).
It would have further been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Ligler in view of Ngo, a displacement assay for the detection of C-peptide, wherein the ligand and the analyte both bind specifically to an immobilized antibody and the antibody binds with greater affinity to the analyte then the ligand, to arrive at the claimed C-peptide ligand with a substitution of the leucine residue at position 12 with cysteine, because Wahren teaches that the C-peptide analogues can be modified at any one or combination of the leucine residues at positions 5, 12, 21, 24, 26, or 30 and that the substitutions can be one of the well-known 20 conventional amino acids. Specifically, the combination would have been an obvious matter of selecting a substitution from the finite list of suitable alternatives, to arrive at a peptide comprising the C-peptide of SEQ ID No: 6, which is amino acids 8-17 of SEQ ID NO. 1 with a substitution of L(12) to C (SEQ ID No: 6 being applicant’s elected species), as claimed. See MPEP 2143 (I)(E). The ordinary artisan would have been motivated to do so, because of the teaching of Wahren that a substitution of the leucine residues, including the leucine residue at position 12 increases the stability of the C-peptide analogue and that the substitution comprises one of the well-known 20 amino acids, which include cysteine. Wahren teaches increased stability in an in vitro assay, while the native C-peptide starts being degraded within only 15-20 min.
One of ordinary skill in the art would have a reasonable expectation of success, because Ligler teaches a method of detecting C-peptide in a displacement assay, where the displaced ligand can be structurally distinct form the analyte, for example C-peptide, as long as it binds specifically to the immobilized receptor and Wahren teaches modified C-peptide variants that retain affinity in a protein binding assay.
It would have further bee prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have use the antibody PEP-001 in the method of Ligler and the cited art above because the combination of the art teaches a method to detect human C-peptide and PEP-001 is a monoclonal anti-human C-peptide antibody.
One of ordinary skill in the art would have a reasonable expectation of success because Ligler teaches a method of detecting a protein, including C-peptide, in a sample using an antibody and PEP-001 is an anti-C-peptide antibody.
Response to Arguments
Applicant’s arguments, see page 7, filed 03/31/2026, with respect to the rejection under 35 U.S.C. §112(a) of claims 1, 8, and 9 (and the dependent claims) have been fully considered and are persuasive. The recitation of specific antibody clones in the specification provides support that the applicant was in possession of the claimed subject matter. The rejection of claims 1, 3-9, and 16 has been withdrawn.
Applicant's arguments filed 03/31/2026 regarding the rejection under 35 U.S.C. §103 have been fully considered but they are not persuasive.
Applicant states on page 7 that arguments presented in the previous amendment and response filed 05/06/2025 are incorporated by reference.
The response to the arguments in the final office action (of record, 10/01/2025) is maintained.
Applicant further argues that new claims 17 and 18 recite specific anti-C-peptide antibodies that can be used to practice the invention and that said anti-C-peptide antibodies are listed in the specification. Therefore claims 17-19 are clearly enabled and described by the application.
However, while the method is enabled using specific anti-C-peptide antibodies to detect C-peptide in a sample, new claims 17-19 are rejected under 35 U.S.C. §103 (see above).
For all the reasons above, the arguments are not persuasive.
Communication
Any inquiry concerning this communication or earlier communications from the examiner should be directed to STEFANIE J KIRWIN whose telephone number is (571)272-6574. The examiner can normally be reached Monday - Thursday 7.30 - 4 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Bao-Thuy Nguyen can be reached at (571) 272-0824. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/STEFANIE J. KIRWIN/Examiner, Art Unit 1677
/Soren Harward/Primary Examiner, TC 1600
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