METHODS AND REAGENTS FOR THE DETECTION OF ANALYTES

§102 §103 §112

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 . Election/Restrictions 2. Applicant’s election without traverse of Group I (claims 1-11, 13-17, 20-21, 24, 27-28, 31, 34, 37, 43, 45, and 47) and AAV (AAV9 if needed) as the bait molecule in the reply filed on 21 July 2026 is acknowledged. It is noted that the species election for the bait molecule will be taken as an election for AAV9. Claims 9-11, 14-16, 34, 43, 47, and 53 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and/or species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 21 July 2026. It is noted that claim 34 has been withdrawn as the complement C9 protein will not bind to the bait molecule, nor binds to the antibodies that will bind to the bait molecule. Claim Status 3. Claims 12, 18-19, 22-23, 25-26, 29-30, 32-33, 35-36, 38-42, 44, 46, 48-52, and 54-60 are canceled. Claims 9-11, 14-16, 34, 43, 47, and 53 are withdrawn. Claims 1-8, 13, 17, 20-21, 24, 27-28, 31, 37, and 45 are under consideration. Priority 4. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. The Instant Application is a 371 National Stage Application that claims priority to foreign application GB 2110404.7, filed 20 July 2021. Claims 1-8, 13, 17, 20-21, 24, 27-28, 31, 37, and 45 are supported by the foreign priority document and thus U.S. effective filing date of these claims is 20 July 2021. 5. It is noted that the Instant Specification does not have a statement referencing the prior-filled foreign priority application. While not required, it is encouraged by the Office to provide an explicit incorporation by reference statement. See MPEP 213.02(I). Information Disclosure Statement 6. The information disclosure statements (IDS) submitted on 11 April 2024 were filed before the mailing date of the Non-Final Office Action. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. 7. The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered. Drawings 8. The drawings are objected to for the following reasons: The figure labels for figures 1, 1A, 4, 6-9, 11A, 12, 13F, 14, 15B-C, and 16-22 do not go the same way as the figures themselves. Figures 1, 1A, and 19-20 are indiscernible. The caption for figure 5 caption recites (i)-(ii) but the figures go to (iii). Page 47 of the drawings (presumably Figure 14A) is not labeled as such. Figures 9, 11-13, and 17-18 refers to colors in the caption when the drawings are not in color. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Color photographs and color drawings are not accepted in utility applications unless a petition filed under 37 CFR 1.84(a)(2) is granted. Any such petition must be accompanied by the appropriate fee set forth in 37 CFR 1.17(h), one set of color drawings or color photographs, as appropriate, if submitted via the USPTO patent electronic filing system or three sets of color drawings or color photographs, as appropriate, if not submitted via the via USPTO patent electronic filing system, and, unless already present, an amendment to include the following language as the first paragraph of the brief description of the drawings section of the specification: The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. Color photographs will be accepted if the conditions for accepting color drawings and black and white photographs have been satisfied. See 37 CFR 1.84(b)(2). Nucleotide and/or Amino Acid Sequence Disclosures 9. 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: 10. Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d). Required response – Applicant must provide: A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, 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. See pages 80 and 112 of the Instant Application. 11. Specific deficiency - The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing or incomplete. See item 1) a) or 1) b) above. Required response – Applicant must provide: A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, 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 12. The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. 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://, www., or other browser-executable code. See MPEP § 608.01. See pages 28, 35, 80, and 112 of the Instant Specification. 13. The use of the terms “EDI” (Page 2), “Liaison” (Page 2), and “Elecsys” (Page 78), which are trade names or marks used in commerce, have been noted in this application. The terms should be accompanied by the generic terminology; furthermore the terms should be capitalized wherever they appear or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the terms. Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Note that these are merely examples and all improper uses of trademarks in the specification should be identified by Applicant and properly addressed. Claim Objections 14. Claims 1 and 20 are objected to because of the following informalities: Regarding claim 1, “one or more” should be inserted before “binding molecules” in line 2 for consistency. Regarding claim 20, there should be a comma inserted after “IgG3” for clarity. Appropriate correction is required. Claim Rejections - 35 USC § 112(b) 15. 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. 16. Claims 7-8, 13, 17, 20-21, 24, 27-28, 31, and 37 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. Regarding claims 7, 13, 20, and 21, the phrases "such as", “e.g.”, and “preferably” render the claim indefinite because it is unclear whether the limitations following the phrases are part of the claimed invention. See MPEP § 2173.05(d). Claims 8, 17, 20-21, 24, 27-28, 31, and 37, which are dependent on claim 7, are similarly rejected. Claim Rejections - 35 USC § 102 17. 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. (a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention. 18. Claims 1-6 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Music (2019, Clin. Proteom., 16(25)). Regarding claims 1-6, Music teaches methods of identifying autoantibody protein targets in serum samples from patients with inflammatory bowel disease (Abstract). Music teaches using an immuno-mass spectrometry (immuno-MS) approach with the following steps (Figure 1): PNG media_image1.png 296 603 media_image1.png Greyscale As illustrated by the figure, “First, all the IgG antibodies, including the autoantibodies, in serum are captured and purified on protein G beads, followed by addition of a protein mix containing thousands of human proteins. This is followed by exhaustive washing of the beads, captured antigen digestion by trypsin and shotgun tandem mass spectrometry (MS) analysis (Fig. 1). Protein G is a streptococcal bacteria cell wall protein that has a very high affinity for immunoglobulin G (IgG), and can be used to purify IgG from the sera of various species. MS is a powerful tool for the precise identification and quantification of the constituents in a complex protein sample.” (Introduction, ¶ 2). In summary, Music teaches a method of identifying and quantifying autoantibody protein targets (binding molecule) in human serum samples by adding the serum samples to form complexes with the antibodies and protein G (bait molecules), digesting the complexes with trypsin (a type of proteolytic digestion), and subjecting them to mass spectrometry. The binding, incubating, and washing causes the isolation of the complex: “We used the protocol of Fig. 1 to immunoaffinity purify proteins on previously captured autoantibodies from serum.” (Identification of CUZD1 and GP2 Proteins, ¶ 1). The magnetic beads are a surface in which the bait molecules are bound prior to addition of the sample. These bait molecules are still bound to the magnetic beads both during and after the isolation process as they are part of the binding complexes. Claim Rejections - 35 USC § 103 19. 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. 20. 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. 21. Claims 1-8, 13, 17, 24, 28, 31, 37, and 45 are rejected under 35 U.S.C. 103 as being unpatentable over Music (2019, Clin. Proteom., 16(25)) in view of Jiang (14 July 2020, Nature Communications, 11(3581)) and Falese (07 December 2017, Gene Ther., 24(12): 768-778). Regarding claims 1-8, 13, 17, 24, and 45, Music teaches methods of identifying autoantibody protein targets in serum samples from patients with inflammatory bowel disease (Abstract). Music teaches using an immuno-mass spectrometry (immuno-MS) approach with the following steps (Figure 1): PNG media_image1.png 296 603 media_image1.png Greyscale As illustrated by the figure, “First, all the IgG antibodies, including the autoantibodies, in serum are captured and purified on protein G beads, followed by addition of a protein mix containing thousands of human proteins. This is followed by exhaustive washing of the beads, captured antigen digestion by trypsin and shotgun tandem mass spectrometry (MS) analysis (Fig. 1). Protein G is a streptococcal bacteria cell wall protein that has a very high affinity for immunoglobulin G (IgG), and can be used to purify IgG from the sera of various species. MS is a powerful tool for the precise identification and quantification of the constituents in a complex protein sample.” (Introduction, ¶ 2). In summary, Music teaches a method of identifying and quantifying autoantibody protein targets (binding molecule) in human serum samples by adding the serum samples to form complexes with the antibodies and protein G (bait molecules), digesting the complexes with trypsin (a type of proteolytic digestion), and subjecting them to mass spectrometry. The binding, incubating, and washing causes the isolation of the complex: “We used the protocol of Fig. 1 to immunoaffinity purify proteins on previously captured autoantibodies from serum.” (Identification of CUZD1 and GP2 Proteins, ¶ 1). The magnetic beads are a surface in which the bait molecules are bound prior to addition of the sample. These bait molecules are still bound to the magnetic beads both during and after the isolation process as they are part of the binding complexes. Music does not teach using this method with a virus or to detect antibodies. However, Jiang teaches a SARS-CoV-2 proteome microarray to detect IgG and IgM responses (Page 1), wherein the SARS-CoV-2 proteins and controls were printed onto a substrate slide (Page 9, Protein microarray fabrication); incubated with blocking buffer and then serum samples with eGFP and PBS; and finally the bound antibodies were detected by incubating with Cy3-conjugated goat anti-human IgG and Alexa Fluor 647-conjugated donkey anti-human IgM and florescence was measured (Page 10, Microarray-based serum analysis). Therefore, it would have been obvious to one of ordinary skill before the effective filing date to take the method of Music and apply the method of Jiang to it. This would result in magnetic beads with SARS-CoV-2 proteins as the bait molecules and IgG/IgM as the binding molecules. Instead of florescence, mass spectrometry can be used to quantify the antibodies, as done with the bound proteins in Music. This would result in a reasonable expectation of success. It would also be equally obvious to use a full SARS-CoV-2 virion with a reasonable expectation of success. The combination of familiar elements is likely to be obvious when it does no more than yield predictable results. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395 – 97 (2007) (see MPEP § 2143, A.). A rationale to support a conclusion that a claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would have yielded nothing more than predictable results to one of ordinary skill in the art. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395 (2007) (see MPEP §§ 2143, A. and 2143.02). In summary, Music in view of Jiang make a method of identifying and quantifying IgG and IgM (binding molecules) against SARS-CoV-2 proteins (bait molecules) bound on a surface (magnetic beads) by contacting the bound bait molecules with human serum to form complexes, isolating the complexes by washing, and identifying and quantifying the IgG/IgM using mass spectrometry. Regarding claims 28, 31, and 37, the combination of Music and Jiang makes claim 7 obvious, as discussed supra. All discussions thereon incorporated here. Music further teaches “Our methodology can also identify immune complexes that are present in the serum, such as antibodies bound to complement proteins and apolipoproteins” (Page 7, ¶ 1). None of the references teach the specific complement proteins. However, West (15 June 2023, Hum. Gene Ther., 34(11-12): 554-566) evidences that complement C4B binds to AAV9 capsid (Table 1) and complement C1q interacts with AAV9 capsid in the presence of antibodies (Page 560, ¶ 1). C4B would bind to the AAV9 bait molecule made obvious above, C4BP binds to C4B and thus would be present when C4B is present, and C1q would bind to the AAV9 antigen-antibody complex. Therefore, it would be obvious to one of ordinary skill before the filing date that the method made obvious by Music and Jiang can be used to measure complement proteins. Regarding the species election of AAV9 as the bait molecule, none of the claims are explicitly drawn to this embodiment. However, regarding claims 7-8, 13, 17, and 24 with this election in mind, claim 1 is taught by Music and Jiang as discussed supra. All discussions thereon incorporated here. Neither Music nor Jiang teach using AAV or rAAV as the bait molecule. However, Falese teaches assays to detect pre-existing AAV5 immunity in humans by detecting antibodies and neutralizing factors (Abstract). Falese teaches coating MSD plates in AAV5 capsids, adding human serum, adding ruthenium-labeled AV5 capsid and MSD read buffer, and detecting total antibodies with electrochemiluminescence (Page 776, AAV5 Tab assay for human plasma). Therefore, it would have been obvious to one of ordinary skill before the effective filing date to take method made obvious by Music and Jiang, and further using AAV5 capsid as the bait molecule to detect anti-AAV5 antibodies. It would further be obvious to substitute AAV5 for AAV9, as any bait molecule would predictably be functional in this assay to detect any antibodies or binding proteins. Additionally, if the full capsid can be used, then a rAAV9 vector would be equally obvious. A full AAV9 virion would likewise be obvious. The simple substitution of one known element for another is likely to be obvious when predictable results are achieved. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, USPQ2d 1385, 1395 – 97 (2007) (see MPEP § 2143, B.). In summary, Music in view of Jiang and Falese make a method of identifying and quantifying IgG and IgM (binding molecules) against AAV9 or rAAV9 (bait molecules) bound on a surface (magnetic beads) by contacting the bound bait molecules with human serum to form complexes, isolating the complexes by washing, and identifying and quantifying the IgG/IgM using mass spectrometry. 22. Claims 20-21 and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Music (Supra), Jiang (Supra), and Falese (Supra) as applied to claims 1-8, 13, 17, 24, 28, 31, 37, and 45 above, and further in view of Ladwig (05 May 2017, Clin. Vaccine Immunol., 24(5)), Yates (15 June 2021, Cell Rep. Med., 2(7): 100329), and Sterlin (20 January 2021, Science Translational Medicine, 13). Regarding claims 20-21 and 27, the combination of Music and Jiang makes claims 7 and 17 obvious as discussed supra. All discussions thereon incorporated here. None of the references teach identifying and quantifying IgG isotypes or IgA, nor do they teach detecting antibody isotype by conserved peptide sequences. However, Ladwig teaches “When using mass spectrometry (MS) to characterize and quantify MAbs, the variable region is the target and its uniqueness is compared to the endogenous polyclonal Ig repertoire. The conserved amino acid sequences designate the heavy chain isotype IgG, IgA, IgM, IgD, or IgE and the light chain either kappa or lambda. The IgG isotype has four subclasses with different characteristics: IgG1, IgG2, IgG3, and IgG4. Therapeutic MAbs currently on the market are predominately IgG1 kappa, with a few being IgG2, IgG4, or hybrids.” (Page 2, ¶ 2). This conserved sequence would not be in the variable region. Furthermore, Yates teaches “We found that IgG1 and IgG3 were the dominant IgG subclasses produced in response to SARS CoV-2 infection (Figure 3A). The responses to nucleocapsid, RBD, and S1 subunit were each dominated by IgG1, with over 90% of specimens testing positive (Table S3). Strikingly, the IgG response toward the S2 subunit was dominated by the IgG3 subclass, with 94% of specimens yielding a positive clinical result. IgG2 responses were moderate, with a positivity rate ranging from 8% to 21%. Finally, IgG4 responses were especially rare with a clinical positivity rate of 0%–9% (Figure S1; Table S3).” (Page 4) and Sterlin teaches “Early SARS-CoV-2–specific humoral responses were dominated by IgA antibodies. Peripheral expansion of IgA plasmablasts with mucosal homing potential was detected shortly after the onset of symptoms and peaked during the third week of the disease. The virus-specific antibody responses included IgG, IgM, and IgA, but IgA contributed to virus neutralization to a greater extent compared with IgG. Specific IgA serum concentrations decreased notably 1 month after the onset of symptoms, but neutralizing IgA remained detectable in saliva for a longer time (days 49 to 73 post-symptoms).” (¶ 1). Therefore, it would have been obvious to one of ordinary skill before the filing date to identify and quantify IgG isotype and IgA antibodies and to identify the antibody isotype by its conserved sequence using the method made obvious supra. The combination of familiar elements is likely to be obvious when it does no more than yield predictable results. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395 – 97 (2007) (see MPEP § 2143, A.). A rationale to support a conclusion that a claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would have yielded nothing more than predictable results to one of ordinary skill in the art. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395 (2007) (see MPEP §§ 2143, A. and 2143.02). The identification and quantification of the different types of antibodies and isotypes can aid in determining the exact type of immune response to the bait molecules at different stages of infection, as supported above. A rationale to support a conclusion that a claim would have been obvious is that there is some teaching, suggestion, or motivation in the prior art or in the knowledge generally available to one of ordinary skill in the art to modify the reference or combine reference teachings, and the modification or combination would have a reasonable expectation of success. See KSR International Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395 (2007) (see MPEP §§ 2143, G. and 2143.02). Conclusion 23. No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to KRISTINA E LY whose telephone number is (571)272-5169. The examiner can normally be reached Monday - Thursday, 8:00 am - 5:00 pm EST. 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, Michael Allen can be reached at (571) 270-3497. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /KRISTINA E. LY/Examiner, Art Unit 1671 /Michael Allen/Supervisory Patent Examiner, Art Unit 1671