DETAILED ACTION
Claims 1-2, 4, 6-11, 14-16, 19-25 are pending.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 02/04/2026 has been entered.
Information Disclosure Statement
The information disclosure statement filed on 11/05/2025 has been considered by the examiner.
Status of Claims
Claims 1-2, 4, 6-11, 14-16, 19-25 are pending. Claims 1, 4, 19-23 have been amended. Claims 24-25 have been newly added.
Claims 1-2, 4, 6-11, 14-16, 19-25 are under examination.
Withdrawn Claim Objections and/or Rejections
The arguments filed on 02/04/2026 have been considered by the examiner.
The rejection of claims 1-2, 4, 9-10, and 13-23 under 35 USC 103 as being unpatentable over Winderickx and Vanmechelen et al., as set forth on pp. 2-12 of the previous office action (mailed on 10/10/2025) has been withdrawn in view of the amended claims (filed on 02/04/2026).
The rejection of claims 6-8 and 11 under 35 USC 103 as being unpatentable over Winderickx, Vanmechelen, and Vandermeeren et al., as set forth on pp. 12-15 of the previous office action (mailed on 10/10/2025) has been withdrawn in view of the amended claims (filed on 02/04/2026).
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.
Claim 23 and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Sankaranarayanan et al., (WO 2014011972A1) (effectively filed on 07/12/2013) (IDS filed on 07/27/2022), in view of Winston et al., “Conjugation of enzymes to antibodies.” Current protocols in molecular biology vol. Chapter 11 (2001): Unit 11.1. doi:10.1002/0471142727.mb1101s50.
Instant claim 23 recites “An antibody conjugate comprising (1) a labeled carrier and (2) at least two different anti-tau protein antibodies covalently bound to the labeled carrier, wherein the labeled carrier is (A) an enzyme, or (B) a carrier protein bound to the enzyme, wherein the antibody conjugate is capable of binding to and detecting a tau protein in an immunoassay assay, and wherein the at least two different anti-tau protein antibodies are anti-tau protein antibodies which recognize different sites in the tau protein”.
Sankaranarayanan teaches an antibody conjugate comprising (1) a labeled carrier and (2) at least two different anti-tau protein antibodies bound to the labeled carrier, wherein the labeled carrier is (A) an enzyme or (B) a carrier protein bound to the enzyme (see page 22 lines 28-32 “Membranes were probed with HT7 (Pierce), Tau12 (Covance, Dedham, MA), KJ9A (Dako, Carpinteria, CA), 30 and mouse IgG 1 monoclonal isotype control (Abeam, Cambridge, MA) conjugated to HRP (LYNX Rapid HRP Antibody Conjugation kit, AbD Serotec, Oxford, UK) in TBST with 1 % BSA for 16 hrs at room temperature.”),
wherein the antibody conjugate is capable of binding to and detecting a tau protein in an immunoassay assay (see page 22 lines 23-32 teaching the use of the enzyme conjugated with two antibodies in a western blot)
wherein the at least two different anti-tau protein antibodies are anti-tau protein antibodies which recognize different sites in the tau protein (see page 22 lines 28-32 “Membranes were probed with HT7 (Pierce), Tau12 (Covance, Dedham, MA), KJ9A (Dako, Carpinteria, CA), 30 and mouse IgG 1 monoclonal isotype control (Abeam, Cambridge, MA) conjugated to HRP (LYNX Rapid HRP Antibody Conjugation kit, AbD Serotec, Oxford, UK) in TBST with 1 % BSA for 16 hrs at room temperature.”), see page 18 lines 28-31 and page 19 lines 1-9 “In a specific embodiment, the present invention provides a kit comprising: (1) a first antibody which binds to an N-terminal portion of a Tau protein; (2) a second antibody which binds to a middle portion of a Tau protein; and (3) reagents necessary for facilitating an antibody-antigen complex formation. To illustrate, the first antibody is Taul2, and the second antibody is selected from BT2, HT7, Tau5, AT270, and PHF6.In another specific embodiment, the present invention provides a kit comprising: (1) a first antibody which binds to amino acid residues 159-163 of Tau 441 (SEQ ID NO: 1); (2) a second antibody which binds to amino acid residues 194- 198, residues 218-225, or the phosphorylated threonine residue 231 of Tau 441 (SEQ ID NO: 1); and (3) reagents necessary for facilitating an antibody-antigen complex formation. To illustrate, the first antibody is HT7, and the second antibody is selected from BT2, Tau5, and PHF6.”) (instant claim 23).
Sankaranarayanan teaches wherein the at least two different anti-tau antibodies are selected from a group consisting of a monoclonal antibody BT2, a monoclonal antibody HT7, and a monoclonal antibody AT270 (see claim 18 of Sankaranarayanan, see page 3 lines 9-17 “In certain embodiments, the present invention provides a method of detecting the level of at least one Tau protein in a biological sample, comprising: (a) contacting a biological sample from a subject with a first antibody which binds to amino acid residues 159-163 of Tau 441 (SEQ ID NO: 1), and a second antibody which binds to amino acid residues 194-198, residues 218-225, or the phosphorylated threonine residue 231 of Tau 441 (SEQ ID NO: 1), wherein the first antibody and the second antibody both bind to the Tau protein to form a complex; and (b) detecting the level of the Tau protein in the complex. To illustrate, the first antibody is HT7, and the second antibody is selected from BT2, Tau5, and PHF6.”) (instant claim 25).
Sankaranarayanan does not teach the antibodies being covalently bound to the labeled carrier.
Winston teaches antibodies being covalently bound to the labeled carrier (see page 1 unit 11.1 “Conjugation of enzymes to antibodies involves the formation of a stable, covalent linkage between an enzyme [e.g., horseradish peroxidase (HRPO), urease, or alkaline phosphatase] and an antigen-specific monoclonal or polyclonal antibody in which neither the antigen-combining site of the antibody nor the active site of the enzyme is functionally altered.”) (instant claim 23).
It would have been obvious to one of ordinary skill in the art at the time of the instant application to modify the tau antibody conjugate taught by Sankaranarayanan with the methods of enzyme-antibody conjugation that is covalently bound taught by Winston. Winston provides motivation by teaching that in order to conjugate enzymes to antibodies, they have to contain a covalent linkage between them (see page 1 unit 11.1). Winston provides motivation by teaching that direct conjugation of enzymes to antibodies has greatly simplified the development and performance of many different types of immunoassays (see page 6 unit 11.1.6). Winston teaches that the method of covalently bonding an enzyme to antibodies is a known technique in the art (see page 1 unit 11.1). The artisan would have reasonable expectation of success based on the cumulative disclosure of these prior art references at the time the instant application was filed.
Allowable Subject Matter
Claims 1-2, 4, 6-11, 14-16, 19-22 and 24 are allowed.
Claims 1-2, 4, 6-11, 14-16, 19-22 and 24 are allowed because there is no prior art that teach or suggests the claimed invention of an antibody conjugate that comprises (1) a labeled carrier and (2) at least two different anti-tau protein antibodies covalently bound to the labeled carrier, wherein the at least two different anti-tau protein antibodies comprise a first antibody that recognizes an epitope present between positions 153 and 169 in the amino acid sequence of SEQ ID NO:1 and a second antibody that recognizes an epitope present between positions 188 and 207 in the amino acid sequence of SEQ ID NO:1.
The closest prior art for claims 1-2, 4, 6-11, 14-16, 19-22 and 24 is Sankaranarayanan et al., (WO 2014011972A1) (IDS filed on 07/27/2022). Sankaranarayanan teaches an antibody conjugate comprising (1) a labeled carrier and (2) at least two different anti-tau protein antibodies bound to the labeled carrier, wherein the labeled carrier is (A) an enzyme, or (B) a carrier protein bound to the enzyme, wherein the antibody conjugate is capable of binding to and detecting a tau protein in an immunoassay.
Sankaranarayanan does not teach or suggest wherein the at least two different anti-tau protein antibodies comprise a first antibody that recognizes an epitope present between positions 153 and 169 in the amino acid sequence of SEQ ID NO:1 and a second antibody that recognizes an epitope present between positions 188 and 207 in the amino acid sequence of SEQ ID NO:1.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MCKENZIE A DUNN whose telephone number is (571)270-0490. The examiner can normally be reached Monday-Tuesday 730 am -530pm, Wednesday-Friday 730 am-430 pm.
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, Gregory Emch can be reached at (571)272-8149. 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.
/MCKENZIE A DUNN/Examiner, Art Unit 1678
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678