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 .
Election/Restrictions
1. Applicant’s election of Group I, claims 1-13 in the reply filed on November 10, 2025 and the IgBP peptide species SEQ ID NO: 2 without traverse is acknowledged.
2. Claims 1-24 are pending.
3. Claims 3, 4, 8, 9 and 14-24 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species or invention, there being no allowable generic or linking claim.
4. Claims 1, 2, 5-7 and 10-13 are currently under consideration as drawn to the elected species.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
5. 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:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification at p. 3-lines 24-25 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.
Priority
6. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Specification
7. The specification is objected to as failing to provide proper antecedent basis for the claimed subject matter. See 37 CFR 1.75(d)(1) and MPEP § 608.01(o). The claimed subject matter that does not have antecedent basis in the specification is in claim 2, i.e., [t] he method according to claim 1, wherein the Carrier-binding IgBP is IgG or an Fc fusion protein.
It is noted that original claim 2, prior to the preliminary amendment of 04/21/2022, was drawn to [t] he method according to claim 1, wherein the Fc molecule is IgG or an Fc fusion protein.
Because the claims as filed in the original specification are part of the disclosure, even though the material disclosed in the claims is not disclosed in the remainder of the specification, the applicant may amend the specification to include the claimed subject matter. In re Benno, 768 F.2d 1340, 226 USPQ 683 (Fed. Cir. 1985). Thus amendment of the specification to include the material disclosed in the claims will obviate this objection.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
6. Claims 1, 2, 5-7 and 10-13 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.
The preamble of claim 1 recites “A method for increasing a proportion of an Fc molecule where one Fc-binding IgBP, per Fc molecule, is bound, in an Fc molecule reacted with Fc-binding IgBP”. It is unclear if the claims are drawn to increasing the proportion an Fc molecule where one Fc-binding IgBP, per Fc molecule, is bound in a composition or increasing the proportion of Fc-binding IgBP molecules bound to the Fc molecule or some other proportion. Thus, this limitation makes claims 1, 2, 5 and 6 indefinite.
Although claim 6 recites “wherein a proportion of an Fc molecule where one IgBP is bound to one Fc molecule, relative to the entire Fc molecule, in an Fc molecule composition is 55% or more,” it still unclear if the proportion is referring to the proportion of Fc-binding IgBP bound to the Fc molecule or the proportion an Fc molecule where one Fc-binding IgBP per Fc molecule is bound compared to the total amount Fc molecule in the composition.
Amendment of claim 6 to, e.g., “wherein the proportion of an Fc molecule where one IgBP is bound to one Fc molecule, compared to the total amount of Fc molecule in an Fc molecule composition is 55% or more,” would help to obviate this rejection.
The term “a large amount of an IGBP-bound Fc” in claim 7 is a relative term which renders the claim indefinite. The term “a large amount of an IGBP-bound Fc” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention.
Section 2171 of the M.P.E.P. states
Two separate requirements are set forth in 35 U.S.C. 112(b) and pre-AIA 35 U.S.C. 112, second paragraph, namely that:
(A) the claims must set forth the subject matter that the inventor or a joint inventor regards as the invention; and
(B) the claims must particularly point out and distinctly define the metes and bounds of the subject matter to be protected by the patent grant.
The first requirement is a subjective one because it is dependent on what the inventor or a joint inventor for a patent regards as his or her invention. Note that although pre-AIA 35 U.S.C. 112, second paragraph, uses the phrase "which applicant regards as his invention," pre-AIA 37 CFR 1.41(a) provides that a patent is applied for in the name or names of the actual inventor or inventors.
The second requirement is an objective one because it is not dependent on the views of applicant or any particular individual, but is evaluated in the context of whether the claim is definite — i.e., whether the scope of the claim is clear to a hypothetical person possessing the ordinary level of skill in the pertinent art.
In the instant case of “a large amount of an IGBP-bound Fc”, one of skill in the art could find representative examples in the art which have been defined in such terms, however, it is unclear at what point one of skill in the art would be infringing on the claims without limitations as to the metes and bounds of “a large amount of an IGBP-bound Fc” and the amount of deviation acceptable under the term. Although claims 12 and 13 recite a specific proportion of IgBP bound Fc molecule, the claims do not define the proportions as the “large amount of an IGBP-bound Fc” of the preamble.
Claim Rejections - 35 USC § 102
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.
7. Claim(s) 1, 2, 5 and 6 are rejected under 35 U.S.C. 102(a)(1) as being anticipate by US 2010/0297606 A1 (Ito, Y. Nov. 25, 2010, IDS), “Ito”.
Ito teaches a peptide tag capable of specifically binding to human IgG or an Fc containing fragment thereof. See abstract and ¶¶ 0008-0030
Ito teaches the present invention also relates to a method for purifying human IgG or an Fc region-containing fragment thereof in a sample, comprising the following steps a) and b): a) contacting the peptide tag of the present invention with an acid-treated sample, thereby binding human IgG or an Fc region-containing fragment thereof in a sample to the peptide tag; and b) separating the human IgG or the Fc region-containing fragment thereof bound to the peptide tag prepared by step a) from the sample. See ¶¶ [0126]-[0128].
Ito teaches, after contacting of the peptide tag of the present invention with an acid-treated sample, human IgG or an Fc region-containing fragment thereof bound to the peptide tag as a result of contacting can be separated from the sample by a technique for separation and purification of biological molecules well-known to persons skilled in the art. For example, when the peptide tag immobilized on a solid-phase support such as a column, a plate, or a sensor chip is used, human IgG or an Fc region-containing fragment thereof bound to the peptide tag on the solid-phase support can be separated from the other ingredients in the sample by washing the solid-phase support after contacting under conditions where the peptide tag does not dissociate from the solid-phase support. See ¶ 0131.
Regarding the preamble of claim 1, when reading the preamble in the context of the entire claim, the recitation of “[a] method for increasing a proportion of an Fc molecule where one Fc-binding IgBP, per Fc molecule, is bound, in an Fc molecule reacted with Fc-binding IgBP” is not limiting because the body of the claim describes a complete invention and the language recited solely in the preamble does not provide any distinct definition of any of the claimed invention’s limitations. Thus, the preamble of the claim(s) is not considered a limitation and is of no significance to claim construction. See Pitney Bowes, Inc. v. Hewlett-Packard Co., 182 F.3d 1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See MPEP § 2111.02.
Regarding claim 6, a wherein clause in a method claim is not given patentable weight when it simply expresses the intended result of a process step positively recited. See MPEP 2111.04 (I).
Claim Rejections - 35 USC § 103
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.
8. Claim(s) 1, 2, 5-7 and 10-13 are rejected under 35 U.S.C. 103 as being unpatentable over US 2010/0297606 A1 (Ito, Y. Nov. 25, 2010, IDS), “Ito”.
Ito teaches as set forth above.
Ito also teaches the present invention relates to a method for purifying a protein, comprising the following steps a) to c): a) producing a fusion protein containing a protein linked to the peptide tag of the present invention and then preparing a sample containing the fusion protein; b) contacting the sample prepared by step a) with acid-treated human IgG or an Fc region-containing fragment thereof, thereby binding the fusion protein to the human IgG or Fc region-containing fragment thereof; and c) separating the fusion protein bound to the human IgG or Fc region-containing fragment thereof prepared by step b) from the sample. See ¶¶ 0145-0149.
Ito also teaches the fusion protein may have a cleavable link (e.g., protease recognition site) between the peptide tag and a protein of interest. See ¶¶ 0149.
Ito also teaches when a fusion protein has a linker containing a cleavable link (e.g., protease recognition site), the fusion protein is separated from the sample and then subjected to cleavage such as protease treatment so as to separate a protein of interest from the peptide tag of the present invention. and they can be each recovered and purified separately. See ¶¶ 0155.
Ito also teaches injecting a IgG binding peptide tag and antibody into a column for separation of acid denatured IgG. See Examples 10 and ¶¶ 0207 and 0212, in particular.
Ito does not explicitly teach cutting a bond between the Carrier-binding IgBP and the Fc molecule to recover the bound product of the Fc-binding IgBP and the Fc molecule from the carrier or injecting an Fc molecule to a column to which a Carrier-binding IgBP is bound.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Ito inject an Fc molecule to a column to which a Carrier-binding IgBP is bound to bind the Fc molecule to Fc binding peptide with a cleavable linker that could be enzymatically cleaved to recover the bound product of the Fc-binding IgBP and the Fc molecule from the carrier because Ito teaches using column injection techniques and cleavable linkers for purification of Fc containing fragments. One would have been motivated with a reasonable expectation to use column injection techniques and cleavable linkers for purification of Fc containing fragments because these are routine protein purification methods in the art as exemplified by the teachings of Ito.
Regarding the preamble of claim 7, when reading the preamble in the context of the entire claim, the recitation of “[a] method for preparing a Fc molecule composition comprising a large amount of an IgBP-bound Fc molecule where only one IgG affinity peptide for Fc molecule binding (Fc-binding IgBP) is bound to one molecule having an Fc region (Fc molecule)” is not limiting because the body of the claim describes a complete invention and the language recited solely in the preamble does not provide any distinct definition of any of the claimed invention’s limitations. Thus, the preamble of the claim(s) is not considered a limitation and is of no significance to claim construction. See Pitney Bowes, Inc. v. Hewlett-Packard Co., 182 F.3d 1298, 1305, 51 USPQ2d 1161, 1165 (Fed. Cir. 1999). See MPEP § 2111.02.
Regarding claims 12 and 13, a wherein clause in a method claim is not given patentable weight when it simply expresses the intended result of a process step positively recited. See MPEP 2111.04 (I).
9. Claim(s) 1, 2, 5-7 and 10-13 are alternatively rejected under 35 U.S.C. 103 as being unpatentable over US 2010/0297606 A1 (Ito, Y. Nov. 25, 2010, IDS), “Ito” in view of US 2014/0274790 A1 (Ito, Y. Sep. 18, 2014, IDS), “Ito-2”.
Ito teaches as set forth above, but does not teach using the elected IgBP peptide of SEQ ID NO: 2.
Ito-2 teaches peptides that bind to human IgG for purification of human IgG See abstract and ¶¶ 0018-0021 and claims 18-27..
Ito-2 teaches that the peptides include DCAYHRGELVWCT (SEQ ID NO: 56), which is a SEQ ID NO: 2 where X is an R. See ¶-[5] and Appendix.
Ito-2 teaches that the human IgG-binding peptide of the present invention is advantageous in that it can bind to human IgG more selectively than to IgA, IgM, and IgE, meaning that it can selectively separate IgG from, for example, human serum. See ¶ 0021.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Ito and Ito-2 and use the IgG-binding peptides of Ito-2, like SEQ ID NO: 56, in the methods of Ito because Ito teaches using for IgG-binding peptides purifying human IgG or an Fc region-containing fragment thereof and Ito-2 teaches that the peptides are advantageous in selective purification of IgG. Thus, one would have been motivated to use the use the IgG-binding peptides of Ito-2, like SEQ ID NO: 56, in the methods of Ito which also use IgG-binding peptides for IgG or Fc purification and Ito-2 teaches the advantages of the IgG binding peptides.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
10. Claims 1, 2, 5-7 and 10-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11-13 of U.S. Patent No. 8,372,950 (Ito Y., Feb. 12, 2013) in view of US 2010/0297606 A1 (Ito, Y. Nov. 25, 2010, IDS).
The ‘950 claims 11-13 are drawn to:
11. A method for purifying human IgG or an Fc region-containing fragment thereof in a sample, comprising the steps a) and b): a) contacting the peptide tag according to claim 1 (A human IgG binding peptide) with an acid-treated sample containing human IgG or an Fc region-containing fragment thereof, thereby binding human IgG or an Fc region-containing fragment thereof in the sample to the peptide tag; and b) separating the human IgG or the Fc region-containing fragment thereof, which is bound to the peptide tag in the step a), from the sample.
12. A method for removing an acid-denatured human IgG or Fc region-containing fragment thereof from a sample, comprising the steps a) and b): a) contacting the peptide tag according to claim 1 (A human IgG binding peptide) with a sample containing acid-denatured human IgG or an Fc region-containing fragment thereof; and b) removing human IgG or an Fc region-containing fragment thereof bound to the peptide tag prepared by the step a), from the sample.
13. A method for purifying a protein, comprising the steps a) to c): a) producing a fusion protein according to claim 7, and then preparing a sample containing the fusion protein; b) contacting the sample prepared by step a) with acid-treated human IgG or an Fc region-containing fragment thereof, thereby binding the fusion protein to the human IgG or Fc region-containing fragment thereof; and c) separating the fusion protein, which is bound to the human IgG or Fc region-containing fragment thereof in the step b), from the sample.
The ‘950 claims do not teach a carrier to which the IgBP is bound, cutting a bond between the Carrier-binding IgBP and the Fc molecule to recover the bound product of the Fc-binding IgBP and the Fc molecule from the carrier or injecting an Fc molecule to a column to which a Carrier-binding IgBP is bound.
Ito teaches as set forth above.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘950 claims and Ito and inject an Fc molecule to a column to which the carrier-binding IgBP is bound to bind the Fc molecule to Fc binding peptide with a cleavable linker that could be enzymatically cleaved to recover the bound product of the Fc-binding IgBP and the Fc molecule from the carrier because Ito teaches using column injection techniques and cleavable linkers for purification of Fc containing fragments. One would have been motivated with a reasonable expectation to use column injection techniques and cleavable linkers for purification of Fc containing fragments because these are routine protein purification methods in the art as exemplified by the teachings of Ito.
It is noted that for the reasons set forth above, the preambles of claims 1 and 7 and the wherein clauses of claims 6, 12 and 13 are not given patentable weight.
11. Claims 1, 2, 5-7 and 10-13 are alternatively rejected on the ground of nonstatutory double patenting as being unpatentable over claims 11-13 of U.S. Patent No. 8,372,950 (Ito Y., Feb. 12, 2013) in view of US 2010/0297606 A1 (Ito, Y. Nov. 25, 2010, IDS) in view of US 2014/0274790 A1 (Ito, Y. Sep. 18, 2014, IDS), “Ito-2”.
The ‘950 claims and Ito teach as set forth above, but does not teach using the elected IgBP peptide of SEQ ID NO: 2.
Ito-2 teaches as set forth above.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of the ‘950 claim, Ito and Ito-2 and use the IgG-binding peptides of Ito-2, like SEQ ID NO: 56, in the methods of ‘950 claims and Ito because Ito teaches using for IgG-binding peptides purifying human IgG or an Fc region-containing fragment thereof and Ito-2 teaches that the peptides are advantageous in selective purification of IgG. Thus, one would have been motivated to use the use the IgG-binding peptides of Ito-2, like SEQ ID NO: 56, in the methods of ‘950 claims and Ito which also use IgG-binding peptides for IgG or Fc purification and Ito-2 teaches the advantages of the IgG binding peptides.
Conclusion
12. No claims allowed.
13. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time.
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, Janet L Epps-Smith can be reached at 571-272-0757. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/PETER J REDDIG/ Primary Examiner, Art Unit 1646
APPENDIX
SEQ ID NO: 2 alignment with SEQ ID NO: 56 of Ito-2.
US-14-240-083-56
(NOTE: this sequence has 7 duplicates in the database searched.
See complete list at the end of this report)
Sequence 56, US/14240083
Publication No. US20140274790A1
GENERAL INFORMATION
APPLICANT: OTSUKA CHEMICAL CO., LTD.
APPLICANT: KAGOSHIMA UNIVERSITY
TITLE OF INVENTION: a method of detecting and purifying IgG by using human IgG
TITLE OF INVENTION: specific peptide ligand
FILE REFERENCE: PH-5304-PCT
CURRENT APPLICATION NUMBER: US/14/240,083
CURRENT FILING DATE: 2014-02-21
PRIOR APPLICATION NUMBER: JP 2011-182539
PRIOR FILING DATE: 2011-08-24
NUMBER OF SEQ ID NOS: 107
SEQ ID NO 56
LENGTH: 17
TYPE: PRT
ORGANISM: Artificial
FEATURE:
OTHER INFORMATION: IgG-binding peptide
Query Match 99.0%; Score 104; Length 17;
Best Local Similarity 94.1%;
Matches 16; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 GPDCAYHXGELVWCTFH 17
||||||| |||||||||
Db 1 GPDCAYHRGELVWCTFH 17