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 .
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.
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1-3, 5-6, 8-9, 11-12, 17-19, 24-25, 34-35, 61-65, 72, 131, and 227-230) in the reply filed on 02/19/2026 is acknowledged. Applicant further selected with traverse for the elected species. Applicant argues that there is no search burden to the generic claims. The argument is not found persuasive because as stated in the restriction (pg. 5) each species has different chemical structures. Also, as evidenced below, the elected species have different chemical structures that requires different field of prior art search.
Claims 47, 91, 161, 192, 193, 207 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected groups, there being no allowable generic or linking claim. Election was made without traverse.
Claim Objections
Claim 61 is objected to because of the following informalities: Appropriate correction is required.
Claim 61 recites “DAP” which needs to be “the probe” or the term DAP needs to be accompanied by an unabbreviated form.
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.
Claims 3, 6, 9, 11, 18-19, 24-25, 63-65 and 227-229 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.
Claims 3, 6, 11, 18-19, 24-25 are dependent from claim 1 and these claims recite a wherein clause that has LI elements, which have not been recited in claim 1. Therefore, the claim is unclear and lacks antecedent basis. Wherein clauses are used to define the existing structure of a preceding claim but these claims recite elements that have not been identified in claim 1.
Claim 9 recites “any peptide sequence of Table 1 herein” is unclear to the metes and bounds of the claim. There is no limit to the length of a claim. If the subject matter can be listed in the specification, that list can be copied and pasted into a claim. "Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table 'is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim. Incorporation by reference is a necessity doctrine, not for applicant’s convenience.' Ex parte Fressola, 27 USPQ2d 1608, 1609 (Bd. Pat. App. & Inter. 1993)" (MPEP 2173.05(s)).
Claim 19 recites “CE is an antibody or an antigen binding fragment thereof” lacks antecedent basis because CE has been identified in claim 18. The claim is also unclear if antigen-binding fragment thereof is referring to the antibody?
Claim 63 recites a wherein clause that is also bound to a SBP, which has not been recited in claim 61. Claim 61 only has the surface particle fused or bound to a NACE or a capture element. Wherein clauses are used to define the existing structure of a preceding claim but the claim recites elements that have not been identified in claim 61. Therefore, it is unclear to what is present in the formulas.
Claim 64 recites “NACE comprises one or more selected from the group consisting of…” is unclear to the metes and bounds of the claimed NACE element. The claim recites both an open-ended recitation and a closed recitation (Markush language).
Claim 65 recites the phrase "such as" (“e.g.”) renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claims 227-229 recites wherein clauses that have “the probe comprises” are unclear to the metes and bounds of these peptide sequences with respect to SBM and CE of claim 1. Are these peptide sequences additionally elements (further comprises) or these peptide sequences are directed to the elements of SBM and CE. If they are, which elements have these peptide sequences. Therefore, the claims are unclear to what is the relationship between claim 1 and these peptide sequences.
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 19 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 19 recites the limitations of CE is an antibody or antigen binding fragment therefore, LI is an amino acid sequence comprising protein G from Streptococcus is broadening the scope of claim 18 which recites that LI only includes an amino acid sequence comprising streptavidin from Streptomyces and the antibody or antigen-binding fragment thereof is conjugated with biotin.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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.
(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.
Claims 1-3, 5-6, 8-9, 11-12, 17-19, 24-25, 34-35, 61-65, 72, 131, and 227-230 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Greene et al. (WO2022/051861A1, filing date 09/10/2021, see IDS dated 08/04/2023, cite no. 003).
With respect to claims 1-3, 5, Greene teaches in Figs. 19-20 a dual-affinity probe for detecting an analyte in a sample, the probe comprising a surface binding moiety (SBM) and a capture element (CE), wherein the probe binds specifically to a surface material selected from the group consisting of gold, silica, silver, cellulose, plastic, polystyrene and graphene (also see para. [0030]). Greene teaches the biosensor material is gold, silica, silver, cellulose, plastic, polystyrene, and graphene (see para. [0011]).
With respect to claims 6, 12, and 72, Greene teaches LI is a single bond, or is selected from one or more of the group consisting of a peptide or amino acid linker, an amino acid sequence comprising protein G from Streptococcus, and an amino acid sequence comprising streptavidin from Streptomyces (see para. [0025]).
With respect to claims 8-9, Greene teaches the peptide sequences of Table 1 (see para. [00204], Example 2).
With respect to claim 11, Greene teaches the polypeptide having the claimed formulas (see pg. 71, middle of page).
With respect to claims 17-19 and 24, Greene teaches CE is an antigen or an antibody wherein the antigen or antibody is conjugated with biotin, and the LI includes an amino acid sequence comprising streptavidin from Streptomyces or protein G from Streptococcus (see para. [00160]).
With respect to claims 25 and 34-35, Greene teaches the dual-affinity probe is a single fusion protein (see paras. [00151 and [00176]).
With respect to claims 61-65, Greene teaches in Figs. 19-20 a dual-affinity probe for detecting an analyte in a sample, the probe comprising a surface binding moiety (SBM) and a capture element (CE), wherein the probe binds specifically to a surface material selected from the group consisting of gold, silica, silver, cellulose, plastic, polystyrene and graphene (also see para. [0030]). Greene teaches the biosensor material is gold, silica, silver, cellulose, plastic, polystyrene, and graphene (see para. [0011]). Greene teaches formula Ic (see para. [00142]).
With respect to claim 72, Greene teaches the NACE comprises protein G and/or streptavidin. (see para. [00176]).
With respect to claim 131, Greene teaches in Figs. 19-20 a dual-affinity probe for detecting an analyte in a sample, the probe comprising a surface binding moiety (SBM) and a capture element (CE), wherein the probe binds specifically to a surface material selected from the group consisting of gold, silica, silver, cellulose, plastic, polystyrene and graphene (also see para. [0030]). Greene teaches the biosensor material is gold, silica, silver, cellulose, plastic, polystyrene, and graphene (see para. [0011]). Greene teaches formula Ic (see para. [00142]).
With respect to claim 227, Greene teaches SEQ ID NOs: 27 and 28 in Table 1 (see pg. 42).
With respect to claim 228, Greene teaches SEQ ID NOs: 20, 23, 24 and 34 in Table 1 (see pgs. 40-44). Greene teaches the biosensor material is gold (see para. [0011]).
With respect to claim 229, Greene teaches SEQ ID NO: 26in Table 1 (see pg. 42). Greene teaches the biosensor material is silica (see para. [0011]).
With respect to claim 230, Green teaches one or both of the CE and the SBM is an antibody, and wherein the CE and the SBM are fused to form a bispecific immunoglobulin A (see para. [0057]).
Claims 1-3, 5-6, 8-9, 11, 17, 24-25, 34, 61-65 and 131 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Ko et al. (Directed self-assembly of gold binding polypeptide-protein A fusion proteins for development of gold nanoparticle-based SPR immunosensors”, Biosensors and Bioelectronics, vol. 24, pgs. 2592-2597, published 2009, see IDS dated 05/21/2026).
With respect to claim 1, Ko teaches effective immobilization of antibodies on a sensing platform and sensitivity enhancement are crucial in designing SPR immunosensors and wherein the colloidal gold nanoparticles were directly assembled onto a surface of SPR Au chip (see abstract). Fig. 1 and Fig. 4 show a dual-affinity probe wherein the probe comprising a surface binding moiety (SBM) and a capture element (CE) wherein the probe binds to the gold nanoparticle.
With respect to claim 2, Ko teaches in Fig.1 the CE is directly or indirectly connected to the SBM via a LI linker wherein the LI linker is a single bond or amino acid sequence (i.e., protein).
With respect to claim 3, Fig. 1 also shows the probe has the following formulas SBM-LI-CE or CE-LI-SBM.
With respect to claim 5, Fig. 1 shows the CE is an antibody or antigen-binding fragment thereof.
With respect to claim 6, Fig. 1 shows LI is a single bond or a peptide.
With respect to claim 8, Fig. 1 shows SBM is a protein or an immunogenic fragment thereof.
With respect to claim 9, Fig. 1 shows a gold binding poplypeptide (GBP) (also see abstract).
With respect to claim 11, Fig. 1 and Fig. 4 show a gold binding polypeptide (GBP) with the claimed formulas.
With respect to claim 17, Fig. 1 and Fig. 4 show CE is an antigen, antibody or an engineered protein (GBP).
With respect to claim 24, Fig. 1 and Fig.4 show LI is a single bond, or a peptide.
With respect to claim 25, Fig. 1 and Fig. 4 show a fusion protein (also see abstract).
With respect to claim 34, Fig. 1 shows two different types of fragments, Fab and Fc. Thus, the figure shows the CE is a single chain variable fragment from an antibody and SBM and CE are fused as a bispecific antibody fragment. Additionally, Fig. 4 shows that the Fab fragments are bispecific as the anti-hIgG only binds to one of the fragments.
With respect to claim 61-63, Fig. 1 and Fig.4 show a dual-affinity probe comprising a surface particle fused or bound to a NACE or a capture element (CE).
With respect to claims 64-65, Fig. 1 and Fig. 4 show the NACE is a linker or an antibody.
With respect to claim 131, Fig. 1 shows a dual-affinity probe comprising: i) a surface binding moiety (SBM), wherein the SBM is a gold binding protein (GBP), fused or bound to a non-analyte capture element (NACE), or ii) a surface binding moiety (SBM), wherein the SBM is a gold binding protein (GBP), fused or bound to a capture element (CE).
Claims 1-3, 5-6, 8-9, 11-12, 17-19, 24-25, 34-35, 61-65, 72, and 230 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rhiel et al. (US Patent No. 10676733B2, published 06/09/2020), as evidenced by De Blas et al. (“Detection of Antigens on Nitrocellulose Paper lmmunoblots with Monoclonal Antibodies”, Analytical Biochemistry, vol. 133, pgs. 214-219, published 1983).
With respect to claims 1-3, 5, Rhiel teaches in Fig. 11 a dual-affinity probe for detecting an analyte in a sample, the probe comprising a surface binding moiety (SBM) and a capture element (CE) wherein the (CE) is directly or indirectly connected to the SBM via one or more linker (LI) probe has the following formulas SBM-LI-CE (Ia) or CE-LI-SBM (IIa). Fig. 11 also shows wherein the CE comprises an antibody. Rhiel teaches Western blot analysis also showed that SA-ZZ fusion proteins bind both IgG and biotinylated protein (Fig. 1). Meanwhile, the evidentiary teachings of De Blas indicate that nitrocellulose sheet is Western blot (see abstract). Thus, Rhiel’s western blot analysis of the assay would be on cellulose.
With respect to claim 6, Rhiel teaches a recombinant fusion protein streptavidin-ZZ (SA-ZZ) (see col. 7, lines 1-4; and Fig. 11). SEQ ID NO:3 of Rhiel (SA-ZZ) is a similar amino acid sequence to the instant claimed SEQ ID NOS: 23, 24, 26-28, 34 (see col. 8, lines 30-36).
With respect to claims 8-9, Fig. 11 shows the SBM is a binding peptide, a protein, an antibody with an affinity to the surface material. Rhiel teaches all the structure of the claimed antibody; therefore, would have the same affinity as claimed.
With respect to claim 11, Fig. 11 shows the dual-affinity probe comprises a polypeptide having at least one of the formulas SBM-LI-AL (IIIa); AL-LI-SBM (IIIb); ALB-LI-CE (IVa); or CE-LI-ALB (IVb), wherein AL is an active linker and ALB is an active linker binder.
With respect to claim 12, Fig. 11 shows a recombinant fusion protein streptavidin-ZZ (SA-ZZ) (also see col. 7, lines 1-4; and Fig. 11). SEQ ID NO:3 of Rhiel (SA-ZZ) is a similar amino acid sequence to the instant claimed SEQ ID NOS: 23, 24, 26-28, 34 (see col. 8, lines 30-36).
With respect to claim 17, Fig. 11 shows the CE is an antigen, an antibody or, an engineered protein.
With respect to claim 18, Fig. 11 shows the CE is an antigen or antibody, wherein the antigen or antibody is conjugated with biotin, through the LI includes an amino acid sequence comprising streptavidin from Streptomyces. Rhiel also teaches biotinylated antigen (see col. 3, line 1).
With respect to claim 19, Rhiel teaches Protein G (see col. 16, lines 23-25).
With respect to claims 24-25, Fig. 11 shows the dual-affinity probe is a single fusion protein wherein LI is a single bond, or a peptide or amino acid linker.
With respect to claim 34, Fig. 11 shows the CE is a single chain variable fragment from an antibody, and wherein the SBM and the CE are fused as a bispecific antibody fragment.
With respect to claim 35, Fig. 11 shows the SBM is a ingle chain variable fragment that is a Vh gold binding motif. The antibody in Fig. 11 reads on the structure as claimed which has a Vh.
With respect to claim 61, Fig. 11 shows a dual-affinity probe for detecting an analyte in a sample, the DAP comprising i) a surface binding moiety (SBM) fused or bound to a non-analyte capture element (NACE).
With respect to claims 62-64, Fig. 11 shows NACE is a linker (LI), streptavidin, protein G, biotin, an antigen protein or peptide, or an antibody.
With respect to claim 72, Fig. 11 shows NACE comprises streptavidin.
With respect to claim 230, Rhiel teaches engineered antibody that is bispecific molecules generated by dimerization of two variable heavy-variable light fragments (see col. 20, lines 23-25). Rhiel teaches immunoglobulin molecules include IgA (see col. 27, lines 35-40).
Claims 1-3, 5-6, 8-9, 11-12, 17-18, 24, 61-65, 72, 131 and 229 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Orschel et al. (“Evaluation of several methods to quantify immobilized proteins on gold and silica surfaces”, Colloids and Surfaces B: Biointerfaces, vol. 10, pgs. 273-279, published 1998), as evidenced by Rhiel et al. (US Patent No. 10676733B2, published 06/09/2020).
With respect to claims 1-3, 5, 8-9, 11, 17, 24, Orschel teaches streptavidin was bound covalently on gold and silica surfaces (see abstract). Orschel teaches an enzyme-linked immunosorbent-assay based on enzyme-labeled anti-streptavidin antibodies was developed to determine streptavidin on the gold or silica surfaces (see pg. 274, left col., bottom of left col.). Orschel also teaches streptavidin-biotin complex which was immobilized and after immobilization, the gold or silica chips were incubated (see pg. 275, left col., para. 1). Hence, Orschel’s immobilized surfaces read on a dual-affinity probe for detecting an analyte in a sample, the probe comprising a surface binding moiety (SBM) and a capture element (CE) wherein the probe binds specifically to gold or silica.
With respect to claims 6, 12, 18, 61-65, 72, 131, and 229, Orschel teaches streptavidin was bound covalently on gold and silica surfaces (see abstract). The evidentiary teachings of Rhiel indicate that SA (streptavidin) has the amino acid sequence of SEQ ID NO: 2 (see col. 8, lines 27-30). Meanwhile, SEQ ID NO: 2 of Rhiel has a 100% local similarity to instant claimed SEQ ID NO: 26 (see below). Because the claim recites “a” peptide sequence of SEQ ID NO: 26, it encompasses peptide sequences that comprise the full-length sequence of SEQ ID NO: 26 or any portion of SEQ ID NO: 26. The claim is anticipated by any dinucleotide or larger oligonucleotide.
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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.
Claims 1-3, 5-6, 8-9, 11-12, 17-19, 24-25, 34-35, 61-65, 72, 131 and 229-230 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-8, 12, 14, 15, 16, 18, 30, 33, 39, of copending Application No. 18025867 (‘867) (reference application), in view of as evidenced by Rhiel et al. (US Patent No. 10676733B2, published 06/09/2020).
Regarding claims 1 and 61-65, although the claims at issue are not identical, they are not patentably distinct from each other because the copending Application ‘867 recites a dual-affinity probe for detecting analyte in a sample, the probe comprising a surface binding moiety (SBM), wherein the SBM comprises an inorganic surface binding peptide (ISBP), and a capture element (CE), wherein the probe comprises one or more polypeptides, and wherein the ISBP and the CE are present on the same or different polypeptides. Copending claim 7 recites the SBM or ISBP binds specifically to a biosensor material selected from the group consisting of gold, silica, silver, cellulose, plastic, polystyrene and graphene. Copending claim 14 recites the ISBP comprises a gold binding motif, cellulose binding motif, silica binding motif or polystyrene binding motif.
Regarding claim 2, the copending claim 2 recites wherein the (CE) is directly or indirectly connected to the SBM or ISBP via one or more linker (LI), wherein each LI is a single bond or an amino acid sequence.
Regarding claims 3 and 11, copending claim 3 recites the immunoprobe has the following formula :SBM-LI-CE (Ia); CE-LI-SBM (Ila); SBM-LI-AL (IIIa); AL-LI-SBM (IIIb); ALB-LI-CE (IVa); or CE-LI-ALB (IVb); wherein AL is an active linker and ALB is an active linker binder.
Regarding claim 5, copending claim 5 recites the CE comprises: an antibody, an antigen-binding fragment thereof, a single chain variable fragment (scFv), or a Fab fragment; or an antigen.
Regarding claims 6, 72, 131, copending claim 6 recites LI is a single bond, or is selected from one or more of the groups consisting of: a peptide or amino acid linker, an amino acid sequence comprising protein G from Streptococcus, and an amino acid sequence comprising streptavidin from Streptomyces.
Regarding claims 8-9, copending claim 8 recites the SBM or ISBP is selected from the group consisting of a binding peptide, a protein, an antibody, a single chain variable fragment from an antibody, an antibody with an affinity to the inorganic surface, er an immunogenic fragment thereof, a single chain variable fragment (scFv),er a Fab fragment, and a peptide sequence in Table 1.
Regarding claims 12, copending claim 12 recites AL is an amino acid sequence comprising protein G from Streptococcus or an amino acid sequence comprising streptavidin from Streptomyces.
Regarding claims 17-19, copending claim 18 recites the CE is an antigen, antibody or an antigen- binding fragment thereof, wherein the antigen, antibody or antigen- binding fragment thereof is conjugated with biotin, and the LI comprises an amino acid sequence comprising streptavidin or protein G from Streptomyces.
Regarding claims 24-25 and 34, copending claim 30 recites the SBM or ISBP and the CE are fused as a bispecific antibody fragment.
Regarding claim 35, copending claim 33 recites the CE and the SBM or ISBP are fused to form a bispecific immunoglobulin A.
Regarding claims 131 and 229-230, Copending claim 7 recites the SBM or ISBP binds specifically to a biosensor material selected from the group consisting of gold, silica, silver, cellulose, plastic, polystyrene and graphene. Copending claim 14 recites the ISBP comprises a gold binding motif, cellulose binding motif, silica binding motif or polystyrene binding motif. copending claim 12 recites AL is an amino acid sequence comprising protein G from Streptococcus or an amino acid sequence comprising streptavidin from Streptomyces.
The evidentiary teachings of Rhiel indicate that SA (streptavidin) has the amino acid sequence of SEQ ID NO: 2 (see col. 8, lines 27-30). Meanwhile, SEQ ID NO: 2 of Rhiel has a 100% local similarity to instant claimed SEQ ID NO: 26 (see above rejection). Because the claim recites “a” peptide sequence of SEQ ID NO: 26, it encompasses peptide sequences that comprise the full-length sequence of SEQ ID NO: 26 or any portion of SEQ ID NO: 26. The claim is anticipated by any dinucleotide or larger oligonucleotide.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
No claim is allowed.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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