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 .
Objections/Rejections Withdrawn
Rejections and/or objections not reiterated from previous Office Actions are hereby withdrawn. The following rejections and/or objections are either reiterated or newly applied, and constitute the complete set presently being applied to the instant application.
Response to Arguments
35 U.S.C. 102(a)(1) and (a)(2)
Applicant’s arguments with respect to claim(s) 1-3, rejected by Berenson, and 1-6, rejected by Weiss, have been considered but are moot because the new ground of rejection does not rely on any reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument.
35 U.S.C. 103
Applicant's arguments filed 12/1/2025 have been fully considered but they are not persuasive.
Applicant’s position is that the addition of Ala residues to the C-domain connecting polypeptide does not predict that the resulting insulin analogue would have one or more desirable properties or even be active at all. This is not found persuasive because absolute predictability is not required to support a conclusion of obviousness, only some degree of predictability; see MPEP 2143.02(II) (“Obviousness does not require absolute predictability, but at least some degree of predictability is required. Evidence showing there was no reasonable expectation of success may support a conclusion of nonobviousness. In re Rinehart, 531 F.2d 1048, 189 USPQ 143 (CCPA 1976).”).
At the time of filing, Weiss set forth that the C-domain connecting the B- and A-chains of insulin could comprise a length of 4-11 residues, wherein N-terminal residues C1 and C2 are acidic and C-terminal residues contain two basic residues such as Arg-Arg. The remaining residues between the N- and C-terminal elements, when the domain is 5-11 amino acids, contains a flexible joint; some amino acids contemplated by Weiss that could comprise this flexible join include Gly-Pro, Ser-Pro, Ala, Pro, Gly-Ser, Ser-Ser, Gly-Gly, or Ala-Ala ([0016]). The exactly linker “EEPRRR” is well-known within the art, and at only 6 residues in length, could accommodate up to 5 additional residues selected from those taught by Weiss.
Applicant cites Figure 4 and [0034] of the instant specification to support their position, but the data shown are more like alanine-scanning experiments rather than modification of the C-domain through lengthening the hinge region. The further examples given by the Applicant detail the importance of residues “EE”, “RR”, and “P” within the C-domain “EEGPRR”, all of which are present and maintain their relative positioning in the modified C-domains with elongated hinge regions, as taught by Weiss in US2018/0265560 A1. Weiss does not contemplate removing these residues and instead simply contemplates the addition of Ala residues in the hinge region, which is in the middle of the sequence, thereby leaving the aforementioned critical residues intact.
Therefore, although not absolutely predictable, Weiss established a reasonable expectation of success, and the rejections had been maintained/modified herein.
Double patenting
The double patenting rejections have been modified/maintained herein to reflect the amended claim set.
Election/Restrictions
Applicant’s election without traverse of Group I: Claims 1-9, drawn to a single-chain insulin analogue in addition to the species of SEQ ID NO: 5, wherein Xaa at position 28 is Pro, and Xaa at positions 29, 44, and 50 are all Glu in the reply filed on 5/5/25 is acknowledged.
Upon further search and examination, the elected species was broadened to include SEQ ID NO: 5, wherein Xaa at position 28 and 29 are any amino acid, and one or both are amino acids other than Pro, Xaa at position 44 is Thr, His, Ser, Glu, or Ala, and Xaa at position 50 is any amino acid; and SEQ ID NO: 6-10, along with previously elected SEQ ID NO: 5, wherein Xaa at position 28 is Pro and Xaa at positions 29, 44, and 50 are all Glu.
Claim Status
Claims 1, 4, 7-10, 13, 16-18, and 23-25 are pending. Claims 10, 13, and 16-18 are currently withdrawn as non-elected inventions. Claims 23-25 are new. Claims 1 and 4 are currently amended.
Priority
The application is the 371 of PCT/US20/33493, filed 5/18/20, which claims priority to the provisional application 62/849,363, filed 5/17/19. The priority date of 5/17/19 is acknowledged.
Nucleotide and/or Amino Acid Sequence Disclosures
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:
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 image below where “Glu-Glu-Gly-Pro-Arg-Arg” (EEGPRR) still does not have a SEQ ID NO on Pg 11
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Specification
The disclosure is objected to because of the following informalities: A peptide sequence is disclosed in the specification with 4 or more specifically defined and enumerated residues, as described above. This peptide sequence requires a SEQ ID NO.
Appropriate correction is required.
Claim Rejections - 35 USC § 102
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 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.
Claim(s) 1 and 23 are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Weiss and Pokorski (WO 2017112952 A1, published 6/29/2017).
Weiss and Pokorski teach insulin analogues (Abstract). One such analogue is SEQ ID NO: 11, which consists of the sequence Phe-Val-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu- Val-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Glu-Thr-Glu-Glu-Gly-Pro-Arg- Arg-Gly-Ile-Val-Glu-Gln-Cys-Cys-Glu-Ser-Ile-Cys-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys-Asn ([0057]; Sequence Listing). SEQ ID NO: 11 anticipates the single-chain insulin analogue of claim 1, wherein the A-chain polypeptide comprises residues 37-57 of SEQ ID NO: 5, wherein residue 44 is Glu and residue 50 is Tyr (can be any amino acid); the C-domain comprises residues 31-36 of SEQ ID NO: 5; and the B-chain polypeptide comprises residues 1-30 of SEQ ID NO: 5, wherein residue 28 is Pro and residue 29 is Glu.
Likewise, Weiss and Pokorski also anticipate claim 23, wherein the C-domain consists of residues 31-36 of SEQ ID NO: 5.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1 and 23-25 are rejected under 35 U.S.C. 103 as being unpatentable over Weiss and Pokorski (WO 2017112952 A1, published 6/29/2017).
The teachings of Weiss and Pokorski have been set forth above. Weiss and Pokorski do not teach the single-chain insulin analogue as recited in claim 1 wherein residue 50 is Glu.
However, in addition to the teachings set forth above, Weiss and Pokorski also teach substitutions at position A14 (equivalent to the instant residue 50 of SEQ ID NO: 5) for non-beta-branched acidic or polar side chain amino acids (Abstract; [0003, 0008]). Acidic amino acids include Asp and Glu ([0028]). Weiss and Pokorski further teach that the purpose of mutating A14 to an acidic or polar amino acid can help protect single-chain insulin analogues from physical and chemical degradation due by mitigating the reverse-hydrophobic effect associated with solvent exposure of Tyr A14 in wild-type human insulin ([0027]). Moreover, Weiss and Pokorski teach an embodiment of this insulin analogue wherein Glu is substituted for Tyr at A14 ([0031]).
Thus, regarding claims 24 and 25, Weiss and Pokorski teach a single-chain insulin analogue comprising the instant SEQ ID NO: 5, as described above, wherein the only difference between the analogue taught by Weiss and Pokorski and SEQ ID NO: 5 of the instant claim 1 is residue 50 is not Glu. However, Weiss and Pokorski also teach that position 50 can be Glu. Therefore, it would be prima facie obvious to substitute the residue at position 50 for Glu. One skilled in the art would be motivated to do so in order to reduce the potential of physical and chemical degradation associated with having Tyr at residue 50. One would have a reasonable expectation of success as Weiss and Pokorski indicated that such a substitution could be made in conjunction with or without other substitutions in the A- and B- chains to further improve the physical and chemical stability of insulin analogues.
Claim(s) 4 and 7-9 are rejected under 35 U.S.C. 103 as being unpatentable over Weiss (US2018/0265560 A1, published 9/20/2018).
Weiss teaches single-chain insulin polypeptides comprising a C-domain of 6 to 11 amino acid residues, comprising at least two acidic residues at the N-terminal side of the C-domain and at least two basic residues at the C-terminal side of the C-domain peptide, a basic amino acid residue at the position corresponding to A8 of human insulin, and an acidic amino acid residue at the position corresponding to A14 of human insulin (Abstract). The single-chain insulin analogues exhibit enhanced pharmaceutical properties, such as increased thermodynamic stability, augmented resistance to thermal fibrillation above room temperature, decreased mitogenicity, and/or altered pharmacokinetic and pharmacodynamic properties ([0003]).
Weiss teaches a single-chain insulin analogue SEQ ID NO: 8. The difference between SEQ ID NO: 8 and the instant SEQ ID NO: 8-10 as recited in claims 4 and 7-9 is that SEQ ID NO: 8 of Weiss comprises a C-domain “EEGPRR” and does not include 1-3 Ala residues interspersed between the Gly and Pro.
However, Weiss further teaches that the connecting domain is of length 4-11 amino acids and consists of two elements: 1) The N-terminal element consists of the first two residues, C1, and C2, that correspond to residues B31 and B32 of an extended insulin B-chain, wherein C1 and C2 contain at least one acidic side chain and a net formal electrostatic charge at pH 7.4 of -1 or -2; and 2) the C-terminal element, which contains two basic residues such as Arg-Arg, Lys-Lys, Arg-Lys, or Lys-Arg. Four-residue connecting domains contemplated by Weiss include, but are not limited to, Glu-Glu-Arg-Arg, Glu-Ala-Arg-Arg, Ala-Glu-Arg-Arg, Asp-Glu-Arg-Arg, Glu-Glu-Lys-Arg, Glu-Glu-Arg-Lys, and Glu-Glu-Lys-Lys. In the case of connecting domains of length greater than 4 (i.e., in the range 5-11), the connection domain contains a flexible joint. In the example of a six-residue connecting domain, such sequences may contain at positions C3 and C4 Gly-Pro, Ser-Pro, Ala, Pro, Gly-Ser, Ser-Ser, Gly-Gly, or Ala-Ala as well as other possibilities (Pg 3, [0016]).
Moreover, Weiss teaches a C-domain consisting of Y1Y2B1-5RR, wherein Y1 and Y2 can each be Glu or Asp and B1-5 are optional and may be selected from Ala, Asn, Gln, Gly, Pro, Ser, or Thr (see Pg 9, SEQ ID NO: 61 and [0039] of Weiss). A C-domain linker wherein each of Y1 and Y2 are Glu, B1 is Gly, the following 1-3 residues are Ala, and the final residue is Pro reads on the C-domains of the instant SEQ ID NO: 8-10.
Thus, regarding claims 4 and 7-9, Weiss teaches SEQ ID NO: 8 which is similar to the instant SEQ ID NO: 8-10 with the only difference being the C-domain region connecting the B- and A-chains together. Weiss further teaches modifications to length the C-domain, including the addition of Ala residues to lengthen the hinge region between the N-terminal two acidic residues and the C-terminal two basic residues. Based on these teachings, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to adjust the flexible joint region in the C-domain of the SEQ ID NO: 8 of Weiss by adding additional Ala residues between the critical N-terminal and C-terminal elements of the C domain as described above, thereby arriving at the instant SEQ ID NO: 8-10. One would be motivated to do so with a reasonable expectation of success in order to further augment the flexibility of the hinge region of the C-domain; Ala residues are well-known in the art as having inherent flexibility due to the relatively small size of their side chain, making them an ideal residue to add to the flexible joint region. Moreover, one of ordinary skill in the art would have been motivated to try adding 1-3 Ala residues as Weiss taught that up to 5 residues could be added between the N-terminal acidic Glu-Glu and the C-terminal basic Arg-Arg sequences. One would have a reasonable expectation of success as Weiss established that such linkers could be to improve single-chain insulin analogues as described above.
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 4 and 7-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4 and 13-20 of U.S. Patent No. US 10,392,429 B2 (‘429). Although the claims at issue are not identical, they are not patentably distinct from each other because they contain overlapping subject matter.
Claim 1 of US ‘429 recites a single-chain insulin comprising: a C-domain of from 6 to 11 amino acid residues comprising at least two acidic residues at the N-terminal side of the C-domain and at least two basic residues at the C-terminal side of the C-domain peptide, wherein the amino acids at the N-terminal side of the C-domain are the amino acids Glu-Glu; a basic amino acid residue at the position corresponding to A8 of human insulin, and an acidic amino acid residue at the position corresponding to A14 of human insulin. The instant SEQ ID NO: 8-10 anticipate claim 1 of US ‘429.
Dependent claims include wherein the C-domain has the amino acids Arg-Arg, Lys-Lys, Arg-Lys, or Lys-Arg at the C-terminal side of the C-domain (claim 2); the single-chain insulin of claim 2, wherein the C-domain contains a 2 to 4 amino acid joint region between the acidic residues and the basic residues (claim 3); the single-chain insulin of claim 3, wherein the joint region comprises one or more of glycine, serine, and proline residues (claim 4).
Claim 13 of US ‘429 recites a pharmaceutical composition comprising a single-chain insulin formulated at a pH within the range 7.0 to 8.0, wherein the single chain insulin comprises: a C-domain of from 6 to 11 amino acid residues comprising at least two acidic residues at the N-terminal side of the C-domain and at least two basic residues at the C-terminal side of the C-domain peptide, wherein the amino acids at the N-terminal side of the C-domain are the amino acids Glu-Glu; a basic amino acid residue at the position corresponding to A8 of human insulin, and an acidic amino acid residue at the position corresponding to A14 of human insulin.
Dependent claims include the pharmaceutical composition further comprising a pH buffer (claim 14); the pharmaceutical composition of claim 14, wherein the single-chain insulin is formulated at a strength of between U-500 and U-1000 (claim 15); the pharmaceutical composition of claim 15, further comprising 2 to 4 zinc ions per insulin hexamer (claim 16); the pharmaceutical composition of claim 15, further comprising less than 2 zinc ions per insulin hexamer (claim 17); the pharmaceutical composition of claim 13, wherein the single-chain insulin is formulated at a concentration of 0.6 mM to 5.0 mM (claim 18); the pharmaceutical composition of claim 13, wherein the single-chain insulin is formulated at a strength of U-100, U-200, U-300, U-400, or U-500 (claim 19).
Claim 20 of US ‘429 recites a method for lowering the blood sugar level of a patient in need thereof, the method comprising, subcutaneously administering a pharmaceutical composition to the patient, wherein the pharmaceutical composition comprises a single-chain insulin formulated at a pH within the range 7.0 to 8.0, and wherein the single chain insulin comprises: a C-domain of from 6 to 11 amino acid residues comprising at least two acidic residues at the N-terminal side of the C-domain and at least two basic residues at the C-terminal side of the C-domain peptide, wherein the amino acids at the N-terminal side of the C-domain are the amino acids Glu-Glu; a basic amino acid residues at the position corresponding to A8 of human insulin, and an acidic amino acid residue at the position corresponding to A14 of human insulin. The instant specification teaches that peptides of the invention can be used to lower the blood sugar level of a patient in need thereof ([0045]).
Prior Art Cited but not Referenced
Both Glidden et al. (Solution structure of an ultra-stable single-chain insulin analog connects protein dynamics to a novel mechanism of receptor binding. J Biol Chem. 2018 Jan 5;293(1):69-88.) and Glidden et al. (An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein. J Biol Chem. 2018 Jan 5;293(1):47-68.) teach the peptide SCI-b, which comprises the A- and B-chains of the instant SEQ ID NO: 8-10; either Glidden reference in view of Weiss (US2018/0265560 A1, published 9/20/2018) from above would render the instant SEQ ID NO: 8-10 in claims 4 and 7-9 obvious for the same rationale described above.
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Sara E Konopelski Snavely whose telephone number is (571)272-1841. The examiner can normally be reached Monday - Friday 9-6pm EST.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa L Fisher can be reached at 571-270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/SARA E KONOPELSKI SNAVELY/Examiner, Art Unit 1658 /FRED H REYNOLDS/Primary Examiner, Art Unit 1658