Prosecution Insights
Last updated: April 19, 2026
Application No. 17/439,590

STABILIZATION OF PRANDIAL OR BASAL INSULIN ANALOGUES BY AN INTERNAL DISELENIDE BRIDGE

Non-Final OA §103§DP
Filed
Sep 15, 2021
Examiner
HA, JULIE
Art Unit
1654
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Yissum Research Development Company of the Hebrew University of Jerusalem Ltd.
OA Round
4 (Non-Final)
76%
Grant Probability
Favorable
4-5
OA Rounds
2y 8m
To Grant
99%
With Interview

Examiner Intelligence

Grants 76% — above average
76%
Career Allow Rate
831 granted / 1099 resolved
+15.6% vs TC avg
Strong +44% interview lift
Without
With
+44.3%
Interview Lift
resolved cases with interview
Typical timeline
2y 8m
Avg Prosecution
44 currently pending
Career history
1143
Total Applications
across all art units

Statute-Specific Performance

§101
4.4%
-35.6% vs TC avg
§103
27.4%
-12.6% vs TC avg
§102
15.1%
-24.9% vs TC avg
§112
18.5%
-21.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 1099 resolved cases

Office Action

§103 §DP
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 . 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 October 9, 2025 has been entered. Claims 1-16 and 18 are pending in this application and are examined on the merits in this office action. Non-Compliant Amendment Amendment to claim 1 is non-compliant. Applicant amended the claim to add the following recitation: PNG media_image1.png 130 564 media_image1.png Greyscale PNG media_image2.png 50 572 media_image2.png Greyscale . The claims filed on June 12, 2025 had the following recitation at the end of claim 1: PNG media_image3.png 50 566 media_image3.png Greyscale . The term “and” in between “A6 and A11” and “wherein the internal…” needs to be underlined. Applicant is required to correct this error in response to this office action. Withdrawn Objections Objection to the specification is hereby withdrawn in view of Applicant’s amendment to the specification. Objection to the specification amendment filed on June 12, 2025, is hereby withdrawn in view of Applicant’s amendment to the specification. Please note, the specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification. MPEP § 608.01. Maintained and Revised Rejections 35 U.S.C. 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. 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) 1-16 and 18 remain/are rejected under 35 U.S.C. 103 as being unpatentable over Safavi-Hemami et al (WO 2016/172269, filed with IDS) in view of Miao et al (US Patent No. 8946148, cited in the previous office action), Kohn et al (US 2006/0217290, cited in the previous office action), Chiquette et al (US 2015/0174209, cited in the previous office action), and Veronese et al (Drug Discovery Today, 2005, 10(21): 1451-1458, cited in the previous office action). This Rejection is maintained and revised in view of Applicant’s amendment to the claims. Safavi-Hemami et al teach insulin analogs having instant SEQ ID NO: 17 (for insulin A chain) (see for example, SEQ ID NO: 57, claim 20). Safavi-Hemami et al teach the following for insulin A chain analog: Gly-XA2-Val-Glu-XA5-CysA6-CysA7-XA8-XA9-XA10-CysA11-Ser-XA13-XA14-XA15-XA16-XA17-XA18-Tyr-CysA20-XA21 (SEQ ID NO: 57), wherein XA2 = Ile or Val; XA5 = Gln or His; CysA6, CysA7, and CysA11 are independently Cys or selenocysteine; XA8 = Thr or His; XA9 = Ser or Arg; XA10 = Ile or Pro; XA13 = Leu or Asn; XA14 = Tyr or Ala; XA15 = Gln or Glu; XA16 = Leu or Phe; XA17 = Glu or Lys; XA18 = Asn or Lys; CysA20 = Cys, selenocysteine, amidated Cys, or amidated selenocysteine; and XA21 = Asn or absent (see p. 17, lines 10-20 and claim 20). The SEQ ID NO: 57 of Safavi-Hemami et al meets instant SEQ ID NO: 17, wherein XA2 = Ile, XA5 = Gln, CysA6 = selenocysteine, CysA7 = Cys, XA8 = Thr or His; XA9 = Ser, XA10 = Ile, CysA11 = selenocysteine, XA13 = Leu, XA14 = Tyr, XA15 = Gln, XA16 = Leu, XA17 = Glu, XA18 = Asn, CysA20 = Cys, and XA21 = Asn. Additionally, SEQ ID NO: 57 of Safavi-Hemami et al also meets the limitation of instant SEQ ID NOs: 15 and 30. Therefore, this meets the limitation of instant claims 1 and 5, in part. Safavi-Hemami et al teach a pharmaceutical composition comprising the insulin analog and pharmaceutically acceptable carrier (see claims 25-29), meeting the limitation of instant claims 13-14. Safavi-Hemami et al teach a method for treating an insulin-related condition, comprising administering the formulation to a subject in need there of (see claim 30), meeting the limitation of instant claim 16. Safavi-Hemami et al teach insulin B chain having the sequence/formula: PNG media_image4.png 370 652 media_image4.png Greyscale (see claim 20). This is the C-terminal truncated sequence of instant SEQ ID NO: 11 and SEQ ID NO: 18. Safavi-Hemami et al teach the following regards to diselenide bond. “Diselenide bond-containing peptide analogs have similar biological activities to their native peptides and, in some cases, even improved potency or selectivity. Due to the lower redox potential, diselenide bond formation is favored over the disulfide bond formation under acidic conditions…(see p. 20, lines 18-21), meeting the limitation of the last wherein clause of instant claim 1. Safavi-Hemami et al explicitly teach the diselenide bond formation between the residues on the insulin analogs. The MPEP § 2112 states: “Once a reference teaching product appearing to be substantially identical is made the basis of a rejection, and the Examiner presents evidence or reasoning tending to show inherency, the burden shifts to the Applicant to show an unobvious difference ‘[t]he PTO can require an Applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his [or her] claimed product. Whether the rejection is based on inherency’ under 35 U.S.C. 102, on prima facie obviousness’ under 35 U.S.C. 103, jointly or alternatively, the burden of proof is the same...[footnote omitted].” The burden of proof is similar to that required with respect to product-by-process claims. In re Fitzgerald, 619 F.2d 67, 70, 205 USPQ 594, 596 (CCPA 1980) (quoting In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433-34 (CCPA 1977)).” Therefore, the insulin analog of Safavi-Hemami et al would inherently have the same function and activity of the insulin analog of instant claims (i.e., the internal diselenide bridge would enhance efficiency of core packing within the interior of the insulin analogue). Safavi-Hemami et al do not teach the B chain comprising instant SEQ ID NO: 11 or SEQ ID NO: 18, PEGylation and acylation modifications. However, Miao et al teach insulin B chain analogs of instant SEQ ID NO: 5 (see SEQ ID NO: 6) and instant SEQ ID NO: 6 (see SEQ ID NO: 4). Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy (see for example, column 3, lines 4-23), and teach method of treating diabetes (see column 3, lines 24-48). Further, Kohn et al teach the insulin B chain having instant SEQ ID NOs: 4 and 54 (see SEQ ID NO: 4), instant SEQ ID NO: 9 (see SEQ ID NO: 4) and instant SEQ ID NO: 8 (see SEQ ID NO: 2), and teach that the insulin analogs have protracted time of action, and also teach a method of treating diabetes mellitus (see abstract). Additionally, Chiquette et al teach the insulin B chain having instant SEQ ID NO: 7 (see SEQ ID NO: 6). Furthermore, Veronese et al teach the modification to protein, peptide or non-peptide molecule by the linking of one or more polyethylene glycol (PEG) chain. PEG is non-toxic, non-immunogenic, non-antigenic, highly soluble in water and FDA approved. The PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity (see abstract). Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of Safavi-Hemami et, Miao et al, Kohn et al and Chiquette et al, because all references teach insulin analogs and treatment of diabetes. Furthermore, Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy. Additionally, it would have been obvious to one of ordinary skill in the art to combine the teachings with Veronese et al, since Veronese et al teach PEG addition to any peptide and proteins. One of ordinary skill in the art would be motivated to combine with a reasonable expectation of success, since it is well known in the art that insulin analogs comprising for example, modified insulin B chain provide protracted time of action (see Kohn et al, for example). One of ordinary skill in the art would be motivated to further combine with Veronese et al with a reasonable expectation of success, since Veronese et al teach that PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity. Therefore, the combined arts are prima facie obvious over instant claims 1-16 and 18. Response to Applicant’s Arguments Applicant argues that “ PNG media_image5.png 318 584 media_image5.png Greyscale ”. Applicant’s arguments have been fully considered but are not found persuasive. First, Safavi-Hemami et al teach insulin analogs having instant SEQ ID NO: 17 (for insulin A chain) (see for example, SEQ ID NO: 57, claim 20). Safavi-Hemami et al teach the following for insulin A chain analog: Gly-XA2-Val-Glu-XA5-CysA6-CysA7-XA8-XA9-XA10-CysA11-Ser-XA13-XA14-XA15-XA16-XA17-XA18-Tyr-CysA20-XA21 (SEQ ID NO: 57), wherein XA2 = Ile or Val; XA5 = Gln or His; CysA6, CysA7, and CysA11 are independently Cys or selenocysteine; XA8 = Thr or His; XA9 = Ser or Arg; XA10 = Ile or Pro; XA13 = Leu or Asn; XA14 = Tyr or Ala; XA15 = Gln or Glu; XA16 = Leu or Phe; XA17 = Glu or Lys; XA18 = Asn or Lys; CysA20 = Cys, selenocysteine, amidated Cys, or amidated selenocysteine; and XA21 = Asn or absent (see p. 17, lines 10-20 and claim 20). The SEQ ID NO: 57 of Safavi-Hemami et al meets instant SEQ ID NO: 17, wherein XA2 = Ile, XA5 = Gln, CysA6 = selenocysteine, CysA7 = Cys, XA8 = Thr or His; XA9 = Ser, XA10 = Ile, CysA11 = selenocysteine, XA13 = Leu, XA14 = Tyr, XA15 = Gln, XA16 = Leu, XA17 = Glu, XA18 = Asn, CysA20 = Cys, and XA21 = Asn. Additionally, SEQ ID NO: 57 of Safavi-Hemami et al also meets the limitation of instant SEQ ID NOs: 15 and 30. Thus, Safavi-Hemami et al explicitly teach the A-chain recited in the claims (for examples, claims 1-2, 6-8 and 18). Safavi-Hemami et al teach insulin B chain having the sequence/formula: PNG media_image4.png 370 652 media_image4.png Greyscale (see claim 20). This is the C-terminal truncated sequence of instant SEQ ID NO: 11 and SEQ ID NO: 18. Miao et al teach insulin B chain analogs of instant SEQ ID NO: 5 (see SEQ ID NO: 6) and instant SEQ ID NO: 6 (see SEQ ID NO: 4). Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy, and teach method of treating diabetes. Further, Kohn et al teach the insulin B chain having instant SEQ ID NOs: 4 and 54 (see SEQ ID NO: 4), instant SEQ ID NO: 9 (see SEQ ID NO: 4) and instant SEQ ID NO: 8 (see SEQ ID NO: 2), and teach that the insulin analogs have protracted time of action, and also teach a method of treating diabetes mellitus. Additionally, Chiquette et al teach the insulin B chain having instant SEQ ID NO: 7 (see SEQ ID NO: 6). Furthermore, Veronese et al teach the modification to protein, peptide or non-peptide molecule by the linking of one or more polyethylene glycol (PEG) chain. PEG is non-toxic, non-immunogenic, non-antigenic, highly soluble in water and FDA approved. The PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity. Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of Safavi-Hemami et, Miao et al, Kohn et al and Chiquette et al, because all references teach insulin analogs and treatment of diabetes. Furthermore, Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy. Additionally, it would have been obvious to one of ordinary skill in the art to combine the teachings with Veronese et al, since Veronese et al teach PEG addition to any peptide and proteins. One of ordinary skill in the art would be motivated to combine with a reasonable expectation of success, since it is well known in the art that insulin analogs comprising for example, modified insulin B chain provide protracted time of action (see Kohn et al, for example). One of ordinary skill in the art would be motivated to further combine with Veronese et al with a reasonable expectation of success, since Veronese et al teach that PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity. Therefore, the combined arts are prima facie obvious over instant claims 1-16 and 18. In response to applicant's argument that Safavi-Hemami does not teach “an internal diselenide bridge between positions A6 and A11 is larger than a disulfide bridge formed between the positions A6 and A11”, Safavi-Hemami et al do explicitly teach an insulin analog that have selenocysteine at both positions A6 and A11. Safavi-Hemami et al further teach that diselenide bond-containing peptide analogs have similar biological activities to their native peptides and, in some cases, even improved potency or selectivity. Due to the lower redox potential, diselenide bond formation is favored over the disulfide bond formation under acidic conditions. Therefore, the diselenide bridge would be inherently formed between A6 and A11 residues, and the bridge would be inherently larger than a disulfide bonds formed between cysteines at positions A6 and A11. Additionally, in regards to Applicant’s arguments that “the internal diselenide bridge between the positions A6 and A11 enhances efficiency of core packing within the interior of the interior of the insulin analogue,” since the insulin analog of Safavi-Hemami et al teach insulin analogs having the selenocysteine residues at positions A6 and A11 and diselenide bridge formation, the insulin analogs of Safavi-Hemami et al would inherently have ALL of the same functions and activities of instant insulin analogs. The motivation to combine the teachings of Safavi-Hemami et al and Miao et al and Kohn is taught by Miao et al and Kohn et al. Both Miao et al and Kohn et al teach that the insulin B-chain modification allow for long-acting basal insulin therapy and the insulin analogs have protracted time of action. Additionally Veronese et al teach that modifying any peptide molecule by linking one or more with PEG chain allows for prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity. Therefore, the combined arts is prima facie obvious over instant claims 1-16 and 18. The rejection is deemed to be proper and is maintained herein. DOUBLE PATENTING The no statutory 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 no statutory 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 Orne, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Torrington, 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 no statutory 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 no statutory 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 terminal Disclaimer may be filled out completely online using web-screens. An terminal 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 1-16 and 18 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 and 15-16 of copending Application No. 18/288925 (reference application) in view of Miao et al (US Patent No. 8946148, cited in the previous office action), Kohn et al (US 2006/0217290, cited in the previous office action), Chiquette et al (US 2015/0174209, cited in the previous office action), and Veronese et al (Drug Discovery Today, 2005, 10(21): 1451-1458, cited in the previous office action). Although the claims at issue are not identical, they are not patentably distinct from each other because if one of ordinary skill in the art practiced the claimed invention of instant claims, one would necessarily achieve the claimed invention of copending claims and vice versa. This is a provisional nonstatutory double patenting rejection. Instant claims are drawn to: PNG media_image6.png 726 602 media_image6.png Greyscale PNG media_image7.png 64 580 media_image7.png Greyscale . Copending claims are drawn to: PNG media_image8.png 684 404 media_image8.png Greyscale . The copending claims do not teach PEGylation and acyl modification. However, Miao et al teach insulin B chain analogs of instant SEQ ID NO: 5 (see SEQ ID NO: 6) and instant SEQ ID NO: 6 (see SEQ ID NO: 4). Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy (see for example, column 3, lines 4-23), and teach method of treating diabetes (see column 3, lines 24-48). Further, Kohn et al teach the insulin B chain having instant SEQ ID NOs: 4 and 54 (see SEQ ID NO: 4), instant SEQ ID NO: 9 (see SEQ ID NO: 4) and instant SEQ ID NO: 8 (see SEQ ID NO: 2), and teach that the insulin analogs have protracted time of action, and also teach a method of treating diabetes mellitus (see abstract). Additionally, Chiquette et al teach the insulin B chain having instant SEQ ID NO: 7 (see SEQ ID NO: 6). Furthermore, Veronese et al teach the modification to protein, peptide or non-peptide molecule by the linking of one or more polyethylene glycol (PEG) chain. PEG is non-toxic, non-immunogenic, non-antigenic, highly soluble in water and FDA approved. The PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity (see abstract). Therefore, it would have been obvious to one of ordinary skill in the art to combine the teachings of copending application 18/288925, Miao et al, Kohn et al and Chiquette et al, because all references teach insulin analogs and treatment of diabetes. Furthermore, Miao et al further teach acylation of the insulin analog and PEG modifications for long-acting basal insulin therapy. Additionally, it would have been obvious to one of ordinary skill in the art to combine the teachings with Veronese et al, since Veronese et al teach PEG addition to any peptide and proteins. One of ordinary skill in the art would be motivated to combine with a reasonable expectation of success, since it is well known in the art that insulin analogs comprising for example, modified insulin B chain provide protracted time of action (see Kohn et al, for example). One of ordinary skill in the art would be motivated to further combine with Veronese et al with a reasonable expectation of success, since Veronese et al teach that PEG-drug conjugates have several advantages: a prolonged residence in body, a decreased degradation by metabolic enzymes and a reduction or elimination of protein immunogenicity. Therefore, if one of ordinary skill in the art practiced in the claimed invention of instant claims, one would necessarily achieve the claimed invention and vice versa. Response to Applicant’s Arguments Applicant argues that, “The applicants respectfully assert that the double patenting rejections will be addressed after all other rejections are resolved.” Applicant’s arguments have been fully considered but are not found persuasive. Until a properly executed terminal disclaimer is filed and approved by the Office, Double Patenting rejection is maintained. CONCLUSION No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JULIE HA whose telephone number is (571)272-5982. The examiner can normally be reached Monday-Thursday 5:00 am- 6:30 pm EST. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LIANKO GARYU can be reached at 571-270-7367. 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. /JULIE HA/Primary Examiner, Art Unit 1654 2/9/2026
Read full office action

Prosecution Timeline

Sep 15, 2021
Application Filed
Oct 06, 2024
Non-Final Rejection — §103, §DP
Jan 09, 2025
Response Filed
Mar 12, 2025
Non-Final Rejection — §103, §DP
Jun 12, 2025
Response Filed
Jul 15, 2025
Final Rejection — §103, §DP
Sep 17, 2025
Response after Non-Final Action
Oct 09, 2025
Request for Continued Examination
Oct 10, 2025
Response after Non-Final Action
Feb 09, 2026
Non-Final Rejection — §103, §DP (current)

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Prosecution Projections

4-5
Expected OA Rounds
76%
Grant Probability
99%
With Interview (+44.3%)
2y 8m
Median Time to Grant
High
PTA Risk
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