Prosecution Insights
Last updated: April 19, 2026
Application No. 17/928,759

EFFICIENT PEPTIDE CONDENSATION METHOD FOR DIFFICULT SEQUENCES

Non-Final OA §102§103§112
Filed
Nov 30, 2022
Examiner
NIEBAUER, RONALD T
Art Unit
1658
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Chugai Seiyaku Kabushiki Kaisha
OA Round
1 (Non-Final)
41%
Grant Probability
Moderate
1-2
OA Rounds
3y 6m
To Grant
75%
With Interview

Examiner Intelligence

Grants 41% of resolved cases
41%
Career Allow Rate
294 granted / 712 resolved
-18.7% vs TC avg
Strong +33% interview lift
Without
With
+33.3%
Interview Lift
resolved cases with interview
Typical timeline
3y 6m
Avg Prosecution
76 currently pending
Career history
788
Total Applications
across all art units

Statute-Specific Performance

§101
6.8%
-33.2% vs TC avg
§103
28.2%
-11.8% vs TC avg
§102
19.2%
-20.8% vs TC avg
§112
28.1%
-11.9% vs TC avg
Black line = Tech Center average estimate • Based on career data from 712 resolved cases

Office Action

§102 §103 §112
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 and Claim Status Applicant's election with traverse of the species of oxyma (additive), DIC (condensing agent) and the compound of example 1 (peptide compound) in the reply filed on 10/27/25 is acknowledged. The traversal is on the ground(s) that as amended claim 1 requires a combination of conditions including a particular molar ratio of condensing agent to second amino acid or peptide. This is not found persuasive because amended claim 1 is rejected under 102 as set forth below. As such, there is no technical feature that defines a contribution over the prior art. The requirement is still deemed proper and is therefore made FINAL. Claims 3-4 have been canceled. Claim 16 does not read on the elected peptide since the elected peptide is not cyclized. Claim 16 is withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 10/27/25. The elected peptide was not found in the prior art in the context of the instant claims. The search was extended in accord with MPEP 803.02. Claims 1-2, 5-15 and 17-21 are being examined. Priority The priority information is found in the filing receipt dated 6/22/23. Information Disclosure Statement The information disclosure statements (IDS) submitted on 6/9/23, 7/14/23 and 10/27/25 have been considered by the examiner. Specification The disclosure is objected to because of the following informalities: The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code specifically on page 7 lines 12-13. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. 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. Claim 7 is 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. Claim 7 recites ‘is the first molar ratio - 1 or less’. It is unclear if the “-“ symbol is intended to represent a negative value or if it is intended to represent a minus sign in a chemical formula. If the symbol is intended to represent a minus sign it is unclear if the ‘or less’ is also part of the equation. It is unclear if the intent is “((the first molar ratio) - 1) or less” or “(the first molar ratio – (1 or less)”. Since zero is less than 1, the values can correspond to 1 or 2 when the first molar ratio is 2. As such, there are multiple possible interpretations of the claim. Although unclear, the claim has been given the broadest reasonable interpretation consistent with the specification. 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. Claim(s) 1-2, 5, 10-13 and 19 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Takahashi (US 2010/0184952). Takahashi teach methods of peptide synthesis (section 0031). Takahashi teach a coupling step as part of the peptide synthesis that uses amino acids (section 0184), a condensing agent (section 0187) and an activating agent (section 0189) as well as a solvent (section 0190). Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH, 2.25 mmol H-Ala-OtBu.HCl, 0.55 mmol HOBt and 3.03 mmol EDC.HCl were added together in DMF (example 7 sections 0234-0235). Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235). In relation to the condensing agent as recited in claims 1 and 11, Takahashi teach a specific example in which 3.03 mmol EDC.HCl was used (section 0234). Takahashi teach that EDC is N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (section 0062) which is instant EDCI-HCl. In relation to the additive as recited in claims 1 and 10, Takahashi teach a specific example in which 0.55 mmol HOBt was used (example 7 sections 0234-0235). In relation to the first amino acid as recited in claim 1, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the second amino acid as recited in claim 1, Takahashi teach a specific example in which 2.25 mmol H-Ala-OtBu.HCl was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the amounts and ratios of claim 1, the moles of the additive (0.55 mmol HOBt) is smaller than the number of moles of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234). The molar ratio of condensing agent (3.03 mmol EDC.HCl) to second amino acid (2.25 mmol H-Ala-OtBu.HCl) is 1.35. In relation to claim 2, the molar ratio of the additive (0.55 mmol HOBt) to the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234) is 0.24. In relation to claim 5, the molar ratio of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) to the first amino acid (2.89 mmol of Fmoc-Phe-OH) (section 0234) is 0.78. In relation to claim 12, Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235) which comprises Ala and Phe. In relation to claim 13, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). With respect to N-alkylamino acid, the instant specification recognizes that the amino group may be substituted (section 0108 on page 32) and recognizes that amino acid is defined such that each group may have a substituent and there is no limit on the substituent and examples include substituted alkyl (section 0081 on page 28). The Fmoc group is 9-fluorenylmethoxycarbonyl (section 0003) which is a substituted alkyl. In relation to claim 19, Takahashi teach a specific example in which components were added together in DMF (example 7 sections 0234-0235). 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. 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) 1-2, 5-13, 15 and 17-21 is/are rejected under 35 U.S.C. 103 as being unpatentable over Takahashi (US 2010/0184952). Takahashi teach methods of peptide synthesis (section 0031) specifically methods that remove impurities (abstract). Takahashi teach a coupling step as part of the peptide synthesis that uses amino acids (section 0184), a condensing agent (section 0187) and an activating agent (section 0189) as well as a solvent (section 0190). Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH, 2.25 mmol H-Ala-OtBu.HCl, 0.55 mmol HOBt and 3.03 mmol EDC.HCl were added together in DMF (example 7 sections 0234-0235). Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235). Takahashi does not teach all of the conditions and ratios of certain claims (such as claim 6) in a single embodiment. Takahashi recognizes that the order of addition of amino acids is not particularly limited (section 0184). Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150). Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract). Takahashi teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005). Takahashi teach that Fmoc is utilized for solid phase synthesis (section 0007). It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Takahashi based on the specific suggestions of Takahashi. With respect to the amounts of the components to use, Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Thus, based on the specific suggestions of Takahashi one would have been motivated to use various amounts to limit excess of amino acid, promote the reaction and suppress the side reaction. Since Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150) one would have been motivated to use such amino acids. Since Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract) and teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005) and teach that Fmoc is utilized for solid phase synthesis (section 0007) one would have applied the method for such purposes. One would have had a reasonable expectation of success since the components and methods of adding them together were known (compare example 7 of Takahashi). In relation to the condensing agent as recited in claims 1 and 11, Takahashi teach a specific example in which 3.03 mmol EDC.HCl was used (section 0234). Takahashi teach that EDC is N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (section 0062) which is instant EDCI-HCl. In relation to the additive as recited in claims 1 and 10, Takahashi teach a specific example in which 0.55 mmol HOBt was used (example 7 sections 0234-0235). In relation to the first amino acid as recited in claim 1, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the second amino acid as recited in claim 1, Takahashi teach a specific example in which 2.25 mmol H-Ala-OtBu.HCl was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the amounts and ratios of claim 1, the moles of the additive (0.55 mmol HOBt) is smaller than the number of moles of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234). The molar ratio of condensing agent (3.03 mmol EDC.HCl) to second amino acid (2.25 mmol H-Ala-OtBu.HCl) is 1.35. In relation to claim 2, the molar ratio of the additive (0.55 mmol HOBt) to the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234) is 0.24. In relation to claim 5, the molar ratio of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) to the first amino acid (2.89 mmol of Fmoc-Phe-OH) (section 0234) is 0.78. In relation to the amounts and ratios of the claims including claims 6-9 and 17-18, Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Thus, Takahashi generally recognizes a range of amounts up to 4 equivalents and suggest the agents for specific purposes (see MPEP 2144.05 II A). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists. In relation to claim 12, Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235) which comprises Ala and Phe. In relation to claim 13, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). With respect to N-alkylamino acid, the instant specification recognizes that the amino group may be substituted (section 0108 on page 32) and recognizes that amino acid is defined such that each group may have a substituent and there is no limit on the substituent and examples include substituted alkyl (section 0081 on page 28). The Fmoc group is 9-fluorenylmethoxycarbonyl (section 0003) which is a substituted alkyl. In relation to claims 13 and 15, Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150). Proline is an N-alkylamino acid. In relation to claim 19, Takahashi teach a specific example in which components were added together in DMF (example 7 sections 0234-0235). In relation to claims 20-21, Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract). Takahashi teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005). Takahashi teach that Fmoc is utilized for solid phase synthesis (section 0007). Claim(s) 1-2, 5-15 and 17-21 is/are rejected under 35 U.S.C. 103 as being unpatentable over Takahashi (US 2010/0184952) in view of Obrecht et al. (US 2015/0051183; ‘Obrecht’). Takahashi teach methods of peptide synthesis (section 0031) specifically methods that remove impurities (abstract). Takahashi teach a coupling step as part of the peptide synthesis that uses amino acids (section 0184), a condensing agent (section 0187) and an activating agent (section 0189) as well as a solvent (section 0190). Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH, 2.25 mmol H-Ala-OtBu.HCl, 0.55 mmol HOBt and 3.03 mmol EDC.HCl were added together in DMF (example 7 sections 0234-0235). Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235). Takahashi does not teach an example with an amino acid as in claim 14. Takahashi recognizes that the order of addition of amino acids is not particularly limited (section 0184). Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150). Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract). Takahashi teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005). Takahashi teach that Fmoc is utilized for solid phase synthesis (section 0007). Obrecht teach structures with medical applications that can be made by combinatorial chemistry in solution or solid phase (abstract) and recognizes methods of peptide synthesis including those that use Fmoc (section 0283). Obrecht teach specific examples that include combining peptides including Fmoc-NMe-beta-Ala-OH (Table 22a example 193h page 144). On page 200, Obrecht shows the compound containing NMe-beta-Ala (85h-Ex. 193h). Obrecht shows that preparation of Fmoc-NMe-beta-Ala-OH was known (section 0445). It would have been obvious to one of ordinary skill in the art before the effective filing date to modify the teachings of Takahashi based on the specific suggestions of Takahashi. With respect to the amounts of the components to use, Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Thus, based on the specific suggestions of Takahashi one would have been motivated to use various amounts to limit excess of amino acid, promote the reaction and suppress the side reaction. Since Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150) one would have been motivated to use such amino acids. Since Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract) and teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005) and teach that Fmoc is utilized for solid phase synthesis (section 0007) one would have applied the method for such purposes. Further, since Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150) one would have been motivated to use the method for known peptide containing compounds such as those of Obrecht. Obrecht recognizes methods of peptide synthesis including those that use Fmoc (section 0283). Obrecht teach specific examples that include combining peptides including Fmoc-NMe-beta-Ala-OH (Table 22a example 193h page 144). On page 200, Obrecht shows the compound containing NMe-beta-Ala (85h-Ex. 193h). One would have had a reasonable expectation of success since the components and methods of adding them together were known (compare example 7 of Takahashi and section 0445 of Obrecht). In relation to the condensing agent as recited in claims 1 and 11, Takahashi teach a specific example in which 3.03 mmol EDC.HCl was used (section 0234). Takahashi teach that EDC is N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (section 0062) which is instant EDCI-HCl. In relation to the additive as recited in claims 1 and 10, Takahashi teach a specific example in which 0.55 mmol HOBt was used (example 7 sections 0234-0235). In relation to the first amino acid as recited in claim 1, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the second amino acid as recited in claim 1, Takahashi teach a specific example in which 2.25 mmol H-Ala-OtBu.HCl was used (example 7 sections 0234-0235). Instant claim 1 does not distinguish the first or second amino acid and Takahashi refers to 2 amino acids that are added (section 0234) so either amino acid could be considered the first. In relation to the amounts and ratios of claim 1, the moles of the additive (0.55 mmol HOBt) is smaller than the number of moles of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234). The molar ratio of condensing agent (3.03 mmol EDC.HCl) to second amino acid (2.25 mmol H-Ala-OtBu.HCl) is 1.35. In relation to claim 2, the molar ratio of the additive (0.55 mmol HOBt) to the second amino acid (2.25 mmol H-Ala-OtBu.HCl) (section 0234) is 0.24. In relation to claim 5, the molar ratio of the second amino acid (2.25 mmol H-Ala-OtBu.HCl) to the first amino acid (2.89 mmol of Fmoc-Phe-OH) (section 0234) is 0.78. In relation to the amounts and ratios of the claims including claims 6-9 and 17-18, Takahashi teach that the amounts of the amino acids can be varied to limit excess and teach that generally 0.9 to 4 equivalents of one amino acid to another can be used (section 0185). Takahashi teach that the activator promotes the reaction and suppresses side reactions (section 0188) and that generally 0 to 4 equivalents of activator to amino acid can be used (section 0189). Takahashi teach the condensing agent for formation of the peptide (section 0184) and teach that the amount used is generally 0.8 to 4 equivalents of amino acid (section 0187). Thus, Takahashi generally recognizes a range of amounts up to 4 equivalents and suggest the agents for specific purposes (see MPEP 2144.05 II A). Further, MPEP 2144.05 recognizes that where the claimed ranges overlap or lie inside ranges disclosed by the prior art a prima facie case of obviousness exists. In relation to claim 12, Takahashi teach peptide synthesis including another addition step to make Fmoc-Ser(tBu)-Phe-Ala-OtBu (sections 0234-0235) which comprises Ala and Phe. In relation to claim 13, Takahashi teach a specific example in which 2.89 mmol of Fmoc-Phe-OH was used (example 7 sections 0234-0235). With respect to N-alkylamino acid, the instant specification recognizes that the amino group may be substituted (section 0108 on page 32) and recognizes that amino acid is defined such that each group may have a substituent and there is no limit on the substituent and examples include substituted alkyl (section 0081 on page 28). The Fmoc group is 9-fluorenylmethoxycarbonyl (section 0003) which is a substituted alkyl. In relation to claims 13 and 15, Takahashi teach that the amino acid is not limited and includes Pro and beta-Ala (sections 0149-0150). Proline is an N-alkylamino acid. In relation to claims 13-15, Obrecht teach specific examples that include combining peptides including Fmoc-NMe-beta-Ala-OH (Table 22a example 193h page 144). On page 200, Obrecht shows the compound containing NMe-beta-Ala (85h-Ex. 193h). Obrecht shows that preparation of Fmoc-NMe-beta-Ala-OH was known (section 0445). In relation to claim 19, Takahashi teach a specific example in which components were added together in DMF (example 7 sections 0234-0235). In relation to claims 20-21, Takahashi teach methods specifically for compounds protected with an Fmoc group (abstract). Takahashi teach the use of amino protecting groups specifically Fmoc because it provides many advantages (section 0005). Takahashi teach that Fmoc is utilized for solid phase synthesis (section 0007). Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to RONALD T NIEBAUER whose telephone number is (571)270-3059. The examiner can normally be reached M - F 6:30 - 2:30 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, Melissa 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. 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. RONALD T. NIEBAUER Primary Examiner Art Unit 1658 /RONALD T NIEBAUER/Examiner, Art Unit 1658
Read full office action

Prosecution Timeline

Nov 30, 2022
Application Filed
Jan 26, 2026
Non-Final Rejection — §102, §103, §112 (current)

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Prosecution Projections

1-2
Expected OA Rounds
41%
Grant Probability
75%
With Interview (+33.3%)
3y 6m
Median Time to Grant
Low
PTA Risk
Based on 712 resolved cases by this examiner. Grant probability derived from career allow rate.

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