Office Action Predictor
Last updated: April 15, 2026
Application No. 18/024,258

NOVEL ENDO-ß-N-ACETYLGLUCOSAMINIDASE

Final Rejection §101§102§103§112§DP
Filed
Mar 01, 2023
Examiner
PAK, YONG D
Art Unit
1652
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Daiichi Sankyo Company, Limited
OA Round
2 (Final)
74%
Grant Probability
Favorable
3-4
OA Rounds
2y 10m
To Grant
88%
With Interview

Examiner Intelligence

Grants 74% — above average
74%
Career Allow Rate
685 granted / 924 resolved
+14.1% vs TC avg
Moderate +14% lift
Without
With
+14.0%
Interview Lift
resolved cases with interview
Typical timeline
2y 10m
Avg Prosecution
55 currently pending
Career history
979
Total Applications
across all art units

Statute-Specific Performance

§101
7.0%
-33.0% vs TC avg
§103
21.0%
-19.0% vs TC avg
§102
21.9%
-18.1% vs TC avg
§112
32.7%
-7.3% vs TC avg
Black line = Tech Center average estimate • Based on career data from 924 resolved cases

Office Action

§101 §102 §103 §112 §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 . DETAILED ACTION This application is a 371 of PCT/JP2021/032083. The response filed on November 26, 2025 has been entered. Election/Restrictions Applicant elected without traverse of Group I with a species election of (A1) positions 34-928 of SEQ ID NO:2 as the parent polypeptide, (A2) D241M/Q311L as the amino acid modifications made in the parent polypeptide or the polypeptide having the amino acid sequence of SEQ ID NO:7, (B) improvement in the transglycosylation rate as the property of the amino acid modifications, and the N-linked sugar [N3-PEG(3)]-MSG1-)Asn-PEG(3)-N3 as the sugar donor in in the reply filed on July 11, 2025 is acknowledged. Claims 12-15 and 17-44 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species and invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on July 22, 2025. Status of Claims Claims 1, 5-7, 9-15, and 17-44 are pending. Claims 12-15 and 17-44 are withdrawn. Claims 1, 5-7, and 9-11 are under examination. Information Disclosure Statement The information disclosure statement (IDS) submitted on February 17, 2026, October 29, 2025, and October 9, 2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner. Response to Amendments/Arguments Claim Objections Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claim 16 have been fully considered and are persuasive. Claim 16 has been cancelled. Therefore, the objection of claim 16 has been withdrawn. Claim Rejections - 35 USC § 112(b) Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claim 1 and claims depending therefrom have been fully considered and are persuasive. Claim 1 has been amended to recite “an amino acid sequence of amino acid positions 34 to 928. Therefore, the rejection of claim 1 and claims depending under 35 U.S.C. 112(b) has been withdrawn. Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claims 1-2 and 4 and claims depending therefrom have been fully considered and are persuasive. Claim 1 has been amended to delete amino acid positions at 341 and 311. Claims 2 and 4 have been cancelled. Therefore, the rejection of claims 1-2 and 4 and claims depending therefrom under 35 U.S.C. 112(b) has been withdrawn. Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claim 3 have been fully considered and are persuasive. Claim 3 has been cancelled. Therefore, the rejection of claim 3 under 35 U.S.C. 112(b) has been withdrawn. Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claim 5 have been fully considered and are persuasive. Due to the amendment of claim 1 and claim 5, the limitation of the polypeptide recited in claim 5 is definite. Therefore, the rejection of claim 5 under 35 U.S.C. 112(b)has been withdrawn. Applicant’s arguments, see page 10 of the Remarks, filed November 26, 2025, with respect to claim 5 have been fully considered and are persuasive. Claim 5 has been amended to delete the indefinite limitations of clauses (B) and (C). Therefore, the rejection of claim 5 under 35 U.S.C. 112(b) has been withdrawn. Applicant’s arguments, see page 11 of the Remarks, filed November 26, 2025, with respect to claims 8-9 and claims depending therefrom have been fully considered and are persuasive. Claims 8-9 have been amended to delete the usage of parenthesis. Therefore, the rejection of claims 8-9 and claims depending therefrom under 35 U.S.C. 112(b) has been withdrawn. Applicant’s arguments, see page 11 of the Remarks, filed November 26, 2025, with respect to claim 10 have been fully considered and are persuasive. Therefore, the rejection of claim 10 under 35 U.S.C. 112(b) has been withdrawn. Claim Rejections - 35 USC § 112(d) Applicant’s arguments, see page 11 of the Remarks, filed November 26, 2025, with respect to claim 3 have been fully considered and are persuasive. Claim 3 has been cancelled. Therefore, the rejection of claim 3 under 35 U.S.C. 112(d) has been withdrawn. Applicant’s arguments, see page 11 of the Remarks, filed November 26, 2025, with respect to claim 5 have been fully considered and are persuasive. Claim 5 has been amended to property depend from claim 1. Therefore, the rejection of claim 5under 35 U.S.C. 112(d) has been withdrawn. Applicant’s arguments, see page 11 of the Remarks, filed November 26, 2025, with respect to claim 11 have been fully considered and are persuasive. Claim 11 has been amended to property depend from claim 9. Therefore, the rejection of claim 11 under 35 U.S.C. 112(d) has been withdrawn. Claim Rejections - 35 USC § 112(a) Applicant' s arguments, see pages 11-12 of the Remarks, filed November 26, 2025, with respect to claims 1-11 and 16 have been fully considered and are persuasive. Claims 1-2 have been amended to recite a specific amino acid sequence. Therefore, the rejections of claims 1-11 and 16 under 35 U.S.C. 112(a) for lack of written description and lack of enablement have been withdrawn. Claim Rejections - 35 USC § 102 Applicant' s arguments, see page 12 of the Remarks, filed November 26, 2025, with respect to claims 1, 6-11, and 16 have been fully considered and are persuasive. Claim 1 has been amended to recite a polypeptide comprising amino acids 34-928 of SEQ ID NO:7, which is not taught or suggested by A0A3L8GF62_STRIN (UniProtKB/TrEMBL Database. April 10, 2019 – cited previously on form PTO-892). Therefore, the rejection of claims 1, 6-11, and 16 under 35 U.S.C. 102(a)(1) as being anticipated by A0A3L8GF62_STRIN has been withdrawn. Applicant' s arguments, see page 12 of the Remarks, filed November 26, 2025, with respect to claims 1-11 and 16 have been fully considered and are persuasive. Claim 1 has been amended to recite a polypeptide comprising amino acids 34-928 of SEQ ID NO:7, which is not taught or suggested by Yu (102(a)(1) and 102(a)(2): US 2020/0062861– form PTO-892. 102(a)(2): US 11,203,645 – form PTO-892). Therefore, the rejection of claims 1-11 and 16 under 35 U.S.C. 102(a)(1) and/or as being anticipated by Yu has been withdrawn. Applicant' s arguments, see page 12 of the Remarks, filed November 26, 2025, with respect to claims 1-11 and 16 have been fully considered and are persuasive. Claim 1 has been amended to recite a polypeptide comprising amino acids 34-928 of SEQ ID NO:7, which is not taught or suggested by Kawaguchi (102(a)(1): US 2018/0208915– form PTO-1449. 102(a)(2): US 11,001,819 – form PTO-892). Therefore, the rejection of claims 1-11 and 16 under 35 U.S.C. 102(a)(1) and/or as being anticipated by Kawaguchi has been withdrawn. Claim Rejections - 35 USC § 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, 5-7, and 9-11 is/are rejected under 35 U.S.C. 103 as being unpatentable over A0A3L8GF62_STRIN (UniProtKB/TrEMBL Database. April 10, 2019 – cited previously on form PTO-892) and Kawaguchi (US 2018/0208915– form PTO-1449). Regarding claims 1 and 5, A0A3L8GF62_STRIN discloses a Streptococcus endo-beta-N-acetylglucosaminidase having 100% sequence identity to the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of the instant application (page 1 and see the sequence alignment below). The endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN has sugar chain hydrolysis activity. A0A3L8GF62_STRIN does not disclose endo-beta-N-acetylglucosaminidase variants having the amino acid sequence of SEQ ID NO:3 (D241Q), SEQ ID NO:4 (D241Q/Q311L), or SEQ ID NO:5 (D241Q/E360Q) of the instant application. SEQ ID NO:3-5 are endo-beta-N-acetylglucosaminidase variants of Streptococcus endo-beta-N-acetylglucosaminidase, wherein the variant consists of a D241Q, D241Q/Q311L, or D241Q/E360Q amino acid substitutions, respectively. Regarding claim 1 and 5, Kawaguchi discloses endo-beta-N-acetylglucosaminidase mutants having the amino acid sequence of SEQ ID NO:1, 4, and 7, which is the “EndoS D233Q”, “EndoS D233Q /Q303L”, and “EndoS D233Q/E350Q” in Figure 4 (abstract, Figure 4, and [0111]). The amino acid position D233, Q303, and E350 of Kawaguchi corresponds to D241, Q311, and E360 of the endo-beta-N-acetylglucosaminidase of SEQ ID NO:3, 4, or 5 (see the sequence alignments below). Regarding claim 6, the endo-beta-N-acetylglucosaminidase mutants have hydrolysis activity and improved transglycosylation activity on a fucosylate core GlcNAc of an IgG Fc region ([0028]-[0030], [0081]-[0084], [0093]-[0095], [0111], and [0123]-[0127]). Regarding claim 7, the fucosylated core GlcNAc is in an N-linked sugar chain ([0081]-[0084], [0093]-[0095], [0111], and [0123]-[0127]). Regarding claim 9, the N-linked sugar chain is N297-linked sugar chain linked to an Asn at position 297 of the IgG Fc region ([0081]-[0084], [0093]-[0095], [0111], and [0123]-[0127]). Regarding claim 10, the N297-linked sugar chain is a complex-type sugar chain having a non-reducing end ([0081]-[0084], [0093]-[0095], [0111], and [0123]-[0127]). Regarding claim 11, the N-297 linked sugar chain is a fucosylated core GlcNAc ([0081]-[0084], [0093]-[0095], [0111], and [0123]-[0127]). Therefore, combining the teachings of A0A3L8GF62_STRIN and Kawaguchi, it would have been obvious to one having ordinary skill in the art before the claimed invention was effectively filed to enhance the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN by introducing D241Q, D241Q/Q311L, or D241Q/E360Q amino acid substitution as taught by Kawaguchi to arrive at the endo-beta-N-acetylglucosaminidase variants having the amino acid sequence of SEQ ID NO:3 (D241Q), SEQ ID NO:4 (D241Q/Q311L), and SEQ ID NO:5 (D241Q/E360Q). Using the known technique of introducing amino acid substitutions (D241Q, D241Q/Q311L, or D241Q/E360Q) in the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN for improving transglycosylation would have been obvious to one of ordinary skill. The rationale supporting that the claims would have been obvious is that a method of enhancing a particular class of devices (Streptococcus endo-beta-N-acetylglucosaminidase having improved transglycosylation due to D241Q, D241Q/Q311L, or D241Q/E360Q amino acid substitutions) has been made part of the ordinary capabilities of one skilled in the art based upon the teaching of such improvement in other situations. One of ordinary skill in the art would have been capable of applying this known method of enhancement to a “base” device (Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN) in the prior art and the results would have been predictable to one of ordinary skill in the art. Therefore, the above references render claims 1, 5-7, and 9-11 prima facie obvious. Applicant's arguments filed November 26, 2025 have been fully considered but they are not persuasive. Applicant argues that none of the cited references teach or suggest the specifically recited mutated Endo-Si (endo-beta-N-acetylglucosaminidase) enzymes sequences. This is not found persuasive. The endo-beta-N-acetylglucosaminidase variants having the amino acid sequence of SEQ ID NO:3-5 of the instant application are variants of SEQ ID NO:2 of the instant application, wherein the variant consists of D241Q (SEQ ID NO:3), D241Q/Q311L (SEQ ID NO:4) or D241Q/E360Q (SEQ ID NO:5) of the instant application. A0A3L8GF62_STRIN discloses a Streptococcus endo-beta-N-acetylglucosaminidase having 100% sequence identity to the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of the instant application. Kawaguchi discloses endo-beta-N-acetylglucosaminidase mutants having D223Q, D233Q /Q303L, or D233Q/E350Q amino acid substitution(s). The amino acid position D233, Q303, and E350 of Kawaguchi corresponds to D241, Q311, and E360 of the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2, 3, 4, or 5 of the instant application. Therefore, combining the teachings of A0A3L8GF62_STRIN and Kawaguchi, it would have been obvious to one having ordinary skill in the art before the claimed invention was effectively filed to enhance the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN by introducing D241Q, D241Q/Q311L, or D241Q/E360Q amino acid substitution as taught by Kawaguchi to arrive at the endo-beta-N-acetylglucosaminidase variants having the amino acid sequence of SEQ ID NO:3 (D241Q), SEQ ID NO:4 (D241Q/Q311L), and SEQ ID NO:5 (D241Q/E360Q) of the instant application. Applicant argues that the claimed sequences have significantly improved transglycosylation activity compared to the wild type and as demonstrated in Tables 5-6, the enzymes of SEQ ID NO:3-11 showed significantly improved transglycosylation activity compared to wildtype Endo-Si. This is not found persuasive. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., significantly improved transglycosylation activity compared to wildtype Endo-S) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Further, improved transglycosylation activity compared to wildtype Endo-S is an inherent property of the variants of the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN, wherein the variants consist of D241Q, D241Q/Q311L or D241Q/E360Q amino acid substitution(s), because said variants have identical chemical structure as the endo-beta-N-acetylglucosaminidase variants of SEQ ID NO:3 (D241Q), SEQ ID NO:4 (D241Q/Q311L), and SEQ ID NO:5 (D241Q/E360Q), respectively, of the instant application. MPEP 2112.01 states that “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable.” Since the variants of the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN have identical chemical structure as the endo-beta-N-acetylglucosaminidase variants of SEQ ID NO:3, 4, or 5 of the instant application, the recited property “significantly improved transglycosylation activity compared to wildtype Endo-S” is necessarily present. MPEP 2112 II states that “There is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference.” Hence the rejection has been maintained. Claim(s) 1, 5-7, and 9-11 is/are rejected under 35 U.S.C. 103 as being unpatentable over A0A3L8GF62_STRIN (UniProtKB/TrEMBL Database. April 10, 2019 – cited previously on form PTO-892) and Yu (US 2020/0062861– cited previously on form PTO-892 or US 11,203,645 – cited previously on form PTO-892. US 2020/0062861 is used for specific passages of Yu). Regarding claims 1 and 5, A0A3L8GF62_STRIN discloses a Streptococcus endo-beta-N-acetylglucosaminidase having 100% sequence identity to the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of the instant application (page 1 and see the sequence alignment below). The endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN has sugar chain hydrolysis activity. A0A3L8GF62_STRIN does not disclose endo-beta-N-acetylglucosaminidase variants having the amino acid sequence of SEQ ID NO:6 (D241M). SEQ ID NO:6 is endo-beta-N-acetylglucosaminidase variant of Streptococcus endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of the instant application, wherein the variant consists of a D241M amino acid substitution. Regarding claims 1 and 5, Yu discloses an “EndoSn-D234M” variant, which is an endo-beta-N-acetylglucosaminidase mutant having the amino acid sequence of SEQ ID NO:2 (abstract, Figure 4, page 3). The amino acid position D234 of Yu corresponds to D241 of the endo-beta-N-acetylglucosaminidase of SEQ ID NO:6 (see the sequence alignments below). The EndoSn-D234M mutant has hydrolysis activity and improved transglycosylation activity ([0027]-[0029]). Regarding claim 6, the EndoSn-D234M mutant has hydrolysis activity and improved transglycosylation activity on a fucosylated core GlcNAc of an IgG Fc region ([0027]-[0029]). Regarding claim 7, the fucosylated core GlcNAc is an N-linked sugar chain ([0027]-[0029]). Regarding claim 9, the N-linked sugar chain is N297-linked sugar chain linked to an Asn at position 297 of the IgG Fc region ([0027]-[0029]). Regarding claim 10, the N297-linked sugar chain is a complex-type sugar chain having a non-reducing end ([0027]-[0029] and [0061]-[0062]). Regarding claim 11, the N-297 linked sugar chain is a fucosylated core GlcNAc ([0027]-[0029]). Therefore, combining the teachings of A0A3L8GF62_STRIN and Yu, it would have been obvious to one having ordinary skill in the art before the claimed invention was effectively filed to enhance the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN by introducing D241M amino acid substitution as taught by Yu to arrive at the endo-beta-N-acetylglucosaminidase variant having the amino acid sequence of SEQ ID NO:6 (D241M) of the instant application. Using the known technique of introducing amino acid substitutions (D241M) in the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN for improving transglycosylation of the would have been obvious to one of ordinary skill. The rationale supporting that the claims would have been obvious is that a method of enhancing a particular class of devices (Streptococcus endo-beta-N-acetylglucosaminidase having improved transglycosylation due to D241M amino acid substitution) has been made part of the ordinary capabilities of one skilled in the art based upon the teaching of such improvement in other situations. One of ordinary skill in the art would have been capable of applying this known method of enhancement to a “base” device (Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN) in the prior art and the results would have been predictable to one of ordinary skill in the art. Therefore, the above references render claims 1, 5-7, and 9-11 prima facie obvious. Applicant argues that none of the cited references teach or suggest the specifically recited mutated Endo-Si (endo-beta-N-acetylglucosaminidase) enzymes sequences. This is not found persuasive. The endo-beta-N-acetylglucosaminidase variant having the amino acid sequence of SEQ ID NO:6 of the instant application is a variant of SEQ ID NO:2 of the instant application, wherein the variant consists of D241M (SEQ ID NO:6). A0A3L8GF62_STRIN discloses a Streptococcus endo-beta-N-acetylglucosaminidase having 100% sequence identity to the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of the instant application. Yu discloses an endo-beta-N-acetylglucosaminidase mutant having D234M amino acid substitution. The amino acid position D234 of Yu corresponds to D241 of the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 or 6 of the instant application. Therefore, combining the teachings of A0A3L8GF62_STRIN and Yu, it would have been obvious to one having ordinary skill in the art before the claimed invention was effectively filed to enhance the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN by introducing a D241M amino acid substitution as taught by Yu to arrive at the endo-beta-N-acetylglucosaminidase variant having the amino acid sequence of SEQ ID NO:6 (D241M) of the instant application. Applicant argues that the claimed sequences have significantly improved transglycosylation activity compared to the wild type and as demonstrated in Tables 5-6, the enzymes of SEQ ID NO:3-11 showed significantly improved transglycosylation activity compared to wildtype Endo-Si. This is not found persuasive. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., significantly improved transglycosylation activity compared to wildtype Endo-S) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Further, improved transglycosylation activity compared to wildtype Endo-S is an inherent property of the variant of the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN, wherein the variants consist of D241M amino acid substitution, because said variant has identical chemical structure as the endo-beta-N-acetylglucosaminidase variant of SEQ ID NO:6 (D241M) of the instant application. MPEP 2112.01 states that “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable.” Since the variant of the Streptococcus endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN has identical chemical structure as the endo-beta-N-acetylglucosaminidase variant of SEQ ID NO:6 of the instant application, the recited property “significantly improved transglycosylation activity compared to wildtype Endo-S” is necessarily present. MPEP 2112 II states that “There is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference.” Hence the rejection has been maintained. Claim Rejections - 35 USC § 101 Applicant's arguments, see page 13 of the Remarks, filed November 26, 2025, with respect to claims 1, 6-11, and 16 have been fully considered and are persuasive. Claim 1 has been amended to recite a polypeptide comprising amino acids 34-928 of SEQ ID NO:7, which does not read on a product of nature. Therefore, the rejection of claims 1, 6-11, and 16 under 35 U.S.C. 101 has been withdrawn. Double Patenting Applicant's arguments, see pages 13-14 of the Remarks, filed November 26, 2025, with respect to claims 1-9, 11, and 16 have been fully considered and are persuasive. Claim 1 has been amended to recite a polypeptide comprising amino acids 34-928 of SEQ ID NO:7, which is not recited in the claims of U.S. Patent No. 11,001,819. Therefore, the nonstatutory double patenting rejection of claims 1-9, 11, and 16 has been withdrawn. Conclusion Claims 1, 5-7, 9-15, and 17-44 are pending. Claims 12-15 and 17-44 are withdrawn. Claims 1, 5-7, and 9-11 are rejected. 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 YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm. 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, Robert Mondesi can be reached on 408-918-7584. 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. /YONG D PAK/Primary Examiner, Art Unit 1652 Sequence alignment between the polypeptide of SEQ ID NO:2 of the instant application (“Qy”) and the endo-beta-N-acetylglucosaminidase of A0A3L8GF62_STRIN (“Db”) A0A3L8GF62_STRIN ID A0A3L8GF62_STRIN Unreviewed; 928 AA. AC A0A3L8GF62; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 18-JUN-2025, entry version 27. DE RecName: Full=mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase {ECO:0000256|ARBA:ARBA00012566}; DE EC=3.2.1.96 {ECO:0000256|ARBA:ARBA00012566}; GN ORFNames=DIY07_08980 {ECO:0000313|EMBL:RLU55257.1}; OS Streptococcus iniae (Streptococcus shiloi). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1346 {ECO:0000313|EMBL:RLU55257.1, ECO:0000313|Proteomes:UP000269148}; RN [1] {ECO:0000313|EMBL:RLU55257.1, ECO:0000313|Proteomes:UP000269148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QMA0445 {ECO:0000313|EMBL:RLU55257.1, RC ECO:0000313|Proteomes:UP000269148}; RA Barnes A.C., Silayeva O.; RT "Mutators as drivers of adaptation in pathogenic bacteria and a risk factor RT for host jumps and vaccine escape."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta- CC D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl- CC [protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]- CC beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L- CC asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603, CC Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248, CC ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; EC=3.2.1.96; CC Evidence={ECO:0000256|ARBA:ARBA00034414}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. CC {ECO:0000256|ARBA:ARBA00009336}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RLU55257.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QLQD01000076; RLU55257.1; -; Genomic_DNA. DR RefSeq; WP_003102174.1; NZ_QLSP01000075.1. DR AlphaFoldDB; A0A3L8GF62; -. DR SMR; A0A3L8GF62; -. DR STRING; 1346.BMF34_08885; -. DR KEGG; sio:DW64_08875; -. DR KEGG; siq:DQ08_08895; -. DR KEGG; siz:SI82_08880; -. DR OrthoDB; 7183084at2; -. DR Proteomes; UP000269148; Unassembled WGS sequence. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd06542; GH18_EndoS-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR InterPro; IPR049410; EndoS-like_Ig-like. DR InterPro; IPR057016; EndoS_F2-like_TIM-barrel. DR InterPro; IPR001579; Glyco_hydro_18_chit_AS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR032675; LRR_dom_sf. DR Pfam; PF20746; EndoS_Ig-like; 1. DR Pfam; PF23952; LRR_EndoS; 1. DR Pfam; PF23916; TIM-barrel_EndoS; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS01095; GH18_1; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 124..408 FT /note="Endo-beta-N-acetylglucosaminidase EndoS/F2-like TIM- FT barrel" FT /evidence="ECO:0000259|Pfam:PF23916" FT DOMAIN 638..760 FT /note="Endo-beta-N-acetylglucosaminidase EndoS-like Ig- FT like" FT /evidence="ECO:0000259|Pfam:PF20746" FT REGION 905..928 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 928 AA; 104646 MW; 0EE526322AEA087B CRC64; Query Match 100.0%; Score 4809; Length 928; Best Local Similarity 100.0%; Matches 928; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 MNKRLLVKRTFGCVCAAAILGVAPLSHPTIVEAREELKMPNGLEQSIADVEAKIDALTYL 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MNKRLLVKRTFGCVCAAAILGVAPLSHPTIVEAREELKMPNGLEQSIADVEAKIDALTYL 60 Qy 61 SKNSKDEFKHSMYEIPSNREHKPVSPKQALQNAKKADAQAERLAKMTIPKKEELKALEGP 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 SKNSKDEFKHSMYEIPSNREHKPVSPKQALQNAKKADAQAERLAKMTIPKKEELKALEGP 120 Qy 121 LYGGYFRTWQDKTSDPTETNKVNSFGELPKEVDLAFVFHDYTKDYSLFWEELATKQVPKL 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 LYGGYFRTWQDKTSDPTETNKVNSFGELPKEVDLAFVFHDYTKDYSLFWEELATKQVPKL 180 Qy 181 NKQGTRVIRTIPWRFLSGADHSDISADKEKFPNTEAGNKALAKAIVDEYVYKYNLDGLDI 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 NKQGTRVIRTIPWRFLSGADHSDISADKEKFPNTEAGNKALAKAIVDEYVYKYNLDGLDI 240 Qy 241 DIERDSVPKVNDKEDPEALARTVEVFKEIGKLIGANGADKSRLLIMDTTYTAEENPLIKE 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 DIERDSVPKVNDKEDPEALARTVEVFKEIGKLIGANGADKSRLLIMDTTYTAEENPLIKE 300 Qy 301 TAQYLNLLLVQVYGFSGENGNYLHHKNILDETSSMEGRWQGYSKYIRPEQYMVGFSFYEE 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 TAQYLNLLLVQVYGFSGENGNYLHHKNILDETSSMEGRWQGYSKYIRPEQYMVGFSFYEE 360 Qy 361 KDFNNRWKDINEEDPSDPHIGEKIQGTRAERYAKWQPKTGGLKGGLFSYAIDRDGVAQPK 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 KDFNNRWKDINEEDPSDPHIGEKIQGTRAERYAKWQPKTGGLKGGLFSYAIDRDGVAQPK 420 Qy 421 QKTEHPELDKIVKSEYKVSKALKKLMMTDDQYQPIDQSDFPDKALRESIIKQVGTRRGDL 480 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 421 QKTEHPELDKIVKSEYKVSKALKKLMMTDDQYQPIDQSDFPDKALRESIIKQVGTRRGDL 480 Qy 481 ERFKGTLRLDNPEIKDLTGLNKLKRVAKLELINLPKITKIDKDDLPQNLKPLTDNQKSNL 540 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 481 ERFKGTLRLDNPEIKDLTGLNKLKRVAKLELINLPKITKIDKDDLPQNLKPLTDNQKSNL 540 Qy 541 EIKGTYDDSKLYKDIPAFDLVISGLSGLESLDISGHQRDTLSGIDASTLPSLKAINISDN 600 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 541 EIKGTYDDSKLYKDIPAFDLVISGLSGLESLDISGHQRDTLSGIDASTLPSLKAINISDN 600 Qy 601 HFDLAQGTENRHILDTILATLAKNGASTASFDKQKPKGLYPESYSTAPLHLQVGQGKINV 660 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 601 HFDLAQGTENRHILDTILATLAKNGASTASFDKQKPKGLYPESYSTAPLHLQVGQGKINV 660 Qy 661 IDDLIFGTRTNQNTLINTENDFEAYKEQTIQGKPFIAPDYLYDNFKVSYKEYSASIVDST 720 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 661 IDDLIFGTRTNQNTLINTENDFEAYKEQTIQGKPFIAPDYLYDNFKVSYKEYSASIVDST 720 Qy 721 LAETTDKTIDTAKAETYQVTVSNKDGKTVHSVKVIVGDEKPMMVNLAQDAKIIGTDNMTQ 780 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 721 LAETTDKTIDTAKAETYQVTVSNKDGKTVHSVKVIVGDEKPMMVNLAQDAKIIGTDNMTQ 780 Qy 781 SAKVFDGQKDQFLLSWNKDSSVIFELKTPGTAKHWRFFDDGKNDSVTLSVFKGDASNFET 840 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 781 SAKVFDGQKDQFLLSWNKDSSVIFELKTPGTAKHWRFFDDGKNDSVTLSVFKGDASNFET 840 Qy 841 EKDKAENWVEITKDSRKNDDKVFSSPLEVDNAKYLKVTIKKEAKYIYFNELQILGYPGVV 900 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 841 EKDKAENWVEITKDSRKNDDKVFSSPLEVDNAKYLKVTIKKEAKYIYFNELQILGYPGVV 900 Qy 901 AKKTADDLRPTEADKSDDKSDKNDTEAK 928 |||||||||||||||||||||||||||| Db 901 AKKTADDLRPTEADKSDDKSDKNDTEAK 928 Sequence alignment between the polypeptide of SEQ ID NO:2 of the instant application (“Qy”) and the endoglycosidase “EndoSn-D234M” of SEQ ID NO:2 of Yu (“Db”) US-16-454-750-2 Sequence 2, US/16454750 Publication No. US20200062861A1 GENERAL INFORMATION APPLICANT: OBI PHARMA, INC. TITLE OF INVENTION: GLYCOSYNTHASE VARIANTS FOR GLYCOPROTEIN ENGINEERING AND METHODS TITLE OF INVENTION: OF USE FILE REFERENCE: G3004-01101 CURRENT APPLICATION NUMBER: US/16/454,750 CURRENT FILING DATE: 2019-06-27 PRIOR APPLICATION NUMBER: 62/690,669 PRIOR FILING DATE: 2018-06-27 NUMBER OF SEQ ID NOS: 8 SEQ ID NO 2 LENGTH: 998 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: Description of Artificial Sequence: Synthetic polypeptide Query Match 50.9%; Score 2448; Length 998; Best Local Similarity 55.4%; Matches 500; Conservative 134; Mismatches 230; Indels 38; Gaps 15; Qy 19 ILGVAPLSHPTIVEAREELKMPNGLEQSIADVEAKIDALTYLSKNSKDEFKHSMYEIPSN 78 :: : | ::: : | | | |: | | |||| |||:||| ||| : :: Db 1 MVAILAAQHDSLIRVKAEDK----LVQTSPSVSA-IDALHYLSENSKKEFKEELSKV--- 52 Qy 79 REHKPVSPKQALQNAKKADAQAERLAKMTIPKKEELKALEGPLYGGYFRTWQDKTSDPTE 138 : :| |: : |::|| ||: ||:| :|:| :| |:||||||||||| |||||| | Db 53 EKAQPEKLKEIVSKAQQADKQAKTLAEMKVPEKIPMKPLKGPLYGGYFRTWHDKTSDPAE 112 Qy 139 TNKVNSFGELPKEVDLAFVFHDYTKDYSLFWEELATKQVPKLNKQGTRVIRTIPWRFLSG 198 :|||| |||||||||||||||:||||||||:||||| || |||||||||||||||||:| Db 113 KDKVNSMGELPKEVDLAFVFHDWTKDYSLFWQELATKHVPTLNKQGTRVIRTIPWRFLAG 172 Qy 199 ADHSDISADKEKFPNTEAGNKALAKAIVDEYVYKYNLDGLDIDIERDSVPKVNDKEDPEA 258 ||| |: | :|:||| |||||||||||||||||||||||: |||||:|||| :| | Db 173 GDHSGIAEDAQKYPNTPEGNKALAKAIVDEYVYKYNLDGLDVMIERDSIPKVNKEESKEG 232 Qy 259 LARTVEVFKEIGKLIGANGADKSRLLIMDTTYTAEENPLIKETAQYLNLLLVQVYGFSGE 318 : |:::||:||||||| ||||||| |||:|| |::||||: | |::|||||||| || Db 233 IERSIQVFEEIGKLIGPKGADKSRLFIMDSTYMADKNPLIERGAPYIDLLLVQVYGTQGE 292 Qy 319 NGNY--LHHKNILDETSSMEGRWQGYSKYIRPEQYMVGFSFYEEK-DFNNRWKDINEEDP 375 | : :|| : :|| ||: |||||||||||||||||||| : | | |:| || Db 293 KGGFDNANHKAV----DTMEERWESYSKYIRPEQYMVGFSFYEEKANSGNLWYDVNVEDD 348 Qy 376 SDPHIGEKIQGTRAERYAKWQPKTGGLKGGLFSYAIDRDGVAQPKQK-TEHPELDKIVKS 434 ::|:|| :|:||||||||||||||||:|||:||| ||||||| ||: : |:||||||| Db 349 TNPNIGSEIKGTRAERYAKWQPKTGGVKGGIFSYGIDRDGVAHPKKNGPKTPDLDKIVKS 408 Qy 435 EYKVSKALKKLMMTDDQYQPIDQSDFPDKALRESIIKQVGTRRGDLERFKGTLRLDNPEI 494 :|||||||||:| | |: ||| |||||||||::| |||:|||:|||| ||||||||:| Db 409 DYKVSKALKKVMENDKSYELIDQKDFPDKALREAVIAQVGSRRGNLERFNGTLRLDNPDI 468 Qy 495 KDLTGLNKLKRVAKLELINLPKITKIDKDDLPQNLKPLTDNQKSNLEIKGTYDDSKLYKD 554 | | ||||||::|||||| | :|||:| ||:|:|| | | || | : | Db 469 KSLEGLNKLKKLAKLELIGLSQITKLDSSVLPENIKPTKDTLVSVLETYKNDDRKEEAKA 528 Qy 555 IPAFDLVISGLSGLESLDISGHQRDTLSGIDASTLPSLKAINISDNHFDLAQGTENRHIL 614 || | ||||:||: |:::| ||:|:||||::| ||: :::| | ||| ||||| || Db 529 IPQVALTISGLTGLKELNLAGFDRDSLAGIDAASLTSLEKVDLSSNKLDLAAGTENRQIL 588 Qy 615 DTILATLAKNGA---STASFDKQKPKGLYPESYSTAPLHLQVGQGKINVIDDLIFGTRTN 671 ||:|||: |:| | || ||| ||||::| | | | | |:: |:||| || Db 589 DTMLATVTKHGGVSEKTFVFDHQKPTGLYPDTYGTKSLQLPVANDTIDLQAKLLFGTVTN 648 Qy 672 QNTLINTENDFEAYKEQTIQGKPFIAPDYLYDNFKVSYKEYSASIVDSTLAETTDKTIDT 731 | ||||:| |::||:|| | | |: | | | |:||:| : |||| | | : | Db 649 QGTLINSEADYKAYQEQEIAGHRFVDSSYDYKAFAVTYKDYKIKVTDSTLGVTDHKDLST 708 Qy 732 AKAETYQVTVSN--KDGKTVHSVKVIVGDEKPMMVNLAQDAKIIGTD-NMTQSAKVFDG- 787 :| |||:| : | || |::||:|| ||||||: | ||| | : | : ||||| Db 709 SKEETYKVEFFSPINSTKPVHEAKIVVGEEKTMMVNLAEGATIIGGDADPTNAKKVFDGL 768 Qy 788 -QKDQFLLSWNKDSSVIFELKTPGTAKHWRFFDDGKND------SVTLSVFKG---DASN 837 | || : :|:||||| || ||||||:| | | | | |:| Db 769 LNNDTTTLSTSNKASIIFELKEPGLVKHWRFFNDSKISKADYIKEAKLEAFVGHLEDSSK 828 Qy 838 FETEKDKAENWVEITKDSRKNDDKVFSSPLEVDNAKYLKVTI---KKEAKYIYFNELQIL 894 : :|: || :: | : : || || ||| ::|| | : |: ||||: Db 829 VKDSLEKSTEWVTVSDYS--GEAQEFSQPLNNIGAKYWRITIDNKKSQYGYVSLPELQII 886 Qy 895 GY 896 |: Db 887 GH 888 Sequence alignment between the polypeptide of SEQ ID NO:2 of the instant application (“Qy”) and the endo-beta-N-acetylglucosaminidase of SEQ ID NO:5 of Kawaguchi (“Db”) US-15-745-357A-5 Sequence 5, US/15745357A Patent No. 11001819 GENERAL INFORMATION APPLICANT: Daiichi Sankyo Company, Limited TITLE OF INVENTION: NOVEL ENDOS MUTANT ENZYME FILE REFERENCE: DAISAN-1-65131 CURRENT APPLICATION NUMBER: US/15/745,357A CURRENT FILING DATE: 2018-01-16 PRIOR APPLICATION NUMBER: JP2015-141901 PRIOR FILING DATE: 2015-07-16 PRIOR APPLICATION NUMBER: PCT/JP2016/070921 PRIOR FILING DATE: 2016-07-15 NUMBER OF SEQ ID NOS: 9 SEQ ID NO 5 LENGTH: 995 TYPE: PRT ORGANISM: Artificial sequence FEATURE: OTHER INFORMATION: Synthetic FEATURE: NAME/KEY: MISC_FEATURE LOCATION: (1)..(995) OTHER INFORMATION: D233Q mutant of Endo-S Query Match 49.5%; Score 2381; Length 995; Best Local Similarity 52.1%; Matches 509; Conservative 136; Mismatches 262; Indels 70; Gaps 24; Qy 1 MNKRLLVKRTFGCVCAAAILGVAPLSH----PTIVEAREELKMPNGLEQSIADVEAKIDA 56 |:| |||||| |||||| ::| | :| |: : ::: || ||: Db 1 MDKHLLVKRTLGCVCAATLMGAALATHHDSLNTVKAEEKTVQVQKGL--------PSIDS 52 Qy 57 LTYLSKNSKDEFKHSMYEIPSNREHKPVSPKQALQNAKKADAQAERLAKMTIPKKEELKA 116 | |||:||| ||| : : : :| : | |: | |::|| ||: |||| ||:| :| Db 53 LHYLSENSKKEFKEELSK--AGQESQKV--KEILAKAQQADKQAQELAKMKIPEKIPMKP 108 Qy 117 LEGPLYGGYFRTWQDKTSDPTETNKVNSFGELPKEVDLAFVFHDYTKDYSLFWEELATKQ 176 | ||||||||||| |||||||| :|||| |||||||||||:|||:||||||||:||||| Db 109 LHGPLYGGYFRTWHDKTSDPTEKDKVNSMGELPKEVDLAFIFHDWTKDYSLFWKELATKH 168 Qy 177 VPKLNKQGTRVIRTIPWRFLSGADHSDISADKEKFPNTEAGNKALAKAIVDEYVYKYNLD 236 ||||||||||||||||||||:| |:| |: | |:||| |||||||||||||||||||| Db 169 VPKLNKQGTRVIRTIPWRFLAGGDNSGIAEDTSKYPNTPEGNKALAKAIVDEYVYKYNLD 228 Qy 237 GLDIDIERDSVPKVNDKEDPEALARTVEVFKEIGKLIGANGADKSRLLIMDTTYTAEENP 296 |||: :| ||:|||: ||| : |:::||:||||||| | ||||| |||:|| |::|| Db 229 GLDVQVEHDSIPKVDKKEDTAGVERSIQVFEEIGKLIGPKGVDKSRLFIMDSTYMADKNP 288 Qy 297 LIKETAQYLNLLLVQVYGFSGENGNYLHHKNILDETSSMEGRWQGYSKYIRPEQYMVGFS 356 ||: | |:||||| ||| || | : | ::| || |||||||||||||||:||| Db 289 LIERGAPYINLLLVLVYGSQGEKGGWEPVSNRPEKT--MEERWQGYSKYIRPEQYMIGFS 346 Qy 357 FYEEK-DFNNRWKDINEEDPSDP--HIGEKIQGTRAERYAKWQPKTGGLKGGLFSYAIDR 413 |||: | | ||| | | | ||||||||:|||||||:|||:||||||| Db 347 FYEQNAQEGNLWYDINSRKDEDKANGINTDITGTRAERYARWQPKTGGVKGGIFSYAIDR 406 Qy 414 DGVA-QPKQKTEHPEL----DKIVKSEYKVSKALKKLMMTDDQYQPIDQSDFPDKALRES 468 |||| |||: : | | | |:| |||||| :|: | | ||: |||||||||: Db 407 DGVAHQPKKYAKQKEFKDATDNIFHSDYSVSKALKTVMLKDKSYDLIDEKDFPDKALREA 466 Qy 469 IIKQVGTRRGDLERFKGTLRLDNPEIKDLTGLNKLKRVAKLELINLPKITKIDKDDLPQN 528 :: |||||:|||||| |||||||| |: | |||| |::|:|:|| | :|||:|: || | Db 467 VMAQVGTRKGDLERFNGTLRLDNPAIQSLEGLNKFKKLAQLDLIGLSRITKLDRSVLPAN 526 Qy 529 LKPLTDNQKSNLEIKGTY--DDSKLYKDIPAFDLVISGLSGLESLDISGHQRDTLSGIDA 586 :|| | :: || || |: : || | :|||:||: ||:|| |:||:|:|| Db 527 MKPGKDTLETVLE---TYKKDNKEEPATIPPVSLKVSGLTGLKELDLSGFDRETLAGLDA 583 Qy 587 STLPSLKAINISDNHFDLAQGTENRHILDTILATLAKNGAS---TASFDKQKPKGLYPES 643 :|| ||: ::|| | ||| ||||| | ||:|:|:: : | | |||||| | ||:: Db 584 ATLTSLEKVDISGNKLDLAPGTENRQIFDTMLSTISNHVGSNEQTVKFDKQKPTGHYPDT 643 Qy 644 YSTAPLHLQVGQGKINVIDDLIFGTRTNQNTLINTENDFEAYKEQTIQGKPFIAPDYLYD 703 | | | | |::: |:||| ||| ||||:| |::||: | |: |: :| |: Db 644 YGKTSLRLPVANEKVDLQSQLLFGTVTNQGTLINSEADYKAYQNHKIAGRSFVDSNYHYN 703 Qy 704 NFKVSYKEYSASIVDSTLAETTDKTIDTAKAETYQVTVSNKDGKT--VHSVKVIVGDEKP 761 ||||||: |: : |||| |||||: | | |||:| : || ||: |||||||| Db 704 NFKVSYENYTVKVTDSTLGTTTDKTLATDKEETYKVDFFSPADKTKAVHTAKVIVGDEKT 763 Qy 762 MMVNLAQDAKII-GTDNMTQSAKVFDGQ----KDQFLLSWNKDSSVIFELKTPGTAKHWR 816 ||||||: | :| |: : : |||||| | | |: |:||:|| | |||| Db 764 MMVNLAEGATVIGGSADPVNARKVFDGQLGSETDNISLGWDSKQSIIFKLKEDGLIKHWR 823 Qy 817 FFDD-GKNDSVT--------LSVFKGDASNFE------TEKDKAENWVEI-TKDSRKNDD 860 ||:| :| | | :| | : : | : |: : | :: Db 824 FFNDSARNPETTNKPIQEASLQIFNIKDYNLDNLLENPNKFDDEKYWITVDTYSAQGERA 883 Qy 861 KVFSSPLEVDNAKYLKVTI-KKEAKYI--YFNELQILGYPGVVAKKTADDLRPT-----E 912 ||: | :|| :| | :| |||||||| || : | | Db 884 TAFSNTLNNITSKYWRVVFDTKGDRYSSPVVPELQILGYP----LPNADTIMKTVTTAKE 939 Qy 913 ADKSDDK-SDKNDTEAK 928 : || | | | | Db 940 LSQQKDKFSQKMLDELK 956 Sequence alignment between the polypeptide of SEQ ID NO:2 of the instant application (“Qy”) and the endo-beta-N-acetylglucosaminidase of SEQ ID NO:2 of Kawaguchi (“Db”) Title: US-18-024-258A-2 Perfect score: 4809 Sequence: 1 MNKRLLVKRTFGCVCAAAIL..........RPTEADKSDDKSDKNDTEAK 928 Scoring table: BLOSUM62 Gapop 10.0 , Gapext 0.5 Searched: 1 seqs, 995 residues Total number of hits satisfying chosen parameters: 1 Minimum DB seq length: 0 Maximum DB seq length: inf Post-processing: Minimum Match 0% Maximum Match 100% Listing first 1 summaries Database : AASEQ2_08262025_111711.pep:* SUMMARIES % Result Query No. Score Match Length DB ID Description ---------------------------------------------------------------------------- 1 2313 48.1 995 1 AASEQ2_08262025_111711 ALIGNMENTS RESULT 1 AASEQ2_08262025_111711 Query Match 48.1%; Score 2313; DB 1; Length 995; Best Local Similarity 51.2%; Matches 500; Conservative 135; Mismatches 272; Indels 70; Gaps 24; Qy 1 MNKRLLVKRTFGCVCAAAILGVAPLSH----PTIVEAREELKMPNGLEQSIADVEAKIDA 56 |:| |||||| |||||| ::| | :| |: : ::: || ||: Db 1 MDKHLLVKRTLGCVCAATLMGAALATHHDSLNTVKAEEKTVQVQKGL--------PSIDS 52 Qy 57 LTYLSKNSKDEFKHSMYEIPSNREHKPVSPKQALQNAKKADAQAERLAKMTIPKKEELKA 116 | |||:||| ||| : : : :| : | |: | |::|| ||: |||| ||:| :| Db 53 LHYLSENSKKEFKEELSK--AGQESQKV--KEILAKAQQADKQAQELAKMKIPEKIPMKP 108 Qy 117 LEGPLYGGYFRTWQDKTSDPTETNKVNSFGELPKEVDLAFVFHDYTKDYSLFWEELATKQ 176 | ||||||||||| |||||||| :|||| |||||||||||:|||:||||||||:||||| Db 109 LHGPLYGGYFRTWXDKTSDPTEKDKVNSMGELPKEVDLAFIFHDWTKDYSLFWKELATKH 168 Qy 177 VPKLNKQGTRVIRTIPWRFLSGADHSDISADKEKFPNTEAGNKALAKAIVDEYVYKYNLD 236 ||||||||||||||| || |:| |:| |: | |:||| |||||||||||||||||||| Db 169 VPKLNKQGTRVIRTIXWRXLAGGDNSGIAEDTSKYPNTPEGNKALAKAIVDEYVYKYNLD 228 Qy 237 GLDIDIERDSVPKVNDKEDPEALARTVEVFKEIGKLIGANGADKSRLLIMDTTYTAEENP 296 |||: :| ||:|||: ||| : |:::||:||||||| | ||||| || : |::|| Db 229 GLDVQVEHDSIPKVDKKEDTAGVERSIQVFEEIGKLIGPKGVDKSRLFIMXSXXMADKNP 288 Qy 297 LIKETAQYLNLLLVQVYGFSGENGNYLHHKNILDETSSMEGRWQGYSKYIRPEQYMVGFS 356 ||: | |:||||| ||| || | : | ::| || |||||||||||||||:||| Db 289 LIERGAPYINLLLVXVYGSQGEKGGWEPVSNRPEKT--MEERWQGYSKYIRPEQYMIGFS 346 Qy 357 FYE-EKDFNNRWKDINEEDPSDP--HIGEKIQGTRAERYAKWQPKTGGLKGGLFSYAIDR 413 | | | | ||| | | | ||||||||:|||||||:|||:|| || Db 347 FXEXNAQEGNLWYDINSRKDEDKANGINTDITGTRAERYARWQPKTGGVKGGIFSXAIXX 406 Qy 414 DGVA-QPKQKTEHPEL----DKIVKSEYKVSKALKKLMMTDDQYQPIDQSDFPDKALRES 468 |||| |||: : | | | |:| |||||| :|: | | ||: |||||||||: Db 407 DGVAHQPKKYAKQKEFKDATDNIFHSDYSVSKALKTVMLKDKSYDLIDEKDFPDKALREA 466 Qy 469 IIKQVGTRRGDLERFKGTLRLDNPEIKDLTGLNKLKRVAKLELINLPKITKIDKDDLPQN 528 :: |||||:|||||| |||||||| |: | |||| |::|:|:|| | :|||:|: || | Db 467 VMAQVGTRKGDLERFNGTLRLDNPAIQSLEGLNKFKKLAQLDLIGLSRITKLDRSVLPAN 526 Qy 529 LKPLTDNQKSNLEIKGTY--DDSKLYKDIPAFDLVISGLSGLESLDISGHQRDTLSGIDA 586 :|| | :: || || |: : || | :|||:||: ||:|| |:||:|:|| Db 527 MKPGKDTLETVLE---TYKKDNKEEPATIPPVSLKVSGLTGLKELDLSGFDRETLAGLDA 583 Qy 587 STLPSLKAINISDNHFDLAQGTENRHILDTILATLAKNGAS---TASFDKQKPKGLYPES 643 :|| ||: ::|| | ||| ||||| | ||:|:|:: : | | |||||| | ||:: Db 584 ATLTSLEKVDISGNKLDLAPGTENRQIFDTMLSTISNHVGSNEQTVKFDKQKPTGHYPDT 643 Qy 644 YSTAPLHLQVGQGKINVIDDLIFGTRTNQNTLINTENDFEAYKEQTIQGKPFIAPDYLYD 703 | | | | |::: |:||| ||| ||||:| |::||: | |: |: :| |: Db 644 YGKTSLRLPVANEKVDLQSQLLFGTVTNQGTLINSEADYKAYQNHKIAGRSFVDSNYHYN 703 Qy 704 NFKVSYKEYSASIVDSTLAETTDKTIDTAKAETYQVTVSNKDGKT--VHSVKVIVGDEKP 761 ||||||: |: : |||| |||||: | | |||:| : || ||: |||||||| Db 704 NFKVSYENYTVKVTDSTLGTTTDKTLATDKEETYKVDFFSPADKTKAVHTAKVIVGDEKT 763 Qy 762 MMVNLAQDAKII-GTDNMTQSAKVFDGQ----KDQFLLSWNKDSSVIFELKTPGTAKHWR 816 ||||||: | :| |: : : |||||| | | |: |:||:|| | |||| Db 764 MMVNLAEGATVIGGSADPVNARKVFDGQLGSETDNISLGWDSKQSIIFKLKEDGLIKHWR 823 Qy 817 FFDD-GKNDSVT--------LSVFKGDASNFE------TEKDKAENWVEI-TKDSRKNDD 860 ||:| :| | | :| | : : | : |: : | :: Db 824 FFNDSARNPETTNKPIQEASLQIFNIKDYNLDNLLENPNKFDDEKYWITVDTYSAQGERA 883 Qy 861 KVFSSPLEVDNAKYLKVTI-KKEAKYI--YFNELQILGYPGVVAKKTADDLRPT-----E 912 ||: | :|| :| | :| |||||||| || : | | Db 884 TAFSNTLNNITSKYWRVVFDTKGDRYSSPVVPELQILGYP----LPNADTIMKTVTTAKE 939 Qy 913 ADKSDDK-SDKNDTEAK 928 : || | | | | Db 940 LSQQKDKFSQKMLDELK 956
Read full office action

Prosecution Timeline

Mar 01, 2023
Application Filed
Aug 27, 2025
Non-Final Rejection — §101, §102, §103
Nov 26, 2025
Response Filed
Feb 26, 2026
Final Rejection — §101, §102, §103
Apr 09, 2026
Response after Non-Final Action
Apr 09, 2026
Request for Continued Examination
Apr 10, 2026
Response after Non-Final Action

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12595472
MANNANASE VARIANTS
2y 5m to grant Granted Apr 07, 2026
Patent 12590301
METHODS FOR SAFE AND EFFECTIVE THROMBOLYSIS USING SEQUENTIAL ADMINISTRATION OF TISSUE PLASMINOGEN ACTIVATOR AND MUTANT PRO-UROKINASE
2y 5m to grant Granted Mar 31, 2026
Patent 12570964
Bacterium And Obtaining Method And Application Thereof
2y 5m to grant Granted Mar 10, 2026
Patent 12559734
Reverse Transcriptase Mutants with Increased Activity and Thermostability
2y 5m to grant Granted Feb 24, 2026
Patent 12540160
METHODS FOR THE PURIFICATION OF REFOLDED FC-PEPTIDE FUSION PROTEIN
2y 5m to grant Granted Feb 03, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

AI Strategy Recommendation

Get an AI-powered prosecution strategy using examiner precedents, rejection analysis, and claim mapping.
Powered by AI — typically takes 5-10 seconds

Prosecution Projections

3-4
Expected OA Rounds
74%
Grant Probability
88%
With Interview (+14.0%)
2y 10m
Median Time to Grant
Moderate
PTA Risk
Based on 924 resolved cases by this examiner. Grant probability derived from career allow rate.

Sign in for Full Analysis

Enter your email to receive a magic link. No password needed.

Free tier: 3 strategy analyses per month