Prosecution Insights
Last updated: July 17, 2026
Application No. 18/036,580

USE OF THERAPEUTIC ENZYME FUSION PROTEIN IN PREVENTION AND TREATMENT OF RENAL DISEASES CAUSED BY OR ACCOMPANIED BY FABRY DISEASE

Final Rejection §101§102§103
Filed
May 11, 2023
Priority
Nov 13, 2020 — RE 10-2020-0152247 +1 more
Examiner
JONES-FOSTER, ERICA NICOLE
Art Unit
1656
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Hanmi Pharm. Co., Ltd.
OA Round
2 (Final)
49%
Grant Probability
Moderate
3-4
OA Rounds
2m
Est. Remaining
96%
With Interview

Examiner Intelligence

Grants 49% of resolved cases
49%
Career Allowance Rate
37 granted / 75 resolved
-10.7% vs TC avg
Strong +47% interview lift
Without
With
+46.8%
Interview Lift
resolved cases with interview
Typical timeline
3y 4m
Avg Prosecution
50 currently pending
Career history
149
Total Applications
across all art units

Statute-Specific Performance

§101
7.4%
-32.6% vs TC avg
§103
60.7%
+20.7% vs TC avg
§102
10.3%
-29.7% vs TC avg
§112
4.6%
-35.4% vs TC avg
Black line = Tech Center average estimate • Based on career data from 75 resolved cases

Office Action

§101 §102 §103
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 . Support for the amendments is within the instant application specification. Applicant’s amendment to the claims filed on 4/16/2026 in response to the Non-Final Rejection mailed on 1/16/2026 is acknowledged. This listing of claims replaces all prior listings of claims in the application. Claims 1-6, 8-19 are pending. Claims 19 is newly added. Claims 7 is cancelled. Applicant’s remarks filed on 4/16/2026 in response to the Non-Final Rejection mailed on 1/16/2026 have been fully considered and are deemed persuasive to overcome at least one of the rejections and/or objections as previously applied. The text of those sections of Title 35 U.S. Code not included in the instant action can be found in the prior Office Action. Priority Acknowledgement is made of this national stage entry of PCT/KR2021/016630 of Non-provisional Application No. 18/036,580, filed on 11/15/2021, which claims foreign priority under 35 U.S.C. 119(a)-(d) to Korean Patent Application No. KR10-2020-0152247 filing date 11/13/2020. The certified copy has been filed in the present application on 5/11/2023. It is noted, that applicant has filed a certified copy of the English translation as required by 37 CFR 1.55 dated 4/16/2026. Withdrawn Rejections The rejection of claims 5-8 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in view of Applicant’s amendment of claim 5 to recite ‘the amino acid sequence of SEQ ID NO: 8’; amendment of claim 6 to incorporate the specific linker sequences ([GS]x, [GGGS]x, and [GGGGS]x) from claim 7; cancellation of claim 7. The scope of enablement rejection of claim 5 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph is withdrawn in view of Applicant’s amendment of claim 5 to recite ‘the amino acid sequence of SEQ ID NO: 8.’ The rejection of claims 1-18 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ) is withdrawn in view of Applicant’s amendment of claim 1 to recite ‘each independently a peptide linker’; amendment of claim 5 to recite ‘the amino acid sequence of SEQ ID NO: 8’; amendment of claims 11, 13 to recite ‘the individual to which the pharmaceutical composition is administered’ and ‘each compared to a corresponding untreated individual,’ amendment of claim 14 to recite ‘the alpha-galactosidase’; cancellation of claim 7. The rejection of claim 7 under 35 U.S.C. 102(a)(2) as being anticipated by Jung et al (US 2021/0009984 A1, Date Filed: Dec. 21, 2018, cited on PTO-892 dated 1/22/2026, recently (9-24-25) issued as US 12435328) {herein Jung} as evidenced by Politei et al (2016, CNS Neuroscience & Therapeutics, cited on PTO-892 dated 1/22/2026) {herein Politei} is withdrawn in view of Applicant’s cancellation of claim 7. The provisional nonstatutory double patenting rejection of claim 7 under 35 U.S.C. 101 as claiming the same invention as that of claims 1-15 of prior U.S. Patent Application No. 18/036,538 is withdrawn in view of Applicant’s cancellation of claim 7. 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)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention. The rejection of claims 1-6, 8-15, 17-19 under 35 U.S.C. 102(a)(2) as being anticipated by Jung et al (US 2021/0009984 A1, Date Filed: Dec. 21, 2018, cited on PTO-892 dated 1/16/2026, recently (9-24-25) issued as US 12435328) {herein Jung} as evidenced by Torra et al (2008, International Society of Nephrology, cited on PTO-892 dated 1/16/2026) {herein Torra) and Antonowicz et al (1972, Pediat. Res, cited on PTO-892 dated 1/16/2026) {herein Antonowicz} is maintained. The rejection has been modified in view of Applicant’s amendment of claim 1 to recite ‘a method for preventing or treating renal diseases caused by renal inflammation or renal fibrosis,’ cancellation of claim 7 and new claim 19. See MPEP 2131.01 regarding multiple reference 102 rejections. Claims 1-6, 8-15, 17-19 are drawn to a method for preventing or treating renal diseases caused by renal inflammation or renal fibrosis, comprising administering a pharmaceutical composition to a patient in need thereof, wherein the pharmaceutical composition comprises an enzyme fusion protein represented by the following Chemical Formula 1: [Chemical Formula 1] wherein X and X' are each alpha-galactosidase; L and L' are each independently, a peptide linker; F is one polypeptide chain of an immunoglobulin Fc region; is a covalent bond; and : is a covalent or non-covalent bond. With respect to claims 1-6, 8-9, 12, 15, 17, 18, Jung teaches a method for treating Fabry’s disease utilizing a pharmaceutical composition (para 0010, para 0155, para 0056). Evidentiary reference of Torra is cited to demonstrate that Fabry’s disease causes kidney fibrosis and impairment (abstract; page S31, column 1, para 1) which is a type of kidney disease that is known by those of ordinary skill in the art to be accompanied by inflammation. It is noted that Examiner is interpreting ‘kidney’ and ‘renal’ to be synonymous as the only difference is that ‘kidney’ is a noun and ‘renal’ is an adjective. Jung further teaches a method wherein the pharmaceutical composition comprises an enzyme fusion protein of Formula I (para 0010 and para 0155). The pharmaceutical composition of the fusion protein X and X' are each independently the same or a different kind of therapeutic enzyme; L and L' are linkers, each independently the same kind of linker; F is an immunoglobulin Fc region; I is a covalent bond; and is a covalent or non-covalent bond (para 0010-0016). The enzyme may be selected from alpha-galactosidase (para 0031) for the production of an enzyme fusion protein including a therapeutic enzyme in the form of an antiparallel dimer (para 0200). Said fusion protein comprises a monomer that is 100% identical to the instant application SEQ ID NO: 13 (appendix A). The immunoglobulin Fc region may be aglycosylated (para 0050). The Fc region may comprise a hinge region of which may by one having a variation where a part of the hinge region is deleted (para 0119). Said hinge region is comprised of Glu-Ser-Lys-Tyr-Gly-Pro-Pro-Cys-Pro-Ser-Cys-Pro (para 0118). Absent evidence otherwise, it is the Examiner’s position that Glu-Ser-Lys-Tyr-Gly-Pro-Pro-Cys-Pro-Ser-Cys-Pro teaches the limitation of claim 4 of the instant application SEQ ID NO: 31 as the instant application SEQ ID NO: 31 is Pro-Pro-Cys-Pro, of which Glu-Ser-Lys-tyr-Gly-Pro-Pro-Cys-Pro-Ser-Cys-Pro comprises. As such, the instant application SEQ ID NO: 31 is the same as the hinge region taught by Jung since Jung teaches a part of the hinge region is deleted of which is the Examiner’s position would result in the following hinge region: Pro-Pro-Cys-Pro, which is 100% identical to the instant application SEQ ID NO: 31. Furthermore, the immunoglobulin Fc region having the amino sequence of SEQ ID NO: 8, the 2nd amino acid is substituted with proline; the 71st amino acid is substituted with glutamine; or the 2nd amino acid is substituted with proline and the 71st amino acid is substituted with glutamine (Jung: claim 33). SEQ ID NO: 8 taught by Jung is 100% identical to the instant Application SEQ ID NO: 8 (appendix B). Additionally, the linker may include at least one amino acid, specifically 10 to 50 amino acids (para 0108) of which encompasses the claimed range 1 to 100 amino acids in the instant application claim 6. The peptide linker consist of an amino acid sequence: [GS] linker, [GGGS]x linker, and [GGGGS]x linker, etc., in which x is a natural x number of 1 or greater (e.g., 1, 2, 3, 4, 5, or greater) (para 0108) and may consist of the amino acid sequence of SEQ ID NO: 11 (para 0108), of which is 100% identical to the instant application SEQ ID NO: 11 (appendix C). Jung further teaches that the frequency of administration of the pharmaceutical formulation containing the enzyme fusion protein can be significantly reduced (para 0159). With respect to claim 10, Jung teaches a pharmaceutical composition for the treatment of lysosomal disorders (para 0003, 0009-0016). Evidentiary reference of Antonowicz is cited to demonstrate that cystic fibrosis is a lysosomal disorder (abstract). As such, it is the Examiner position that the teaching of the treatment of lysosomal disorders by Jung includes cystic fibrosis. With respect to claim 11, Jung teaches alpha-Galactosidase A is an enzyme that hydrolyzes globotriaosylceramide (Gb3) into lactosylceramide, and it is known that a disorder in alpha-galactosidase A leads to abnormal accumulation of Gb3 in the walls of blood vessels and various parts of the body, thereby causing Fabry's disease to occur (para 0005). Since the art teaches the structure of a pharmaceutical composition for treating renal diseases caused by or accompanied by Fabry disease, it is the Examiner’s position said pharmaceutical composition’s administration would necessarily inherently lead to one or more of the following characteristics in the individual: (i) a reduced level of lyso-Gb3 or Gb3 in kidney tissue; (ii) a reduced level of TIMP-1 (tissue inhibitor of metalloproteinase-1) in kidney tissue; (iii) a reduced level of collagen typel alpha-1 in kidney tissue; (iv) a reduced level of a-SMA (alpha-smooth muscle actin) in kidney tissue; and (v) a reduced level of soluble collagen and insoluble collagen in kidney tissue as Jung teaches the same pharmaceutical composition as the instant application (para 0010-0016). With respect to claim 13, since the art teaches the structure of a pharmaceutical composition for treating renal diseases caused by or accompanied by Fabry disease, it is the Examiner’s position that the administration of said pharmaceutical composition would necessarily and inherently lead to one or more of the following characteristics in an individual to which the pharmaceutical composition is administered: (i) a reduced level of TNF-a in the kidney tissue; (ii) a reduced level of IL-6 in the kidney tissue; (iii) a reduced level of RANTES in the kidney tissue; and (iv) a reduced level of TNFR1 in the blood as Jung teaches the same pharmaceutical composition as the instant application (para 0010-0016). With respect to claim 14, since the art teaches the structure of a pharmaceutical composition for treating renal diseases caused by or accompanied by Fabry disease, it is the Examiner’s position that the tissue targetability of the enzyme fusion protein for the kidney would necessarily be greater than that of an enzyme alone as Jung teaches the same fusion protein as the instant application (para 0010). With respect to claim 19, Jung teaches a method for treating Fabry’s disease utilizing a pharmaceutical composition (para 0010, para 0155, para 0056). Kidney disease is a major complication of Fabry’s disease. As such, it is the Examiner’s position that renal disease is accompanied by Fabry’s disease. RESPONSE TO REMARKS: Beginning on p. 10 of Applicant’s remarks, Applicants in summary contend that Jung, Torra, and Antonowitz, individually or in combination, do not disclose the therapeutic effects of the enzyme fusion protein of present claim 1 on "renal inflammation and renal fibrosis.” Jung is directed to the therapeutic effect of the fusion protein on Fabry disease. In Jung, it was merely confirmed that the enzyme activity of the fusion protein is increased and the intracellular uptake activity is not lost. Nowhere does Jung disclose a direct therapeutic effect of the fusion protein of the present claims on "renal diseases." Additionally, in summary, Applicant contends that Torra and Antonowitz do not teach or disclosed a method for preventing or treating renal diseases caused by renal inflammation and renal fibrosis This argument is found to be not persuasive. Examiner contends that Jung teaches a method for treating Fabry’s disease utilizing a pharmaceutical composition (para 0010, para 0155, para 0056). Examiner contends that Torra and Antonowitz are evidentiary references. Examiner contends that Torra demonstrates that Fabry’s disease causes kidney fibrosis and impairment (abstract; page S31, column 1, para 1) which is a type of kidney disease that is known by those of ordinary skill in the art to be accompanied by inflammation. Examiner contends that Antonowicz demonstrates that cystic fibrosis is a lysosomal disorder (abstract). Therefore, the teachings of Torra and Antonowitz beyond what is disclosed as evidentiary, is not pertinent to the instant application office action. Applicant is reminded that claim 1 recites ‘renal inflammation or renal fibrosis’ of which only one need to be taught. Maintained Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The rejection of claim 16 under 35 U.S.C. 103 as being unpatentable over Jung et al (US 2021/0009984 A1, Date Filed: Dec. 21, 2018, cited on PTO-892 dated 1/16/2026, recently (9-24-25) issued as US 12435328) {herein Jung} as evidenced by Torra et al (2008, International Society of Nephrology, cited on PTO-892 dated 1/16/2026) {herein Torra) and Antonowicz et al (1972, Pediat. Res, cited on PTO-892 dated 1/16/2026) {herein Antonowicz} is maintained. Claim 16 is drawn to the method of claim 1, wherein the pharmaceutical composition is administered to an individual once every two weeks or once a month. The teachings of Jung as applied to claims 1-6, 8-15, 17-19 are set forth in the 102a2 rejection above. With respect to claim 16, Jung teaches the pharmaceutical composition is administered to patients (para 0008). Jung further teaches that the frequency of administration of the pharmaceutical formulation containing the enzyme fusion protein can be significantly reduced (para 0159). Although the reference of Jung does not explicitly teach the limitations of claim 16, MPEP 2144.05 states"[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or frequency at which to administer the [pharmaceutical composition to an individual by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP 2144.05 IIA)." One of ordinary skill would desire to optimize the frequency upon which the pharmaceutical composition is given to subjects depending on the particular application. It would be routine for one to arrive at the frequency for the application they intend on using the pharmaceutical composition. Therefore, the above invention would have been prima facie obvious. However, Jung does not teach the method of claim 16, wherein the pharmaceutical composition is administered to an individual once every two weeks or once a month (claim 16). Before the effective filing date of the claimed invention, it would have been obvious to one of ordinary skill in the art to modify the frequency upon which the pharmaceutical composition is administered to a patient to once every two weeks or once a month. Especially when Junga teaches said composition is able to maximize pharmacological efficacy by increasing the blood stability of the therapeutic enzymes and maintaining their blood concentration at a high level for a longer period of time (para 0008). Jung further teaches that the frequency of administration of the pharmaceutical formulation containing the enzyme fusion protein can be significantly reduced (para 0159). One of ordinary skill in the art would have had a reasonable expectation of success, a reasonable level of predictability, and would be motivated to modify the frequency upon which the pharmaceutical composition is administered as Jung teaches frequent injections to maintain the blood concentration of active polypeptides may cause significant pain to the patient (para 0008). As such, reducing the frequency upon which the pharmaceutical composition is administered to the recited once every two weeks or once a month would reduce the pain of the patient while maintaining the therapeutic efficacy of the pharmaceutical composition. Therefore one of ordinary skill in the art would expect similar results if the pharmaceutical composition is injected once every two weeks or once a month. Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. RESPONSE TO REMARKS: Beginning on p. 10 of Applicant’s remarks, Applicant contends that the rejection has been addressed by amendment and is unobvious. In summary, Applicant contends that the amended claims are directed to a significant therapeutic effect of a composition, which comprises the enzyme fusion protein represented by Chemical Formula 1, on renal inflammation and renal fibrosis, as set forth in amended claim 1. However, Jung, Torra, and Antonowitz, individually or in combination, do not disclose or make obvious the therapeutic effects of the enzyme fusion protein of present claim 1 on "renal inflammation and renal fibrosis." This argument is found to be not persuasive. Examiner contends that Jung teaches the administration of a pharmaceutical composition to treat or prevent lysosomal storage diseases such as Favry diseases which causes renal inflammation. Jung further teaches that the frequency of administration of the pharmaceutical formulation containing the enzyme fusion protein can be significantly reduced (para 0159). MPEP 2144.05 states"[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or frequency at which to administer the [pharmaceutical composition to an individual by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955) (MPEP 2144.05 IIA)." One of ordinary skill would desire to optimize the frequency upon which the pharmaceutical composition is given to subjects depending on the particular application. It would be routine for one to arrive at the frequency for the application they intend on using the pharmaceutical composition. Therefore, the above invention would have been prima facie obvious. Maintained Double Patenting A rejection based on double patenting of the “same invention” type finds its support in the language of 35 U.S.C. 101 which states that “whoever invents or discovers any new and useful process... may obtain a patent therefor...” (Emphasis added). Thus, the term “same invention,” in this context, means an invention drawn to identical subject matter. See Miller v. Eagle Mfg. Co., 151 U.S. 186 (1894); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Ockert, 245 F.2d 467, 114 USPQ 330 (CCPA 1957). A statutory type (35 U.S.C. 101) double patenting rejection can be overcome by canceling or amending the claims that are directed to the same invention so they are no longer coextensive in scope. The filing of a terminal disclaimer cannot overcome a double patenting rejection based upon 35 U.S.C. 101. The provisional rejection of claims 1-6, 8-19 under 35 U.S.C. 101 as claiming the same invention as that of claims 1-15 of prior U.S. Patent Application No. 18/036,538 {herein 538} is maintained. The rejection has been modified in view of Applicant’s amendment of claim 1 to recite ‘renal inflammation or renal fibrosis’ and add new claim 19. Said applications have a common assignee of Hanmi Pharm. This is a statutory double patenting rejection. Independent claims 1, 7 of ‘538 are not patentably distinct from claims 1, 10-14, 19 of the instant application because claim 1 of ‘538 recites a method for preventing or treating neuropathy caused by or accompanied by Fabry disease, comprising administering a pharmaceutical composition to a patient in need thereof, wherein the pharmaceutical composition comprises an enzyme fusion protein represented by the following Chemical Formula 1: wherein X and X' are each alpha-galactosidase; L and L' are linkers, each independently the same or a different kind of linker; F is one polypeptide chain of an immunoglobulin Fc region; I is a covalent bond; and: is a covalent or non-covalent bond. Claim 1 of the copending application is drawn to the limitation “treating neuropathy caused by or accompanied by Fabry disease.” Said recitation renders the instant application claim 1 obvious as claim 19 of the instant application is drawn to the renal disease being accompanied by Fabry disease. Furthermore, the preamble of the claim does not carry any patentable weight as the steps of the method and the fused enzyme used in the method are identical and therefore any treatment method using said fused enzyme would inherently treat both conditions, of the instant application as well as that of the copending application. Therefore there would be a reasonable expectation of success to arrive at the above invention. Therefore, the above invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. Dependent claim 2 of ‘538 is not patentably distinct from claim 2 of the instant application because claim 2 of ‘538 recites the method of claim 1, wherein the enzyme is an anti-parallel dimer formed by X and X'. Dependent claim 3 of ‘538 is not patentably distinct from claim 3 of the instant application because claim 3 of ‘538 recites the method of claim 1, wherein the immunoglobulin Fc region is aglycosylated. Dependent claim 4 of ‘538 is not patentably distinct from claim 4 of the instant application because claim 4 of ‘538 recites the method of claim 1, wherein the immunoglobulin Fc region includes a hinge region having an amino acid sequence of SEQ ID NO: 15. Dependent claim 5 of ‘538 is not patentably distinct from claim 5 of the instant application because claim 5 of ‘538 recites the method of claim 1, wherein the immunoglobulin Fc region has a substitution of praline for an amino acid at position 2; a substitution of glutamine for an amino acid at position 71; or a substitution of praline for an amino acid at position 2 and a substitution of glutamine for an amino acid at position 71 in an amino acid sequence of SEQ ID NO: 8. Dependent claim 6 of ‘538 is not patentably distinct from claim 6 of the instant application because claim 6 of ‘538 recites the method of claim 1, wherein the linker is a peptide linker consisting of 1 amino acid to 100 amino acids. Dependent claim 7 of ‘538 is not patentably distinct from claim 7 of the instant application because claim 7 of ‘538 recites the method of claim 6, wherein the peptide linker consists of an amino acid sequence of [GS]x, [GGGS]x, or [GGGGS]x, wherein x is a natural number of 1 to 20. Dependent claim 8 of ‘538 is not patentably distinct from claim 8 of the instant application because claim 8 of ‘538 recites the method of claim 7, wherein the peptide linker has an amino acid sequence of SEQ ID NO: 11. Dependent claim 9 of ‘538 is not patentably distinct from claim 9 of the instant application because claim 9 of ‘538 recites the method of claim 1, wherein the neuropathy is polyneuropathy or small fiber neuropathy. Dependent claim 12 of ‘538 is not patentably distinct from claim 15 of the instant application because claim 12 of ‘538 recites the method of claim 1, wherein an administration frequency of the enzyme fusion protein is lesser than that of an enzyme alone. Dependent claim 13 of ‘538 is not patentably distinct from claim 16 of the instant application because claim 13 of ‘538 recites the method of claim 1, wherein the pharmaceutical composition is administered once every two weeks or once a month. Dependent claim 14 of ‘538 is not patentably distinct from claim 17 of the instant application because claim 14 of ‘538 recites the method of claim 1, wherein the enzyme fusion protein comprises a monomer including an amino acid sequence of SEQ ID NO: 13. Dependent claim 15 of ‘538 is not patentably distinct from claim 18 of the instant application because claim 15 of ‘538 recites the method of claim 1, wherein X and X' are enzymes, each including an amino acid sequence the same as or different from each other. Conclusion Status of Claims Claims 1-6, 8-19 are pending. Claims 1-6, 8-19 are rejected. No claims are in condition for allowance. 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 ERICA NICOLE JONES-FOSTER whose telephone number is (571)270-0360. The examiner can normally be reached mf 7:30a - 4:30p. 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, Manjunath Rao can be reached at 571-272-0939. 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. /ERICA NICOLE JONES-FOSTER/ Examiner, Art Unit 1656 /MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656 Appendix A Jung SEQ ID NO: 13 vs Instant Application SEQ ID NO: 13 Query Match 100.0%; Score 3707; Length 680; Best Local Similarity 100.0%; Matches 680; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP 60 Qy 61 DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL 120 Qy 121 ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL 180 Qy 181 ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK 240 Qy 241 SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL 300 Qy 301 RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG 360 Qy 361 GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT 420 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 361 GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT 420 Qy 421 MQMSLKDLLGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSPPCPAPEFLGGPSVFLFPPKP 480 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 421 MQMSLKDLLGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSPPCPAPEFLGGPSVFLFPPKP 480 Qy 481 KDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFQSTYRVVSVLT 540 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 481 KDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFQSTYRVVSVLT 540 Qy 541 VLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTC 600 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 541 VLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTC 600 Qy 601 LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSV 660 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 601 LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSV 660 Qy 661 MHEALHNHYTQKSLSLSLGK 680 |||||||||||||||||||| Db 661 MHEALHNHYTQKSLSLSLGK 680 Appendix B Jung SEQ ID NO: 8 vs Instant Application SEQ ID NO: 8 Query Match 100.0%; Score 1186; Length 222; Best Local Similarity 100.0%; Matches 221; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 PSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHN 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 2 PSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHN 61 Qy 61 AKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREP 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 62 AKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREP 121 Qy 121 QVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFL 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 122 QVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFL 181 Qy 181 YSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK 221 ||||||||||||||||||||||||||||||||||||||||| Db 182 YSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK 222 Appendix C Jung SEQ NO: 11 vs Instant Application SEQ ID NO: 11 Query Match 100.0%; Score 168; Length 30; Best Local Similarity 100.0%; Matches 30; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 GGGGSGGGGSGGGGSGGGGSGGGGSGGGGS 30 |||||||||||||||||||||||||||||| Db 1 GGGGSGGGGSGGGGSGGGGSGGGGSGGGGS 30
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Prosecution Timeline

May 11, 2023
Application Filed
Jan 16, 2026
Non-Final Rejection mailed — §101, §102, §103
Apr 16, 2026
Response Filed
Jun 29, 2026
Final Rejection mailed — §101, §102, §103 (current)

Precedent Cases

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

3-4
Expected OA Rounds
49%
Grant Probability
96%
With Interview (+46.8%)
3y 4m (~2m remaining)
Median Time to Grant
Moderate
PTA Risk
Based on 75 resolved cases by this examiner. Grant probability derived from career allowance rate.

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