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 Applicant's election with traverse of Group I, claims 1-7, 9, 13-14, and 25 in the reply filed on 3/3/2026 is acknowledged. The traversal is on the ground(s) that the prior art references of record dis not teach the amended claims . This is not found persuasive because new references teaching the amended claims have been found. Furthermore, this instant claims comprise both polypeptide and polynucleotide encoding the fusion protein. Polypeptides comprise amino acid residues and polynucleotides comprise purines and pyrimidines without a common core structure; thus, this instant application lacks unity of invention. The requirement is still deemed proper and is therefore made FINAL. In response to species election, applicant elected the fusion peptide of SEQ ID NO: 3 (SEQ ID NO: 2 is C-terminus to a heterologous polypeptide) , reading on claims 1-3, 7, 9, 13-14, and 25 . Claim s 16, 19, 22, 27, 29, 31-33, and 37 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention , there being no allowable generic or linking claim. Claims 4-6 are further withdrawn as the claims directed to non-elected species. Applicant timely traversed the restriction (election) requirement in the reply filed on 3/3/2026. Claim Status Claims 1-7, 9, 13-14, 16, 19, 22, 25, 27, 29, 31-33, and 37 are pending. Claims 8, 10-12, 15, 17-18, 20-21, 23-24, 26, 28, 30, 34-36, and 38 are cancelled. Claims 16, 19, 22, 27, 29, 31-33, and 37 are withdrawn as being directed to a non-elected invention and claims 4-6 are withdrawn as being directed to a non-elected species , the election having been made on 3/3/2026. Also polynucleotide of claim 25 is further withdrawn. Claims 1-3, 7, 9, 13-14, and 25 (only fusion peptide) have been examined. Priority This application is a 371 of PCT/CN2021/129378 filed on 11/08/2021 and claims foreign priority of PCTCN2020129067 filed on 11/16/2020 . Information Disclosure Statement The information disclosure statement (IDS) submitted on 10/28/2013 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered by the examiner. Claim Objections Claim s 1- 2 and 14 is objected to because of the following informalities: Claim 1 is objected to because the phrase “ a polypeptide comprising an amino a ci d sequence …” in line 1-2 should be revised to “ a polypeptide comprising the amino a ci d sequence …” Claim 2 is objected to because the phrase “the polypeptide” should be revised to “the polypeptide (1)”. Claim 14 is objected to because the phrase “ an amino acid sequence having at least 90% i dentity to SEQ ID NO: 3 ” should be revised to “the amino acid sequence having at least 90% i dentity to SEQ ID NO: 3 ” . 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 appl icant regards as his invention. Claims 2- 3 , 7, and 13 are 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 2 is unclear with respect to the fusion protein comprising polypeptide (1) and polypeptide (2). The metes and bounds are unclear because it is unclear with respect to the cut-off amino acid or sequence between polypeptides (1) and (2) . Claim 3 is unclear with respect to the word “ optionally ” because the word “optionally” has the same meaning as “preferred to ”. C laim 7 recites parenthetical expressions “(human or mouse)”. The metes and bounds of claim 7 is rendered vague and indefinite by the parenthetical recitation of “(human or mouse)” because it is unclear as to whether the limitation is part of the instantly claimed subject matter. With respect to claim 13, it is unclear with respect to “a functional fragment of MYDGY”. Neither the specification not claim 13 distinctly define a protein sequence of “a functional fragment of MYDGY” rendering the metes and bounds of “a functional fragment of MYDGY” indefinite. Furthermore, it is unclear with respect to the word “optionally” because the word “optionally” has the same meaning as “preferred to”. 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. 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. Claim s 1-3, 7, 9, and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Alvarez et al. (WO 2013/184939 A2, cited in IDS) and evidenced by Fuleihan et al. ( https://www . wolterskluwer .com/ en /know/clinical-effectiveness-terms. 2026© UpToDate, Inc. ) in view of Doyonnas et al. ( The Journal of Immunology, 2000, 165: 840–851 , cited in IDS ) and Chan et al. ( J Biol Chem. ( 2001 Jan 19;276(3):2139-52 , cited in IDS) . Alvarez et al. teach fusion polypeptides comprising a mucin-domain polypeptide covalently linked to an active protein to improve pharmacokinetic and/or physicochemical properties (Abstract). Alvarez et al. teach m ucin-domain polypeptides may be linked to the active protein via either the N-or C-terminus of the active protein (p16, line 10-11). Alvarez et al. teach a mucin domain polypeptide may also comprise all or a portion of a protein comprising a mucin domain of CD164 or other m ucin-domain polypeptides (p18, line 26; claim 10) . Alvarez et al. teach a mucin domain polypeptide comprises domains of tandem amino acid repeats that are rich in Pro, Ser and Thr. In one aspect of this embodiment, the number of tandem repeat units within a mucin domain polypeptide of the invention is between 1 and 25 (p19, line 3-6; claim 11) . Alvarez et al. teach the conjugated therapeutic proteins comprising recombinant follicle-stimulating ho rm one /r FSH (p38, line 14), parathyroid hormone (PTH ) 1 -84 (p38, line 31), or GLP-1 (p25, line 13). Fuleihan et al. is cited as evidenced to show PTH (1-84) ha ving a plasma half-life of two to four minutes (p1, para 2) , consistent with Alvarez’s teachings . Alvarez et al. and evidenced by Fuleihan et al. do not specify a protein sequence of a mucin-domain of CD164. Doyonnas et al. teach CD164 protein structure and protein sequence well known in the right 279792 0 0 art shown as follows (p843, Fig 1A and 1B) comprising Mucin domain-2 ( SEQ ID NO: 2 ) . The transient phrase “comprising” is an open-ended language and the mucin domain polypeptide can be beneficially including additional amino acids in particular serine and threonine for O-linked glycosylation (p841, col 1, line 8-10) at the N- and/or C-terminus of the Mucin domain s . Similarly, Chan et al. is cited to show the transmembrane domain of CD164 starts at Ala 163 (mucin domain 2 ends at Asp 162) and the N-terminal S erine 110 linked to mucin domain 2 (Exon 4) is also a potential O-linked glycosylation site shown as follows (p2178, Fig 7A). Because Alvarez et al. teach a mucin domain polypeptide (e.g., CD164) comprises 1-25 domains of tandem amino acid repeats that are rich in Pro, Ser and Thr (p19, line 3-6; claim 11) conjugated to short half-life therapeutic proteins comprising recombinant follicle-stimulating ho rm one /r FSH (p38, line 14), parathyroid hormone (PTH ) 1 -84 (p38, line 31), and/or GLP-1 (p25, line 13), one or ordinary skill in the art would have found it obvious to conjugate Doyonnas ’s mucin domain polypeptide comprising 1 - 25 tandem repeat units from the CD164 protein to a short half-life protein as taught by Alvarez et al. A Mucin domain derived from CD164 comprising SEQ ID NO: 2 with multiple glycosylation sites and 1-25 tandem repeat units (enriched with Pro, Ser and Thr ) known in the art as taught by both Doyonnas and Chan et al. , one of ordinary skill in the art would have found it obvious to use select the underlined amino acid sequence comprising mucin domain 2 for conjugation to a short half-life bioactive peptide. One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine Alvarez et al. with Doyonnas et al. because (a) Alvarez et al. teach fusion polypeptides comprising a mucin-domain polypeptide of CD164 (p18, line 26; claim 10) covalently linked to an active protein with short half-life , e.g., parathyroid hormone (PTH ) 1 -84 (p38, line 31) , to improve pharmacokinetic and/or physicochemical properties (Abstract) , (b) Doyonnas et al. teach CD164 protein structure and protein sequence well known in the art (p843, Fig 1A and 1B) comprising SEQ ID NO: 2 , and (c) Chan et al. is cited to show the transmembrane domain of CD164 starts at Ala 163 and the N-terminal serine of mucin domain 2 (Exon 4) is also a potential O-linked glycosylation site (p2178, Fig 7A). The combination would have reasonable expectation of success because all the references teach mucin domain polypeptide of CD164. Fuleihan et al. is cited as evidenced to show PTH (1-84) ha ving a plasma half-life of two to four minutes (p1, para 2), consistent with Alvarez’s teachings. Fuleihan et al. is cited as evidenced to show PTH (1-84) ha ving a plasma half-life of two to four minutes (p1, para 2), consistent with Alvarez’s teachings. With respect to claim 2, Chan et al. show the transmembrane domain of CD164 starts at Ala 163 and the N-terminal Serine 110 linked to mucin domain 2 (Exon 4) is also a potential O-linked glycosylation site shown as follows (p2178, Fig 7A). The mucin domain peptide fragment from Ser110 to Asp162 has 100% identity to the instant SEQ ID NO: 2 shown as follows. With respect to claim 3, Alvarez et al. teach m ucin-domain polypeptides may be linked to the active protein via either the N-or C-terminus of the active protein (p16, line 10-11). With respect to claim s 7 and 9, Alvarez et al. in view of Doyonnas et al. and Chan et al. teach a mucin domain polypeptide of CD164 (comprising SEQ ID NO: 2) fusion to parathyroid hormone (or other short half-life protein of GLP-1 or recombinant follicle-stimulating ho rm one ). The same fusion protein must has the same properties of half-life as claimed. W hen the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent ”. See MPEP 2112.01(I). Alvarez et al. teach a mucin-domain polypeptide total sequence length is from 32 to 200. As increased half-life correlates with increasing hydrodynamic radius . Furthermore, mucinylation allows for the half-life to be optimized by increasing or reducing the number of mucin tandem repeats in the mucin-domain peptide of the fusion protein (p21, last para to p22, para 1) . Thus, one of ordinary skill in the art would expect the serum half-life of parathyroid PTH (1-84) , 2-4 minutes, with significant increase after conjugation to a mucin-domain polypeptide taught by Alvarez et al.in view of Doyonnas et al. With respect to claim 25, Alvarez et al. teach a pharmaceutical composition comprising a fusion protein comprising a therapeutic active protein linked to an mucin-domain polypeptide and at least one pharmaceutically acceptable carrier (p45, line 25-27). 2. Claim s 1-3, 7, 9, 13-14, and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. , Chan et al. as applied to claims 1-3, 7, 9, and 25 and further in view of Korf- Klingebiel et al. ( Nat Med. 2015 Feb;21(2):140-9 cited in IDS) and Uniport MYDGF ( https://www.uniprot.org/uniprotkb/ A0A2R9B4B0/ entry#sequences . 2018-06-20 ). Claim 13 is drawn to the hetero1ogous polypeptide a s MYDGF or a functional fragment thereof. Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. and Chan et al. teach beneficial conjugation of a short half-life bioactive protein covalently linked to a mucin domain polypeptide (Abstract) to treat cardiac diseases and/or myocardial infarction /MI (p45, line 9). Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. and Chan et al. did not specify the bioactive protein as m yeloid-derived growth factor (MYDGF) . Korf- Klingebiel et al. teach Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction /MI (Title and Abstract). Korf- Klingebiel et al. teach Mydgf protects cardiac myocytes from cell death (p142, col 2, para 1; p142, Fig 2). Korf- Klingebiel et al. teach administration of Mydgf as a therapy for acute MI and e limination of Mydgf from plasma approximated a first-order kinetic with an estimated half-life of 15.3 min , suggesting Mydgf is a short half-life protein (p145, col 2, Mydgf protein therapy after MI ). Because Korf- Klingebiel et al. teach Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction and Mydgf is a short half-life protein, one of ordinary skill in the art would have found it obvious to conjugate Alvarez’s mucin domain peptide to Mydgf to treat myocardial infarction (MI), reading on claim 13. 2609215 2540 0 0 Uniport MYDGF is cited to show the protein sequence of MYDGF comprising t he amino acids 1-31 as the signal peptide (p3). The full-length MYGDF is further shown as follows (p4) . A sequence alignment of comparing the instant SEQ ID NO: 3 with the MYDGF protein fusion to with the mucin domain peptide taught by Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. and Chan et al. is shown as follows , reading on claim 14. One of ordinary skill in the art before the effective filing date of this invention would have found it obvious to combine (i) Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. and Chan et al. with (ii) Korf- Klingebiel et al. in view of NP_061980.1 . because (a) Alvarez et al. and evidenced by Fuleihan et al. in view of Doyonnas et al. and Chan et al. teach a fusion protein comprising a mucin-domain polypeptide covalently linked to a short half- life active protein (Abstract) to treat cardiac diseases and/or myocardial infarction /MI (p45, line 9) and (b) Korf- Klingebiel et al. teach Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction /MI (Title and Abstract). and Mydgf protects cardiac myocytes from cell death (p142, col 2, para 1; p142, Fig 2). The combination would have reasonable expectation of success because both Alvarez et al. and Korf- Klingebiel et al. teach administration of a bioactive peptide to treat myocardial infarction . Uniport MYDGF is cited to show MYDGF protein sequence consisting of amino acids 32-173 by excluding the signal peptide sequence of amino acids 1-31. Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT JIA-HAI LEE whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)270-1691 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT Mon-Fri from 9:00 AM to 6:00 PM . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. 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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. /J.L/ Examiner, Art Unit 1658 26-March-2026 /LI N KOMATSU/ Primary Examiner, Art Unit 1658