CTFR 17/908,427 CTFR 80388 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. This office action is in response to Applicants’ amendments/remarks received April 15, 2026. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn. Claims 1-12, 14-16, 18-21, 23, 30-33 are canceled. Claims 25-29, 34 are withdrawn. Claims 13, 17, 22, 24, 35-43 are under consideration. Priority: This application is a 371 of PCT/US2021/020591, filed March 3, 2021, which claims benefit of provisional application 62/985179, filed March 4, 2020. Objections and Rejections 07-29-01 AIA Claim 24 is objected to because of the following informalities: in claim 24, the set of double brackets “[[ ]]” should be deleted . Appropriate correction is required. 07-30-02 AIA The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. 07-34-01 Claim 41 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 41 recites the polypeptide comprises modified amino acids, a reporter protein, or an enzyme. It is not clear which polypeptide in claim 13, (i) or (ii), comprises the modified amino acids, a reporter protein, or an enzyme recited in claim 41. Further clarification and/or correction is requested. 07-06 AIA 15-10-15 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. 07-20-aia AIA 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. 07-21-aia AIA Claim s 13, 17, 22, 24, 35-42 are rejected under 35 U.S.C. 103 as being unpatentable over You et al. (WO 2018231834; previously cited) in view of Braisted et al. (US 6013763; previously cited). You et al. disclose a resilin-like polypeptide comprising GFP-His-(GRGDQPYQ)20 (at least paragraph 0118, Table 3). You et al. further disclose a resilin-like polypeptide comprising GFP-His-(GRGDSPYS)80 (at least paragraph 0118, Table 3). You et al. disclose the systems comprising elastin-like polypeptides (ELPs) and resilin-like polypeptides (RLPs) can be attached to a biomolecule of interest, including enzymes, therapeutic biologics, antigenic proteins, immunogenic proteins, GFP, GLP-1, etc. (at least paragraphs 0102-0104). You et al. disclose fusion proteins comprising RLP fused to a biomolecule and/or ELP fused to a biomolecule (at least p. 29-30 Table 3). You et al. disclose the production of a wide range of proteins with RLP or ELP, which can be extended to express multiple therapeutic biologics (at least paragraphs 0202-0203) . Braisted et al. disclose protein A from Staphylococcus aureus binds with high affinity to a region of IgG (col. 1 lines 15-20). Braisted et al. disclose Z domain variants for therapeutic use in compositions comprising auxiliary agents (col. 42-44 section V). Braisted et al. disclose the Z domain of protein A has the amino acid sequence of SEQ ID NO: 4 (col. 4 lines 3-11), where SEQ ID NO: 4 has 100% sequence identity with instant SEQ ID NO: 159. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate and/or attach a Z domain variant derived from SEQ ID NO: 4 of Braisted et al. for the biomolecule of interest with the resilin-like polypeptides comprising -(GRGDQPYQ)20 and/or -(GRGDSPYS)80 of You et al. to arrive at the claimed fusion protein composition (instant claims 13, 22, 24) because You et al. disclose the systems comprising resilin-like polypeptides for production of an attached protein or fusion protein, including antigenic proteins, immunogenic proteins, etc. One of ordinary skill would have a reasonable expectation of success because methods for engineering resilin-like polypeptides comprising a protein of interest were known and disclosed in the prior art. Regarding instant claim 17, since You et al. disclose a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited, the polypeptides of You et al. will necessarily have the property to enhance bioavailability of a molecule as recited in the instant claim. “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). MPEP 2112.01. Regarding instant claims 35-42, since You et al. disclose a fusion protein comprising a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited, the polypeptides of You et al. will necessarily have the phase separation properties recited in the instant claims. “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). MPEP 2112.01. Reply : In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection as being anticipated by You et al. has been withdrawn. However, the 103 rejection over You et al. and Braisted et al. is maintained for the reasons noted above and herein. Applicants assert that the office cites paragraphs 0102-0104 of You et al. for allegedly disclosing that resilin-like polypeptides can be attached to a molecule of interest. Applicants assert that this is incorrect. Applicants assert that You et al. does not disclose fusion proteins containing RLPs and biomolecules of interest. Applicants assert that rather, You et al. disclose systems for biomolecule production using microorganisms that are contained within an encapsulation material and disclose that RLPs as examples of either encapsulation materials or biomolecules that may be produced (paragraphs 0104, 0106, 0108 of You et al.). Applicants’ remarks are not persuasive. It is known that disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments. In re Susi, 440 F.2d 442, 169 USPQ 423 (CCPA 1971). MPEP 2123. In this instance, You et al. has disclosed that the materials for encapsulation, including ELPs and RLPs, are fused to a biomolecule of interest (at least p. 29-30 Table 3). Therefore, You et al. disclose fusion proteins comprising RLP fused to a biomolecule and/or ELP fused to a biomolecule, i.e. a GFP-His-(GRGDSPYS)80, a GLP1-ELP, etc. (at least p. 29-30 Table 3). You et al. disclose the production of a wide range of proteins with RLP or ELP, which can be extended to express multiple therapeutic biologics (at least paragraphs 0202-0203). Therefore, You et al. reasonably disclose that to express a biomolecule of interest, the biomolecule is fused to the RLP. While You et al. do not explicitly teach that the biomolecule of interest comprises instant SEQ ID NO: 159, You et al. disclose that biomolecules of interest including enzymes, therapeutic biologics, antigenic proteins, immunogenic proteins, GFP, GLP-1, etc. (at least paragraphs 0102-0104), where Braisted et al. disclose Z domain variants of protein A for therapeutic use in compositions, having the amino acid sequence of SEQ ID NO: 4 (col. 4 lines 3-11, col. 42-44 section V), where SEQ ID NO: 4 has 100% sequence identity with instant SEQ ID NO: 159. Therefore, It would have been obvious to one of ordinary skill to incorporate and/or attach a Z domain variant derived from SEQ ID NO: 4 of Braisted et al. for the biomolecule of interest with the resilin-like polypeptides comprising -(GRGDQPYQ)20 and/or -(GRGDSPYS)80 of You et al. to arrive at the claimed fusion protein composition because You et al. disclose the systems comprising resilin-like polypeptides for production of an attached protein or fusion protein, including antigenic proteins, immunogenic proteins, etc. One of ordinary skill would have a reasonable expectation of success because methods for engineering resilin-like polypeptides comprising a protein of interest were known and disclosed in the prior art. Applicants assert that expressing the attached molecules as fusion proteins unexpectedly rescues protein expression of the attached molecules. Applicants point to Table 8 and Fig. 33 of the instant specification. Applicants’ remarks are not persuasive. MPEP 716.02(b) notes that Applicant has the burden to establish that the results are unexpected and significant. Evidence of unexpected properties may be in the form of a direct or indirect comparison of the claimed invention with the closest prior art which is commensurate in scope with the claims. See also MPEP 716.02(e) noting that the claimed subject matter has to be compared with the closest prior art to be effective to rebut a prima facie case of obviousness. MPEP 716.01(c) notes that objective evidence which must be factually supported by an appropriate affidavit or declaration to be of probative value includes evidence of unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor. See, for example, In re De Blauwe , 736 F.2d 699, 705, 222 USPQ 191, 196 (Fed. Cir. 1984) (“It is well settled that unexpected results must be established by factual evidence.” “[A]ppellants have not presented any experimental data showing that prior heat-shrinkable articles split. Due to the absence of tests comparing appellant’s heat shrinkable articles with those of the closest prior art, we conclude that appellant’s assertions of unexpected results constitute mere argument.”). See also In re Lindner, 457 F.2d 506, 508, 173 USPQ 356, 358 (CCPA 1972); Ex parte George , 21 USPQ2d 1058 (Bd. Pat. App. & Inter. 1991). Further, the arguments of counsel cannot take the place of evidence in the record. In re Schulze , 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965). Examples of attorney statements which are not evidence and which must be supported by an appropriate affidavit or declaration include statements regarding unexpected results, commercial success, solution of a long-felt need, inoperability of the prior art, invention before the date of the reference, and allegations that the author(s) of the prior art derived the disclosed subject matter from the inventor or at least one joint inventor. In this instance, Applicants have not shown or established that the results are unexpected and significant over the closest prior art fusion proteins comprising a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited. For at least these reasons, the 103 rejection is maintained . 07-21-aia AIA Claim s 13, 17, 22, 24, 35-43 are rejected under 35 U.S.C. 103 as being unpatentable over Chilkoti et al. (US 20120121709, cited as US 8470967 on IDS 01.05.23; previously cited) in view of Braisted et al. (US 6013763; previously cited). Chilkoti et al. disclose environmentally responsive proteins comprising at least ten sequences selected from GRGDSPYQ (SEQ ID NO: 48) (at least paragraphs 0008, 0053, p. 47 claim 21). Chilkoti et al. disclose attaching the environmentally responsive protein to a polypeptide of interest, including therapeutics, polymers, to form fusion proteins (at least paragraphs 0074-0075) . Braisted et al. disclose protein A from Staphylococcus aureus binds with high affinity to a region of IgG (col. 1 lines 15-20). Braisted et al. disclose Z domain variants for therapeutic use in compositions comprising auxiliary agents (col. 42-44 section V). Braisted et al. disclose the Z domain of protein A has the amino acid sequence of SEQ ID NO: 4 (col. 4 lines 3-11), where SEQ ID NO: 4 has 100% sequence identity with instant SEQ ID NO: 159. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate and/or attach a Z domain variant derived from SEQ ID NO: 4 of Braisted et al. for the polypeptide of interest with the polypeptides comprising at least ten sequences of GRGDSPYQ (SEQ ID NO: 48) of Chilkoti et al. to arrive at the claimed fusion protein composition (instant claims 13, 22, 24) because Chilkoti et al. disclose the systems comprising environmentally responsive polypeptides for attaching to biomolecule of interest, including proteins, therapeutics, etc. One of ordinary skill would have a reasonable expectation of success because methods for engineering environmentally responsive polypeptides comprising a protein of interest were known and disclosed in the prior art. Regarding instant claim 17, since Chilkoti et al. disclose a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited, the polypeptides of Chilkoti et al. will necessarily have the property to enhance bioavailability of a molecule as recited in the instant claim. “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). MPEP 2112.01. Regarding instant claims 35-41, since Chilkoti et al. disclose a fusion protein comprising a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited, the polypeptides of Chilkoti et al. will necessarily have the phase separation properties recited in the instant claims. “Products of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). MPEP 2112.01. Regarding instant claim 42, as noted above, Chilkoti et al. disclose an environmentally responsive protein comprising at least ten sequences of GRGDSPY Q (SEQ ID NO: 48) (at least paragraphs 0008, 0053, p. 47 claim 21). Chilkoti et al. disclose the design of the behavior of the polypeptides is tuned by adjusting the hydrophobicity of the residues comprising the repeating unit (at least paragraph 0120). Chilkoti et al. disclose that incorporating a glutamine (Q) significantly reduced the UCST of the biopolymer (at least paragraph 0120). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to arrive at the recited repeat sequence GRGDSPY S by substituting another hydrophilic amino acid residue, serine (S), for the glutamine (Q) residue in the repeat sequence GRGDSPY Q of Chilkoti et al. because Chilkoti et al. disclose peptides that are similar to the recited peptides and disclose that the behavior of the polypeptides can be tuned and it is known that serine is also a hydrophilic amino acid residue. Regarding instant claim 43, it is disclosed in the instant specification that instant SEQ ID NO: 3 comprises the repeat sequence (GRGDQPYQ) 40 . As noted above, Chilkoti et al. disclose an environmentally responsive protein comprising at least ten sequences of GRGD S PYQ (SEQ ID NO: 48) (at least paragraphs 0008, 0053, p. 47 claim 21). Chilkoti et al. disclose the design of the behavior of the polypeptides is tuned by adjusting the hydrophobicity of the residues comprising the repeating unit (at least paragraph 0120). Chilkoti et al. disclose that incorporating a glutamine (Q) significantly reduced the UCST of the biopolymer (at least paragraph 0120). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to arrive at the recited repeat sequence GRGD Q PYQ by substituting another hydrophilic amino acid residue, serine (S), for the glutamine (Q) residue in the repeat sequence GRGD Q PYQ of Chilkoti et al. because Chilkoti et al. disclose peptides that are similar to the recited peptides and disclose that the behavior of the polypeptides can be tuned and it is known that serine is also a hydrophilic amino acid residue. Reply : In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection as being anticipated by Chilkoti et al. has been withdrawn. However, the 103 rejection over Chilkoti et al. and Braisted et al. is maintained for the reasons noted above and herein. The reasons for maintaining Chilkoti et al. are the same as similarly noted above for You et al. In this instance, Chilkoti et al. expressly disclose fusion proteins comprising the environmentally responsive protein and a polypeptide of interest, including therapeutics, polymers, etc. (at least paragraphs 0074-0075), where Braisted et al. disclose Z domain variants of protein A for therapeutic use in compositions, having the amino acid sequence of SEQ ID NO: 4 (col. 4 lines 3-11, col. 42-44 section V), where SEQ ID NO: 4 has 100% sequence identity with instant SEQ ID NO: 159. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate and/or attach a Z domain variant derived from SEQ ID NO: 4 of Braisted et al. for the polypeptide of interest with the polypeptides comprising at least ten sequences of GRGDSPYQ (SEQ ID NO: 48) of Chilkoti et al. to arrive at the claimed fusion protein composition because Chilkoti et al. disclose the systems comprising environmentally responsive polypeptides for attaching to biomolecule of interest, including proteins, therapeutics, etc. One of ordinary skill would have a reasonable expectation of success because methods for engineering environmentally responsive polypeptides comprising a protein of interest were known and disclosed in the prior art. Regarding Applicants’ remarks that expressing the attached molecules as fusion proteins unexpectedly rescues protein expression of the attached molecules, the remarks are not persuasive. As noted above, Applicants have not shown or established that the results are unexpected and significant over the closest prior art fusion proteins comprising a polypeptide comprising ten or more repeats of an amino acid sequence having the same structural features recited. For at least these reasons, the 103 rejection is maintained . 07-21-aia AIA Claim s 13, 17, 22, 24, 35-43 are rejected under 35 U.S.C. 103 as being unpatentable over Chilkoti et al. (US 20120121709, cited as US 8470967 on IDS 01.05.23; previously cited) in view of Braisted et al. (US 6013763; previously cited) and Wu et al. (US 20210346570; previously cited). The teachings of Chilkoti et al. in view of Braisted et al. over at least instant claims 13, 17, 22, 24, 35-42 are noted above . Further regarding instant claim 43, Wu et al. disclose a resilin-like polypeptide comprising a number of repeating amino acid sequence motifs, comprising MSKGP-(GRGDQPYQ)n, where n greater than 5, including n is 20 (at least paragraphs 0005, 0118-0119, 0368, p. 38 claim 16). Wu et al. disclose a resilin-like polypeptide comprising the amino acid sequence of SEQ ID NO: 15 (p. 37), where SEQ ID NO: 15 has 100% sequence identity with instant SEQ ID NO: 3. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to incorporate the resilin-like polypeptide comprising the amino acid sequence of SEQ ID NO: 15 of Wu et al. for the environmentally responsive polypeptide ten or more repeats of an amino acid sequence in the fusion protein comprising a Z domain variant derived from SEQ ID NO: 4 of Chilkoti et al. in view of Braisted et al. One of ordinary skill would have a reasonable expectation of success because methods for engineering environmentally responsive polypeptides comprising a protein of interest were known and disclosed in the prior art. Reply : In view of Applicants’ amendments/remarks, the previous 102(a)(1) rejection as being anticipated by Wu et al. has been withdrawn. However, Wu et al. is maintained as a 103 reference for the reasons noted above. The reasons for maintaining Chilkoti et al. and Braisted et al. are the same as noted above . 08-33 AIA The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg , 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman , 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi , 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum , 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel , 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington , 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA/25, or PTO/AIA/26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer. 08-35 Claim s 13, 17, 22, 24, 35-42 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 18-19 of copending Application No. 17908415 (‘415) (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the ‘415 application claims are drawn to a fusion protein comprising a polypeptide comprising ten or more repeats of an amino acid sequence as recited in instant claim 13 (see at least claim 18 of the ‘415 application). Regarding instant claim 42, the ‘415 application claim 18 recites polypeptides comprising the repeat sequence is GRGDSPYS. Regarding instant claims 13, 17, 22, 24, the ‘415 application claim 18 recites the polypeptide further comprises a binding polypeptide comprising a Z-domain of staphylococcal protein A . This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Reply : The terminal disclaimer filed on April 15, 2026 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any U.S. patent granted on U.S. Application 17908415 (‘415) has been reviewed and is not accepted. The incorrect terminal disclaimer form was submitted. A PTO/AIA/25 form should be submitted for pending applications. No additional fee is required with the resubmission. See also the terminal disclaimer review decision of April 19, 2026. No claim is allowed. 07-39 AIA THIS ACTION IS MADE FINAL. 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 Marsha Tsay whose telephone number is (571)272-2938. The examiner can normally be reached M-F. 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 N. 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. 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If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /Marsha Tsay/Primary Examiner, Art Unit 1656 Application/Control Number: 17/908,427 Page 2 Art Unit: 1656 Application/Control Number: 17/908,427 Page 3 Art Unit: 1656 Application/Control Number: 17/908,427 Page 4 Art Unit: 1656 Application/Control Number: 17/908,427 Page 5 Art Unit: 1656 Application/Control Number: 17/908,427 Page 6 Art Unit: 1656 Application/Control Number: 17/908,427 Page 7 Art Unit: 1656 Application/Control Number: 17/908,427 Page 8 Art Unit: 1656 Application/Control Number: 17/908,427 Page 9 Art Unit: 1656 Application/Control Number: 17/908,427 Page 10 Art Unit: 1656 Application/Control Number: 17/908,427 Page 11 Art Unit: 1656 Application/Control Number: 17/908,427 Page 12 Art Unit: 1656 Application/Control Number: 17/908,427 Page 13 Art Unit: 1656 Application/Control Number: 17/908,427 Page 14 Art Unit: 1656
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