CTNF 17/998,057 CTNF 81521 DETAILED ACTION Notice of Pre-AIA or AIA Status 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. Election/Restrictions Applicant’s election without traverse of the species of SEQ ID NO: 55 in the reply filed on 10/02/2025 is acknowledged. Claim 46 recites SEQ ID NO: 10, which shares the first 29 residues with SEQ ID NO: 55. Claims 1, 7, 9, 13, 16, 31, 35, 39, 46, 56, 58, 61, 68, 69, 77 and 81 read upon the elected invention and are under examination. 05-03 AIA The Art Unit location of your application in the USPTO has changed. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Art Unit 1675, Examiner Christina Borgeest . Priority Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) and 365(c) is acknowledged. Based on the information given by Applicant and an inspection of the prior applications, the examiner has concluded that the subject matter defined in the instant claims is supported by the disclosures in PCT/US2021/031260 and provisional application serial no. 63/021,814. The priority date of claims 1, 7, 9, 13, 16, 31, 35, 39, 46, 56, 58, 61, 68, 69, 77 and 81 of the instant application is 05/08/2020. Claim Objections Claims 77 and 81 are objected to under 37 CFR 1.75(c) as being in improper form because a multiple dependent claim may not refer back to another multiple dependent claim. Both claims 77 and 81 depend in the alternative upon claim 68, which is a multiple dependent claim, and therefore constitute improper multiple dependent claims. See MPEP § 608.01(n). 07-30-03-h AIA Claim Interpretation Claim 77 is interpreted as a method of treating a relaxin-associated disorder comprising administering an effective amount of: the polypeptide of claim 46; the polynucleotide of claim 56; the expression vector of claim 58; or the pharmaceutical composition of claim 68, wherein the pharmaceutical composition is: the polypeptide of claim 46; the polynucleotide of claim 56; or the expression vector of claim 58. Further, claim 81 is interpreted as a kit comprising an effective amount of: the polypeptide of claim 46; the polynucleotide of claim 56; the expression vector of claim 58; or the pharmaceutical composition of claim 68, wherein the pharmaceutical composition is: the polypeptide of claim 46; the polynucleotide of claim 56; or the expression vector of claim 58. The specification discusses “pharmaceutical compositions” at p. 25, lines 13-15: The pharmaceutical compositions of the invention are formulated with suitable carriers, excipients, and other agents that provide improved transfer, delivery, tolerance, and the like. Thus, a pharmaceutical composition encompasses formulation with carriers, excipients and the like. Claim Rejections - 35 USC § 112(b) 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 Claims 68, 69, 77 and 81 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. Claims 68, 69, 77 and 81 all depend from claim 45 in the alternative, however, claim 45 is canceled, therefore the full scope of the claims cannot be known. The claims must particularly point out and distinctly define the metes and bounds of the subject matter that will be protected by the patent grant (see MPEP 2171). Claim Rejections - 35 USC § 112(a) 07-30-01 AIA The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. 07-31-03 AIA Claims 1, 7, 9, 13, 16, 31, 35, 39, 46, 56, 58, 61, 68, 69, 77 and 81 are r ejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA), first paragraph, because the specification, while being enabling for a fusion protein comprising from N-terminus to C-terminus, a first peptide comprising the amino acid sequence of SEQ ID NO: 2; a peptide linker comprising the amino acid sequence selected from the group consisting of SEQ ID NO: 14 and SEQ ID NO: 16 and a second peptide comprising the amino acid sequence of SEQ ID NO: 1, wherein the first peptide, the peptide linker, and the second peptide are operably linked, or alternatively, a fusion protein comprising a first peptide, a peptide linker, and a second peptide, wherein the amino acid sequence of the fusion protein is SEQ ID NO: 55 and a method of treatment with said fusion proteins as set forth in the prior art, d oes not reasonably provide enablement for t he claims as broadly recited. T he specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to m ake or use t he invention commensurate in scope with these claims. T here are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue.” (See In re Wands , 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 Fed. Cir. 1988). These factors include, but are not limited to: (a) the breadth of the claims; (b) the nature of the invention; (c) the state of the prior art; (d) the level of one of ordinary skill; (e) the level of predictability in the art; (f) the amount of direction provided by the inventor; (g) the existence of working examples; and (h) the quantity of experimentation needed to make or use the invention based on the content of the disclosure. The claims are broad with respect to the recited fusion proteins, polypeptides, polynucleotides, pharmaceutical compositions, methods of treatment and patient population. The claims require between 85-90% sequence identity to the recited sequences. The specification teaches “[t]he components, structures, and sequences of exemplary single chain recombinant relaxin-2 proteins” noting that “[t]he single chain recombinant relaxin-2 proteins have several advantages, including, but not limited to, requiring no downstream processing or modification steps” (see Example 1, Table 1, pages 33-38). The specification outlines methods of generating single chain recombinant relaxin 2 proteins and the biochemical properties of exemplary recombinant single chain proteins SE201 [SEQ ID NO: 34], SE202 [SEQ ID NO: 35], SE203 [SEQ ID NO: 36], SE204 [SEQ ID NO: 37], SE205 [SEQ ID NO: 38], SE206 [SEQ ID NO: 39], SE207 [SEQ ID NO: 40] and SE301 [SEQ ID NO: 41] (see Examples 2-3, p. 39 and Figures 1-3). The specification discloses the percentage of biological activity relative to native relaxin (Emax values) in Table 2 (see Example 4, pages 40-41). The values for SEQ ID NOs: 28, 29, 34-40 shows high activity relative to native relaxin, though SEQ ID NOs: 26, 27, 30 and 43-45 did not have detectable activity (see Table 2 at pages 40-41). See also the specification at p. 43 (Example 6; Table 5 and Figure 14), which shows good biological activity of SE501 (SEQ ID NO: 60) and SE502 (SEQ ID NO: 61). A comparison between the sequences listed in Tables 2 and 5 and SEQ ID NO: 55 show that with the exception of SEQ ID NOs: 26 and 30, all of the sequences listed therein had ≥ 85% sequence identity thereto. Further, some sequences that did not have detectable biological activity, SEQ ID NOs: 43-45, had ≥ 94% sequence identity to instant SEQ ID NO: 55. Therefore, there is no clear nexus between sequence identity and biological activity. Applicant does not teach how between 10-15 of amino acid residues can be mutated in the recited sequences to result in a protein with native relaxin-2 activity (see claim 9). The number of mutations generally possible in any given protein that can be made with a reasonable expectation of success are limited. Certain positions in the sequence are critical to the protein's structure/function relationship, e.g., such as various sites or regions directly involved in binding, activity and in providing the correct three-dimensional spatial orientation of binding and active sites. The art provides evidence that mutations can be destabilizing and their effects unpredictable. Bhattacharya et al. (PLoS ONE 12(3): e0171355. https://doi.org/10.1371/journal.pone.0171355; 22 pages total) teach even single nucleotide variations have a “range of effects at the protein level that are significantly greater than assumed by existing software prediction methods, and that correct prediction of consequences remains a significant challenge” (p. 18, 1 st and 2 nd paragraphs). In addition, Fenton et al. (Medicinal Chemistry Research (2020) 29:1133–1146) review the unpredictability of making substitutions at non-conserved positions in a protein, which can have significant effects on protein function, that computational algorithms cannot predict very well (p. 1134, right column, middle paragraph). Although machine learning algorithms have improved the ability to predict protein 3D structure from sequences, methods based on artificial intelligence for predicting the impact of mutations on protein stability still face challenges, including prediction biases towards “generalization”, “data set”, “destabilizing mutations” and the inability to predict the effects of multiple mutations. See Figure 1, at p. 162 and the discussion at pages 165-166 of Pucci et al. (Current Opinion in Structural Biology 2022, 72: 161-168). Even in the case of single mutations, artificial intelligence programs do not accurately “predict the impact of mutation on protein stability” or function (see p. 2, 2 nd paragraph and p. 7, 1 st full paragraph of Pak et al., PLoS ONE 18(3): e0282689. https://doi.org/10.1371/journal.pone.0282689). In the instant case, the claims encompass up to a 15% divergence from the recited sequences. Applicants have provided little or no guidance beyond the mere presentation of sequence data to enable one of ordinary skill in the art to determine, without undue experimentation, the positions in the protein which are tolerant to change by amino acid substitutions or deletions, and the nature and extent of changes that can be made in these positions. Although the specification outlines art-recognized procedures for producing and screening for active muteins, this is not adequate guidance as to the nature of active derivatives that may be constructed, but is merely an invitation to the artisan to use the current invention as a starting point for further experimentation. Claims 1, 7, 9, 13, 31, 35, 39, 46, 56, 58, 61, 68 and 81 are drawn to products, however, when evaluating whether the claims are enabled, it is appropriate to consider the disclosed intended usages. Claims 69 and 77 are drawn methods of treatment. The specification broadly defines relaxin-associated disorders (see paragraph bridging pages 7-8 of the specification): [T]he relaxin-2-associated disorder is selected from the group consisting of kidney diseases, fibrotic diseases, and cardiovascular diseases. In yet another embodiment, the disorder is selected from the group consisting of focal segmental glomerular sclerosis (FSGS), diabetic nephropathy, hepatorenal syndrome, scleroderma, idiopathic pulmonary fibrosis, renal fibrosis, cardiac fibrosis, NASH, dilated cardiomyopathy, diastolic heart failure, pulmonary arterial hypertension, chronic heart failure, acute heart failure, congestive heart failure, coronary artery disease, hypertension, and pre-eclampsia. Treatment is also broadly defined in the instant specification as encompassing prevention and reversing pathology (see claims 11, lines 27-34). Further, the specification contemplates the disclosed compositions for modulating, that is increasing or decreasing, levels of relaxin-2 (see p. 2, lines 1-6). The specification discloses administering the SE301 protein (SEQ ID NO: 41) to nine CD-1 male mice to test pharmacokinetics, the results of which are shown in FIG. 13 and Table 4: “the circulating half-life of SE301 is about 77.5 hours at 10 mg/kg dosing, about 90.7 hours at 1 mg/kg dosing, and about 130 hours at 0.2 mg/kg dosing” (see Example 5, pages 41-43, especially, p. 43, lines 5-9). The protein set forth in SEQ ID NO: 41 also had relatively high binding affinity for RXFP1, a relaxin receptor (see p. 44). Thus, the specification provides data about the biological half-life and pharmacokinetics of selected fusion proteins, but does not provide any examples demonstrating treatment of the encompassed diseases/disorders with the recited polypeptides and fusion proteins. The art provides limited guidance concerning the treatment of disease with relaxin agonists. Kanai et al. (Molecular and Cellular Endocrinology 487 (2019) 66-74) teach that relaxin has been studied as a “potential treatment for fibrotic diseases since the middle of the 20 th century” (see p. 66, right column, last paragraph). Kanai et al. conclude that there remains “considerable hurdles to clear to reach the ultimate goal of successful treatment of human fibrotic disease” (see p. 72, right column, last paragraph). Yu et al. (Medicine (2018) 97:25(e11010)) teach that treatment of acute heart failure patients with recombinant relaxin “failed to reduce mortality” (see p. 4, left and right columns). The art does suggest an RFXP-1 agonist may be administered during the late secretory phase of the menstrual cycle to treat a woman who has experienced placental syndrome in a previous pregnancy (see claim 1 of US Patent 9,907,833). Nevertheless, the art does not teach or suggest that relaxin agonists can be used to treat the broad array of diseases contemplated in the instant specification. Compounding the breadth of treating or preventing disease in the contemplated patient population, claims 56, 58, 61, 68, 77 and 81 encompass nucleic acid compositions encoding said relaxin fusion proteins and polypeptides and a method of gene therapy for treating relaxin-related disorders. The specification also contemplates gene therapy (see p. 8, lines 7-21), however, it does not teach any gene therapy working examples. Relevant literature teaches despite having made strides over the past 40 years, gene therapy remains unpredictable (see Antoine Gardin and Giuseppe Ronzitti, Archives de Pédiatrie 30 (2023) 8S46–8S52—hereafter “Gardin”). Gardin teaches that while methods of using adeno-associated viral (AAV) vectors for transducing DNA have improved, particularly in the treatment of the liver, central nervous system, muscles, eye and bone marrow, significant challenges remain (see p. 8S46, left column, 1 st paragraph). For instance, besides immunogenicity, challenges include non-target organ effects, the neutralizing effect of autoantibodies and loss of long-term correction (see p. 8S48, left column, 2 nd paragraph; paragraph bridging pages 8S48-8S49; p. 8S49, under “3”). In view of the teachings of the relevant art, the ability to treat relaxin-associated disorders using RNA- or DNA-based therapies was not readily available in the relevant art at the time of filing of the instant application, and the limited teachings of the instant application do not overcome these shortcomings. Due to the large quantity of experimentation necessary to determine which of the encompassed fusion proteins, polypeptides and polynucleotides would be capable of treating or preventing the encompassed diseases/disorders, the lack of direction/guidance presented in the specification regarding and the absence of working examples directed to the same, the complex nature of the invention, the unpredictability of the effects of mutation on protein structure and function, and the breadth of the claims which fail to recite limitations on the fusion proteins, polypeptides, polynucleotides and patient population, undue experimentation would be required of the skilled artisan to make and/or use the claimed invention in its full scope. Notice for all US Patent Applications filed on or after March 16, 2013 : 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 . Claim Rejections - 35 USC § 102 07-07-aia AIA 07-07 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 – 07-08-aia AIA (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. 07-15 AIA Claims 46, 56, 58, 61, 69, 77 and 81 are r ejected under 35 U.S.C. 102(a )(1) as being a nticipated b y S hen et al. (US20160287713A1). The limitation stating at least about 90% identical to the entire amino acid sequence of SEQ ID NO: 10 is interpreted as requiring at least about 90% sequence identity to SEQ ID NO: 10. S hen et al. teach a relaxin sequence that shares at least about 90% sequence identity to SEQ ID NO: 10. See the alignment between instant SEQ ID NO: 10 and sequence 50 of Shen et al.: RESULT 235 US-14-917-689-50 (NOTE: this sequence has 2 duplicates in the database searched) Sequence 50, US/14917689 Publication No. US20160287713A1 GENERAL INFORMATION APPLICANT: THE CALIFORNIA INSTITUTE FOR BIOMEDICAL RESEARCH APPLICANT: THE SCRIPPS RESEARCH INSTITUTE TITLE OF INVENTION: MODIFIED THERAPEUTIC AGENTS AND COMPOSITIONS THEREOF FILE REFERENCE: 41135-709.831 CURRENT APPLICATION NUMBER: US/14/917,689 CURRENT FILING DATE: 2016-06-15 PRIOR APPLICATION NUMBER: US 61/917,816 PRIOR FILING DATE: 2013-12-18 PRIOR APPLICATION NUMBER: PCT/US2014/055457 PRIOR FILING DATE: 2014-09-12 PRIOR APPLICATION NUMBER: US 61/877,799 PRIOR FILING DATE: 2013-09-13 NUMBER OF SEQ ID NOS: 73 SEQ ID NO 50 LENGTH: 29 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: Description of Artificial Sequence: Synthetic peptide Query Match 90.6%; Score 135; Length 29; Best Local Similarity 100.0%; Matches 26; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 2 SWKEEVIKLCGRELVRAQIAICGKST 27 |||||||||||||||||||||||||| Db 2 SWKEEVIKLCGRELVRAQIAICGKST 27 Shen et al. teach that the peptide set forth in sequence 50 may be used as a therapeutic agent in methods of treatment and formulated as a pharmaceutical composition (see paragraph [0174], claims 109-120). Shen et al. also contemplate that the pharmaceutical compositions may also include nucleic acids encoding said peptides, expression vectors, along with recombinant cells (see paragraphs [0454]; [0469]-[0476]). Shen et al. state that the disorders to be treated refers to conditions that would benefit from treatment with the therapeutic agent in question, which in this case, includes relaxin (see paragraphs [0428]; [0518]). Thus, because Shen et al. disclose the limitations of claims 46, they also disclose the limitations of claims 56, 58, 61, 68, 69, 77 and 81 insomuch as they depend upon claim 46. Although Shen et al. do not disclose the effects of sequence 50 (sharing 90.6% sequence identity with instant SEQ ID NO: 10) upon enhancing relaxin as recited in claim 69, because Shen et al. teach administration of the same agent to treat those in need of relaxin (see paragraph [0428]), the same clinically significant improvements as recited in claim 69 must have been inherently occurring in the prior art. See Ex parte Novitski , 26 USPQ2d 1389 (BPAI 1993) and Integra LifeSciences I Ltd. V. Merck KGaA , (DC SCalif) 50 USPQ2d 1846; i.e., the treatment methods set forth in Shen et al. must, by definition achieve the same clinically significant improvements as recited in claim 69 absent evidence to the contrary. Thus, all the limitations are met by Shen and colleagues. Closest Prior Art The sequences set forth in SEQ ID NOs: 1-2 are disclosed in the prior art. For instance, the European Patent Office Search Report (on IDS filed 10/02/2025) lists a number of references disclosing these sequences. An exemplary reference is US 2011/245469 (on IDS filed 10/02/2025), which discloses a recombinant relaxin construct comprising 100% sequence identity to SEQ ID NOs: 2 and 1, respectively (see Figure 3A). However, none of the documents listed in the EPO Search Report or the prior art disclose a peptide linker comprising an amino acid sequence that is at least about 85% identical to the entire amino acid sequence of SEQ ID NOs: 14 or 16. The prior art does not disclose these linker peptides. See also the following alignments between the fused sequences of instant SEQ ID NOs: 2 – 16 – 1 with sequence 44 of US Patent 10,739,924 and sequence 49 of US Patent No. 11,161,891: Patent No. 10730924 GENERAL INFORMATION APPLICANT: ModernaTX, Inc. TITLE OF INVENTION: POLYNUCLEOTIDES ENCODING RELAXIN FILE REFERENCE: M1378.70064US01 CURRENT APPLICATION NUMBER: US/16/025,302 CURRENT FILING DATE: 2018-07-02 PRIOR APPLICATION NUMBER: PCT/US2017/033411 PRIOR FILING DATE: 2017-05-18 PRIOR APPLICATION NUMBER: US 62/338,470 PRIOR FILING DATE: 2016-05-18 NUMBER OF SEQ ID NOS: 589 SEQ ID NO 44 LENGTH: 97 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: Synthetic Polypeptide Query Match 84.6%; Score 296.2; Length 97; Best Local Similarity 75.3%; Matches 55; Conservative 6; Mismatches 4; Indels 8; Gaps 1; Qy 1 DSWMEEVIKLCGRELVRAQIAICGMSTWS--------DAAGANANAGARQLYSALANKCC 52 ||||||||||||||||||||||||||||| ::|:: : |: ||||||||||| Db 25 DSWMEEVIKLCGRELVRAQIAICGMSTWSGSSGGGSGSSSGSSGSGGSGQLYSALANKCC 84 Qy 53 HVGCTKRSLARFC 65 ||||||||||||| Db 85 HVGCTKRSLARFC 97 Patent No. 11161891 GENERAL INFORMATION APPLICANT: THE CALIFORNIA INSTITUTE FOR BIOMEDICAL RESEARCH TITLE OF INVENTION: RELAXIN IMMUNOGLOBULIN FUSION PROTEINS AND METHODS OF USE FILE REFERENCE: 41135-756.831 CURRENT APPLICATION NUMBER: US/16/060,384 CURRENT FILING DATE: 2018-11-08 PRIOR APPLICATION NUMBER: PCT/US2016/065779 PRIOR FILING DATE: 2016-12-09 PRIOR APPLICATION NUMBER: 62/265,344 PRIOR FILING DATE: 2015-12-09 NUMBER OF SEQ ID NOS: 99 SEQ ID NO 49 LENGTH: 62 TYPE: PRT ORGANISM: Artificial Sequence FEATURE: OTHER INFORMATION: Description of Artificial Sequence: Synthetic polypeptide Query Match 83.3%; Score 291.7; Length 62; Best Local Similarity 84.6%; Matches 55; Conservative 1; Mismatches 6; Indels 3; Gaps 1; Qy 1 DSWMEEVIKLCGRELVRAQIAICGMSTWSDAAGANANAGARQLYSALANKCCHVGCTKRS 60 ||||||||||||||||||||||||||||| | : | ||||||||||||||||||| Db 1 DSWMEEVIKLCGRELVRAQIAICGMSTWS---GGGGSGGGGQLYSALANKCCHVGCTKRS 57 Qy 61 LARFC 65 ||||| Db 58 LARFC 62 While each of these alignment shows at least about 85% sequence identity (either overall or local similarity) to the fused sequences set forth in the claims, neither has a peptide linker comprising an amino acid sequence that is at least about 85% identical to the entire amino acid sequence of SEQ ID NOs: 14 or 16. Likewise, the claims of copending application 19/397,507 and US Patent 12,509,497 recite relaxin fusion proteins, however, none of the recited fusion proteins share sequence identity with the linker portion of instant SEQ ID NO: 55. The post-filing date art of Erlandson et al. ( Mol. Pharmaceutics 2024, 21, 4441-4449—on IDS filed 10/02/2025) discloses the linkers set forth in instant SEQ ID NOs: 14 and 16 (see p. 4444, right column, 4 th paragraph). Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA M BORGEEST whose telephone number is (571)272-4482. The examiner can normally be reached M-F 9-5:30 EDT. 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, Jeffrey Stucker can be reached at 5712720911. 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. /CHRISTINA M BORGEEST/Primary Examiner, Art Unit 1675 Application/Control Number: 17/998,057 Page 2 Art Unit: 1675 Application/Control Number: 17/998,057 Page 3 Art Unit: 1675 Application/Control Number: 17/998,057 Page 4 Art Unit: 1675 Application/Control Number: 17/998,057 Page 5 Art Unit: 1675 Application/Control Number: 17/998,057 Page 6 Art Unit: 1675 Application/Control Number: 17/998,057 Page 7 Art Unit: 1675 Application/Control Number: 17/998,057 Page 8 Art Unit: 1675 Application/Control Number: 17/998,057 Page 9 Art Unit: 1675 Application/Control Number: 17/998,057 Page 10 Art Unit: 1675 Application/Control Number: 17/998,057 Page 11 Art Unit: 1675 Application/Control Number: 17/998,057 Page 12 Art Unit: 1675 Application/Control Number: 17/998,057 Page 13 Art Unit: 1675 Application/Control Number: 17/998,057 Page 14 Art Unit: 1675 Application/Control Number: 17/998,057 Page 15 Art Unit: 1675 Application/Control Number: 17/998,057 Page 16 Art Unit: 1675
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