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 .
Priority
The present application was filed on 08/11/2022. This application claims benefit of U.S. Provisional Patent Application 62/976,947 filed on 02/14/2020.
Claim status
Claims 1, 3-9, 12, and 13 are amended. Claims 14-20 are new. Claims 1-20 are pending and examined herein.
Objection/Rejection status
The rejection of claims 5-7 and 9-13 under 35 USC 112(b) is withdrawn in view of the amendment of the claims.
The rejection of claim 12 under 35 USC 112(b) is withdrawn in view of the amendment of the claim.
The rejection of claims 6-7 under 35 USC 112(d) is withdrawn in view of the amendment of the claims.
The rejection of claims 1-20 under 35 USC 102/103 and Double Patenting are updated in view of the amendment of the claims.
Claim Rejections - 35 USC § 102
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)(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.
(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.
Claim(s) 1-6 and 8-11, and 13-17 is/are rejected under 35 U.S.C. 102 (a)(1) and (a)(2) as being anticipated by Ast (US20170247769).
Regarding claim 1, Ast discloses a calcium biosensor comprising a fluorescent domain and an analyte binding domain as shown in Fig.5.
Ast teaches that the fluorescent domain can spontaneously photo switch by cis-trans isomerization or protonation, and wherein the rate of isomerization or rate of protonation is altered by binding of the analyte binding domain to an analyte of interest (see par.112 or 142: teaching that the responsiveness of a sensor polypeptide (e.g. a change in conformation or state) that occurs in response to interaction of the sensor polypeptide with an analyte can cause a change in fluorescence of the fluorescence polypeptide; see par.112: teaching that the change can be the result of an alteration in the environment, structure, protonation or oligomerization status of the fluorescent indicator or chromophore; see par.153: teaching that the fluorescence intensity of the sensor is changed by the protonation equilibrium of the chromophore).
Ast teaches that measurement of the spontaneous photoswitching rate can be used to determine the concentration of the analyte of interest (see par.142, 146, 183-184: teaching the method of generating a standard curve of a known concentration of an analyte and a corresponding amount of an optical property of the fluorescent polypeptide, measuring a change in intensity of fluorescence that occurs following exposure of the analyte in a sample to the change in environmental condition, comparing the amount of the optical property of the fluorescence to the standard curve, determining the concentration of the analyte of interest).
Regarding claim 2, Ast teaches the protein biosensor of claim 1, wherein the photoswitching changes the fluorescent intensity or the fluorescent color of the fluorescent domain (see par. 112, 142, and 153).
Regarding claim 3, Ast teaches the protein biosensor of claim 1. Ast also teaches the analyte binding domain can be attached to the fluorescent domain at N-terminus (see Fig.3-5).
Regarding claim 4, Ast teaches the protein biosensor of claim 1, wherein the analyte binding domain is attached to the C-terminus of the fluorescent domain (see Fig.5: showing that the protein sensor comprises the analyte binding domain which is attached in C-terminus of the fluorescent domain).
Regarding claim 5, Ast teaches the protein biosensor of claim 3 or 4, wherein the fluorescent domain is green fluorescent protein (GFP) or rsCherry (see par.75: disclosing that a fluorescent polypeptide is GFP).
Regarding claim 6, Ast teaches the protein biosensor of claim 1, wherein the analyte binding domain binds calcium (see Fig.5, par.106).
Regarding claim 8, Ast teaches a method of making a protein biosensor of claim 1: .
attaching an analyte binding domain to a fluorescent domain (see Fig.2, Fig.5, Fig.8 and par.27 and par.30: showing that the calcium-binding protein CaM is attached to the fluorescent domain via linkers);
the fluorescent domain can spontaneously photoswitch by cis-trans isomerization or protonation; and wherein the rate of isomerization or rate of protonation is altered by binding of the analyte binding domain to an analyte of interest, such that measurement of the spontaneous photoswitching rate can be used to determine the concentration of the analyte of interest (see par.112, 142, 146, 153, 183-184; see discussion of Ast in claim 1).
Regarding claim 9, Ast teaches the protein biosensor of claim 1. Ast teaches a method of identifying the concentration of an analyte of interest in a sample, comprising contacting the sample with the protein biosensor of claim 1 (see par.106: disclosing a method for detecting the presence of an environmental parameter in a sample, by contacting the sample with a fluorescent sensor or biosensor; see par.142, 146, 183-184: teaching the method of determining the concentration of the analyte of interest).
Regarding claim 10, Ast teaches a method of identifying the concentration of an analyte of interest in a sample of claim 9. Ast teaches a method of identifying the concentration of an analyte of interest in a sample (see par.142, 146, 183-184: teaching the method of generating a standard curve of a known concentration of an analyte and a corresponding amount of an optical property of the fluorescent polypeptide, measuring a change in intensity of fluorescence that occurs following exposure of the analyte in a sample to the change in environmental condition, comparing the amount of the optical property of the fluorescence to the standard curve, determining the concentration of the analyte of interest).
Regarding claim 11, Ast teaches a method of identifying the concentration of an analyte of interest in a sample of claim 9. Ast teaches that the change of fluorescent intensity of the biosensor depends on the concentration of the analyte in the sample (see par.142, Fig.8B). This teaching encompasses the change in fluorescent intensity of the biosensor is not dependent on the concentration of the biosensor.
Regarding claim 13, Ast teaches the protein biosensor of claim 1. Ast also provides kits for determining the presence of an activity and/or analyte in a sample. The kit contains the protein biosensor of claim 1 (see at least par.112, 142, 146-147, 153, 183-184 and Fig.2 and Fig.5: disclosing a kit comprising the fluorescent sensor polypeptide of claim 1). Ast also provides a method for detecting the presence of an analyte in a sample (see par.106). The provided method encompasses the instructions for using the protein sensor.
Regarding claims 14-15, Ast teaches the protein biosensor of claim 2. Ast teaches wherein the analyte binding domain is attached to the N-terminus or C-terminus of the fluorescent domain (see Fig.2-3: showing the analyte binding domain can be attached to C-terminus and N-terminus of the fluorescent domain via linkers).
Regarding claim 16, Ast teaches the protein biosensor of claim 14 or 15, wherein the fluorescent domain is green fluorescent protein (GFP) or rsCherry (see par.75: disclosing that a fluorescent polypeptide is GFP).
Regarding claim 17, Ast teaches the protein biosensor of claim 1, wherein the fluorescent domain is green fluorescent protein (GFP) (see par.75: disclosing that a fluorescent polypeptide is GFP).
Claim(s) 1 and 7 is/are rejected under 35 U.S.C. 102 (a)(1) and (a)(2) as being anticipated by Sergeevich et al. (RU2515903).
Regarding claims 1, and 7, Sergeevich discloses a fluorescent biosensor for detecting nicotinamide NAD+/NADH (see page 1 lines 14-15). The sensor comprises a GFP domain and a touch domain, wherein the touch domain encompasses an analyte binding domain because it is sensitive to changes in certain cell parameters, such as change in concentration of an ion or molecule (calcium ions, hydrogen peroxide, hydrogen ions, etc.) (see page 2 lines 35-41).
Sergeevich further teaches that the fluorescent domain can spontaneously photo switch by cis-trans isomerization or protonation, and wherein the rate of isomerization or rate of protonation is altered by binding of the analyte binding domain to an analyte of interest (see page 15 lines 20-31: disclosing that the dependence of the sensor signal (the ratio of the intensities of the excitation spectrum in the 420/490) of the NAD + / NADH ratio in the system at any given time was determined, which the spectra of the sensor signal were recorded every 30 seconds; the increasing or decreasing in fluorescent intensity corresponds to the deprotonated form of the chromophore of the sensor). The spectral characteristics of the biosensor change following the change in the ratio NAD + / NADH in the medium (see page 15 lines 20-31). This teaching encompasses the rate of isomerization or rate of protonation is altered by binding of the analyte binding domain to an analyte of interest.
Sergeevich teaches that measurements of the spontaneous photoswitching rate can be used to determine the concentration of the analyte of interest (see page 12 lines 50-55: teaching that fluorescent proteins change the spectral properties in the presence of hydrogen peroxide; they can be used to register the change ratio NAD + / NADH in the cell, particularly during the process at which the decrease in the concentration of NADH and consequently increasing the concentration of NAD +).
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.
Claim(s) 12 and 19 is/are rejected under 35 U.S.C. 103 as being unpatentable over Ast (US20170247769), as applied to claim 1 above, in view of Nagai et al. (US20160231248) and Brakemann et al. (Molecular Basis of the Light-driven Switching of the Photochromic Fluorescent Protein Padron, J. of biological chemistry, Volume 285, Issue 19, 7 May 2010, Pages 14603-14609).
Regarding claim 12, Ast teaches the protein biosensor of claim 1.
Ast does not teach the biosensor comprises a sequence of SEQ ID NO. 1 as recited in claim 12.
However, Nagai discloses a fluorescent protein Padron having an amino acid sequence of Sequence ID No. 2 (see par.73), which undergoes a cis-trans isomerization or protonation upon photo-switching as taught by Brakemann (see Brakemann Abstract). The figure below shows that the Sequence ID No. 2 of Nagai is 91.7% matched with the claimed Sequence ID No.1 in the current application.
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Nagai further discloses another fluorescent protein having the amino acid sequence of Sequence ID No. 1, which was produced by introducing seven mutations, namely N1021, L141P, F173S, 5190D, D192V, K202R, and E218G, into Padron (e.g., Sequence ID No. 2). The protein Sequence ID No. 1 is also a photo-switching fluorescent (see par.73). The fluorescence property of the protein having an amino acid sequence of Sequence ID No. 1 in which one to several amino acids are deleted, substituted, and/or added may be the same as that of the protein having an amino acid sequence of Sequence ID No. 1 (see par.27), wherein the term “one to several” in the present disclosure includes 1 to 50, 1 to 40, 1 to 35, 1 to 30, 1 to 25, 1 to 20, 1 to 15, 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1 (see par.27). The figure below shows the Sequence ID No. 1 of Nagai is 90.7% matched with the claimed Sequence ID No.1 in the current application.
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Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the fluorescent domain taught by Ast with the fluorescent protein taught by Nagai, because they may have an equivalent function in terms of photo-switching by a cis-trans isomerization or protonation despite several amino acid differences (see Nagai par.27). A person of ordinary skill in the art would have been motivated to use the fluorescent protein taught by Nagai (e.g., Sequence ID No. 1) because it is a fast photo-switching speed and high photostability (see Abstract and par.6). Moreover, Nagai teaches that the fluorescent protein can be used as a photochromic material applicable to optical recording media such as a biosensor (see par.54).
Regarding claim 19, Ast, Nagai, and Brakemann teach the protein biosensor of claim 12. Ast teaches that the analyte binding domain binds calcium (see Ast Fig.5).
Claim(s) 12 and 20 is/are rejected under 35 U.S.C. 103 as being unpatentable over Sergeevich et al. (RU2515903), as applied to claim 1 above, in view of Nagai et al. (US20160231248) and Brakemann et al. (Molecular Basis of the Light-driven Switching of the Photochromic Fluorescent Protein Padron, J. of biological chemistry, Volume 285, Issue 19, 7 May 2010, Pages 14603-14609).
Regarding claim 12, Sergeevich teaches the protein biosensor of claim 1.
Sergeevich does not teach the biosensor comprises a sequence of SEQ ID NO. 1 as recited in claim 12.
Nagai discloses a fluorescent protein Padron having an amino acid sequence of Sequence ID No. 2 (see par.73), which undergoes a cis-trans isomerization or protonation upon photo-switching as taught by Brakemann (see Brakemann Abstract). The figure below shows that the Sequence ID No. 2 of Nagai is 91.7% matched with the claimed Sequence ID No.1 in the current application.
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Nagai further discloses another fluorescent protein having the amino acid sequence of Sequence ID No. 1, which was produced by introducing seven mutations, namely N1021, L141P, F173S, 5190D, D192V, K202R, and E218G, into Padron (e.g., Sequence ID No. 2). The protein Sequence ID No. 1 is also a photo-switching fluorescent (see par.73). The fluorescence property of the protein having an amino acid sequence of Sequence ID No. 1 in which one to several amino acids are deleted, substituted, and/or added may be the same as that of the protein having an amino acid sequence of Sequence ID No. 1 (see par.27), wherein the term “one to several” in the present disclosure includes 1 to 50, 1 to 40, 1 to 35, 1 to 30, 1 to 25, 1 to 20, 1 to 15, 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1 (see par.27). The figure below shows the Sequence ID No. 1 of Nagai is 90.7% matched with the claimed Sequence ID No.1 in the current application.
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Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the fluorescent domain taught by Sergeevich with the fluorescent protein taught by Nagai, because they may have an equivalent function in terms of photo-switching by a cis-trans isomerization or protonation despite several amino acid differences (see Nagai par.27). A person of ordinary skill in the art would have been motivated to use the fluorescent protein taught by Nagai (e.g., Sequence ID No. 1) because it is a fast photo-switching speed and high photostability (see Abstract and par.6). Moreover, Nagai teaches that the fluorescent protein can be used as a photochromic material applicable to optical recording media such as a biosensor (see par.54).
Regarding claim 20, Sergeevich, Nagai, and Brakemann teach the protein biosensor of claim 12. Ast teaches that the analyte binding domain binds nicotinamide (see Sergeevich page 1 lines 14-15).
Claim(s) 18 is/are rejected under 35 U.S.C. 103 as being unpatentable over Ast (US20170247769), as applied to claim 1 above, further in view of Zhou et al. (Photoswitchable fluorescent proteins: ten years of colorful chemistry and exciting applications, Current Opinion in Chemical Biology, Volume 17, Issue 4, August 2013, IDS filed 01/23/2026).
Regarding claim 18, Ast teaches the protein biosensor of claim 1, wherein the fluorescent domain is a variety of fluorescent protein, e.g., mCherry. Ast does not teach using rsCherry.
Zhou teaches that the reversibly photoswitchable fluorescent proteins are fluorescent proteins having reversibly photoswitch by cis-trans isomerization of the chromophore (see pages 1-2). Recent fluorescent protein (FP) engineering efforts have succeeded in adjusting multiple performance parameters of photoswitchable FPs to improve their utility in biological experiments (see page 2 par.2). One of the improved red photoswitchable FPs includes rsCherry (see page 3 par.2, see Table 1 on page 4).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the fluorescent protein in the fluorescent domain of Ast with the rsCherry for the benefit of improving the biosensor in detecting an analyte of interest as taught by Zhou. One of ordinary skill in the art would have had a reasonable expectation of success in combining Ast and Zhou because the photoswitching FPs of Ast and Zhou are functionally equivalent (Ast teaches the fluorescence polypeptide of a biosensor can change its intensity following an alteration in the environment, structure, protonation or oligomerization status of the fluorescent indicator or chromophore (see par.112) and Zhou teaches the photoswitching feature of the rsCherry FP results from different effects of protonation, chromophore planarity, and pocket flexibility (see page 2 par.1, page 5 last par. page 6 par.1)).
Double Patenting
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 uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-5, 8-11 and 13-18 is/are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 and 7-10 and 12-17 of copending Application No. 18/684,651 (‘651). Although the claims at issue are not identical, they are not patentably distinct from each other because the reasons below.
As for claim 1, While the claim 1 of ‘651 does not mention measurement of the spontaneous photoswitching rate can be used to determine the concentration of the analyte of interest, but the protein biosensor of ‘651 is used to identify the concentration of an analyte of interest in a sample because the change in fluorescent intensity of the biosensor is correlated with the concentration of the analyte of interest in the sample (see Specification of ‘651 par.9). Therefore, claim 1 of ‘651 encompasses the claimed limitations.
As for claim 2, claim 2 of ‘651 encompasses the claimed limitation.
As for claim 3, claim 3 of ‘651 encompasses the claimed limitation.
As for claim 4, claim 4 of ‘651 encompasses the claimed limitation.
As for claim 5, claim 5 of ‘651 encompasses the claimed limitation.
As for claim 8, claim 7 of ‘651 encompasses the claimed limitations.
As for claim 9, claim 8 of ‘651 encompasses the claimed limitation.
As for claim 10, claim 9 of ‘651 encompasses the claimed limitation.
As for claim 11, claim 10 of ‘651 encompasses the claimed limitation.
As for claim 13, claim 12 of ‘651 encompasses the claimed limitation.
As for claim 14, claim 13 of ‘651 encompasses the claimed limitation.
As for claim 15, claim 14 of ‘651 encompasses the claimed limitation.
As for claims 16-18, claims 15-17 of ‘651 encompass the claimed limitation.
Claim 6 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 and 7-10 and 12-17 of copending Application No. 18/684,651 (‘651) in view of Miyawaki (US20030004306).
As for claim 6, claim 1 of ‘651 encompasses the claimed limitations of the instant claim 1. The ‘651 does not teach the analyte of interest is calcium.
Miyawaki teaches the protein biosensor as discussed in claim 1 above under 35 USC 102 rejections. Miyawaki teaches that the analyte of interest is calcium (see Abstract).
‘651 and Miyawaki are analogous to a fluorescent based protein biosensor comprising a fluorescent domain and an analyte binding domain. It would have been obvious to utilize this known fluorescent based protein biosensor for the purpose of detecting calcium in the sample by modifying the protein sensor taught by ‘651, substituting the analyte binding domain with a calcium binding domain as taught by Miyawaki, so that it can detect the concentration of calcium in the sample.
Claim 7 is provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5 and 7-10 and 12-17 of copending Application No. 18/684,651 (‘651) in view of Sergeevich et al. (RU2515903).
As for claim 7, claim 1 of ‘651 encompasses the claimed limitations of the instant claim 1. The ‘651 does not teach the analyte of interest is nicotinamide.
Sergeevich teaches the protein biosensor as discussed in claim 1 above under 35 USC 102 rejections. Sergeevich teaches that the analyte of interest is nicotinamide (see page 1 lines 14-15).
The sensor comprises GFP domain and touch domain, wherein touch domain encompasses an analyte binding domain because it is sensitive to change in a certain cell parameters, such as change in concentration of an ion or molecule (calcium ions, hydrogen peroxide, hydrogen ions and etc.) (see page 2 par.5).
‘651 and Sergeevich are analogous to a fluorescent based protein biosensor comprising a fluorescent domain and an analyte binding domain. It would have been obvious to utilize this known fluorescent based protein biosensor for the purpose of detecting nicotinamide in the sample by modifying the protein sensor taught by ‘651, substituting the analyte binding domain which is sensitive to change in a certain cell parameters, e.g., nicotinamide as taught by Sergeevich, so that it can detect the concentration of nicotinamide in the sample.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 01/23/2026 have been fully considered, but they are not persuasive because the arguments are based on the newly added limitation. The rejections are updated in the office action above.
Conclusion
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 CHAU N.B. TRAN whose telephone number is (571)272-3663. The examiner can normally be reached Mon-Fri 8:30-6:30 CT.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Bao-Thuy L Nguyen can be reached at 571-272-0824. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/CHAU N.B. TRAN/Examiner, Art Unit 1677
/BAO-THUY L NGUYEN/Supervisory Patent Examiner, Art Unit 1677 September 21, 2026
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