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 .
Applicant’s amendment of claims 19, 20, 22-35 and 37, in the paper of 2/20/2026, is acknowledged. Applicants' arguments filed on 2/20/2026, have been fully considered and are deemed to be persuasive to overcome some of the rejections previously applied. Rejections and/or objections not reiterated from previous office actions are hereby withdrawn. Claims 19-37 are still at issue and are present for examination.
Election/Restrictions
Applicant's election without traverse of the following species: Species Group 1: acetone; Species Group 2: Slip_0880(SEQ ID NO:7) and Tle2 (subunit A, SEQ ID NO:19 and subunit B, SEQ ID NO:20) and Species Group 3: Geobacillus, in the paper of 9/2/2025, is acknowledged.
Claims 23 and 25 are withdrawn from further consideration by the examiner, 37CFR 1.142(b), as being drawn to a non-elected invention.
Claim Objections
Claim 20, 24, 29, 34 are objected to because of the following informalities:
Claims 20, 24, 29 and 34 depend form rejected claims 19, 28 and 33.
Appropriate correction and/or comment is required.
Claim Rejections - 35 USC § 112
The rejection of claim(s) 19-22, 24, 26-37 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention is withdrawn based upon applicants amendment of the claims and applicants arguments presented in the paper of 2/20/2026.
The rejection of claim(s) 19-22, 24, 26-37 under 35 U.S.C. 112, first paragraph, based upon a lack of enablement is withdrawn based upon applicants amendment of the claims and applicants arguments presented in the paper of 2/20/2026.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 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) 19, 21, 22, 26-28, 30-33, 35-37 is/are rejected under 35 U.S.C. 103 as being unpatentable Zeldes et al. (Biotechnology and Bioengineering, Vol 115, No. 12, pp 2951-2961, Oct 23, 2018), Shaw et al., Biotechnology for Biofuels, Vol 8:75, May 2015, Sillers et al. US 20130273555, Uniprot Accession No. D7CLS5 Aug 2020, Uniprot Accession No. A8F7H7 Aug 2020 and Uniprot Accession No. A8F7H6 Aug 2020.
This rejection was stated in the previous office action as it applied to previous claims 19, 21, 22, 26-28, 30-33, 35-37. In response to the rejection applicants have amended the claims and traverse the rejection as it applies to the newly amended claims. For applicants convenience the original rejection is repeated herein.
Zeldes et al. demonstrates a synthetic enzymatic pathway for extremely thermophilic acetone production that functions up to at least 70°C in vitro, comprising i) a thiolase (Thl) from Caldanaerobacter subterraneus, ii) heteromultimeric acetoacetyl-CoA:acetate CoA-transferase (CtfAB) complexes from Thermosipho melanesiensis and Caldanaerobacter subterraneus and iii) acetoacetate decarboxylase (Adc) from the mesophile C. acetobutylicum which has unusual thermostability. The Adc protein from C. acetobutylicum taught by Zeldes et al. is 100% identical to instant SEQ ID NO:28. This pathway can be used in an extremely thermophilic host organism (abstract; Fig. 6). Zeldes et al. as a part of their disclosure teach methods of providing a thermophilic cell comprising a i) a thiolase (Thl) from Caldanaerobacter subterraneus, ii) heteromultimeric acetoacetyl-CoA:acetate CoA-transferase (CtfAB) complexes from Thermosipho melanesiensis and Caldanaerobacter subterraneus and iii) acetoacetate decarboxylase (Adc) and nucleic acids and cells comprising a polynucleotide encoding a i) a thiolase (Thl) from Caldanaerobacter subterraneus, ii) heteromultimeric acetoacetyl-CoA:acetate CoA-transferase (CtfAB) complexes from Thermosipho melanesiensis and Caldanaerobacter subterraneus and iii) acetoacetate decarboxylase (Adc).
In Shaw et al., the enzymes i) thiolase, ii) acetoacetate:acetate CoA-transferase, and iii) acetoacetate decarboxylase were assembled in the thermophilic anaerobe T. saccharolyticum with genes from thermophilic donor organisms that do not natively produce acetone. The resultant strain converted acetic acid to acetone and ethanol (page 5, col.1 , par. 2-page 6, col. 1 line 1). Thus Shaw et al. teach methods of producing acetone with the above enzymes and nucleic acids and cells comprising polynucleotides encoding above enzymes.
Sillers et al. describes genetically modified thermophilic microorganisms converting acetate to acetone or isopropanol, wherein the acetyl-CoA is converted to acetoacetyl-CoA by i) a thiolase, the acetoacetyl-CoA is converted to acetoacetate by ii) a CoA transferase, and the acetoacetate is converted to acetone by iii) an acetoacetate decarboxylase (paragraphs [0018] and [0019]; claims 42, 112). Sillers et al. disclose cultivating the above thermophilic cells in a bioreactor at 55oC in cultivation broth thereby producing acetone and recovering the acetone produced.
Zeldes et al., Shaw et al., and Sillers et al. each relate to a thermophilic microorganism comprising three acetone pathway enzymes j), ii) and iii) as functionally defined in claim 1. The cited prior art does however not explicitly disclose a thermophilic cell expressing a combination of the specific enzymes i), ii) and iii), wherein i) is selected from SEQ ID NOs 1,2,3,4,7,59 or functional variants thereof with at least 70% sequence identity, ii) is selected from SEQ ID NOs 19/20 (Tle2) and SEQ ID NO: 21 (Dde2) or functional variants thereof with at least 70% sequence identity, and iii) is according to SEQ ID NO:28 or functional variants thereof with at least 70% sequence identity.
Uniprot Accession No. D7CLS5 Aug 2020 teaches thiolase from Syntrophothermus lipocalidus which has 100% sequence identity to the protein having the instant amino acid sequence of SEQ ID NO:7.
Uniprot Accession No. A8F7H7 Aug 2020 teaches acetate-CoA transferase subunit a from Thermotoga lettingae which has 100% sequence identity to the protein having the instant amino acid sequence of SEQ ID NO:19.
Uniprot Accession No. A8F7H6 Aug 2020 teaches acetate-CoA transferase subunit b from Thermotoga lettingae which has 100% sequence identity to the protein having the instant amino acid sequence of SEQ ID NO:20.
One of skill in the art before the effective filing date would have been motivated to substitute the enzymes taught by Uniprot Accession No. D7CLS5 (thiolase), Uniprot Accession No. A8F7H7 (acetate-CoA transferase subunit a), Uniprot Accession No. A8F7H6 (acetate-CoA transferase subunit b) and the Adc protein from C. acetobutylicum as taught by Zeldes et al. in the methods taught by Shaw et al. for producing acetone. One of skill in the art before the effective filing date would have been motivated to substitute the polynucleotides encoding the above enzymes for use in the methods taught by Shaw et al. In view of the teachings provided in any of Zeldes et al., Shaw et al., and Sillers et al. it would be obvious for a skilled person to select a suitable combination of i) acetyl-CoA acetyltransferase, ii) acetate CoA-transferase, and iii) acetoacetate decarboxylase for providing a synthetic pathway for the production of acetone. The expectation of success is high based upon the high level of skill in the art in the area of genetic engineering and protein expression as exemplified by the teachings of Zeldes et al., Shaw et al., and Sillers et al.
Applicants Response
After applicants summarized interpretation of the rejection applicant traverses the rejection on the basis that applicants submit that the cited reference combination fails to 1) disclose or suggest the desired titers recited in the claims or that such high titers could be acheived; 2) provide motivation to substitute the Uniprot Sequences taught in the cited references; or 3) provide a reasonable expectation of success for the substitution of sequences to arrive at the recited titers.
Applicants submit that claims 19, 28, and 33 recite that acetone is produced with a titer of at least 0.8 g/L and the method of Zeldes showed an acetone titer of less than 2.5 mM. or 0.29 g/L based up0n applicants calculaltion. Applicants submit that the method of Shaw discloses an acetone titer up to 0.78 g/L at 55°C and with maltodextrin as the carbon source. Shaw, Fig. 6, strain M2212. Applicants submit that Figure 16 of Sillers shows acetone production by the same M2212 strain used in Shaw et al., with maltodextrin as sole carbon source - yielding a titer which appears similar (i.e. a titer of 0.78 g/L). Applicants submit that the UniProt Sequences do not teach acetone production.
Applicants submit that Zeldes discloses in vitro acetone production in a cell free environment. Applicants submit that there is no suggestion in Zeldes of acetone production within a cell (in the presence of acetyl-CoA) and/or butanone production within a cell (in the presence of acetyl-CoA and propionyl-CoA), by the same microbial production platform. Applicants submit that thus, the cited references combined with Zeldes et al. does not teach or suggest production of acetone with a titer of at least 0.8 g/L as claimed.
Applicants submit that the cited references do not provide a motivation to substitute the claimed sequences to arrive at the claimed titer.
Applicants submit that The Office Action does not provide an articulated reason for why one of ordinary skill in the art would be motivated by the cited references to substitute the enzymes taught by the UniProt Sequences into the methods taught by Zeldes, Shaw, and Sillers. Applicants submit that simple recognition of other thiolase, CoA-transferase or acetoacetate decarboxylase sequences does not provide any motivation to substitute the sequences disclosed by Zeldes, Shaw, and Sillers to arrive at the claimed acetone titer.
Applicants submit that As discussed supra, there is also no suggestion in Zeldes that the specific enzymes recited in the claims would function sufficiently in a cellular environment, nor that their expression in a thermophilic cell would yield acetone titers >0.8 g/L or produce butanone. Applicants submit that Nowhere does the cited reference combination disclose any of the specific enzymes listed in Zeldes for production of acetone and/or butanone. In fact, Zeldes does not even mention any of the organisms S. lipocalidus, C. aurantiacus and P. lettingae as possible sources for enzymes for the synthetic pathway, neither does Zeldes mention production of butanone at thermophilic conditions.
Applicants submit that while Shaw and Sillers both disclose formation of acetone by engineered bacterial cells, turning to any of those documents would not motivate one of ordinary skill in the art arrive at the invention, as none of them lists any of the organisms S. lipocalidus, C. aurantiacus and P. lettingae as possible sources for enzymes for the synthetic pathway, neither do they mention production of butanone at thermophilic conditions. Applicants submit that importantly, the acetone titer achieved by the cells disclosed in Shaw et al. and Sillers et al. is of 0.78 g/L. There is thus no suggestion in Shaw or Sillers that higher titers of acetone are achievable, let alone using the enzymes listed in the claims.
Applicants submit that furthermore, while the UniProt Sequences allegedly have 100% sequence identity to SEQ ID NOs: 7, 19, and 20, sequence identity alone does not establish functional equivalence or suggest any particular function in any particular environment, nor does it demonstrate 1) proper protein folding or stability in a heterologous host; 2) correct oligomerization of multi-subunit enzymes (e.g., transferase a/3); 3) physiological compatibility with other pathway components; or 4) activity under mesophilic conditions if derived from thermophiles. Applicants submit that none of the cited UniProt Sequences contain experimental data regarding enzyme activity, kinetics, thermodynamic stability, or compatibility in the metabolic systems described by Shaw. Applicants submit that Sequence similarity is not a proxy for predictable function. Applicants submit that the UniProt Sequences do not teach that those enzymes are interchangeable with those recited in the cited references and thus do not provide a motivation for one of ordinary skill in the art to substitute the UniProt Sequences with the methods taught in Zeldes, Shaw, or Sillers.
Applicants submit that In fact, Shaw discloses that expression of the acetone pathway from C. acetobutylicum, i.e. thiolase, acetate:acetoacetyl-CoAtransferase, and acetoacetate decarboxylase, into thermophilic T. saccharolyticum did not result in acetone production at temperatures >48°C. Shaw, p. 5, first column, 1. 1-9. Shaw teaches that "a likely issue was temperature incompatibility of the donor and host organism... ." Id. Applicants submit that Hence, Shaw teaches away from engineering thermophilic bacteria using enzymes from C. acetobutylicum, including acetoacetate decarboxylase Cac, for in vivo acetone production at thermophilic temperatures. Applicants submit that it is only Applicants' own data that shows that, contrary to Shaw's discouraging results, Cac can function in vivo in a thermophilic production platform when paired with specifically selected thiolases and Tle2, yielding the reported titers.
Applicants submit that The Office Action does not provide an articulated reason for why one of ordinary skill in the art would have a reasonable expectation of success to arrive at the claimed acetone titer by substituting the enzymes taught by the UniProt Sequences into the methods taught by Zeldes, Shaw, and Sillers. Applicants submit that simple recognition of other thiolase, CoA-transferase or acetoacetate decarboxylase sequences does not provide any reasonable expectation of success to substitute the sequences disclosed by Zeldes, Shaw, and Sillers to arrive at the claimed acetone titer.
Applicants submit that the Specification teaches that the resulting acetone titers produced by cells expressing different thiolases are extremely unpredictable. Tables 3 and 5 of the Specification provide direct experimental evidence that selection of a thiolase capable of functioning with Tle2 (Pfam No. A8F7H7/A8F7H6) and Cac (Pfam No. P23670) in a thermophilic G. thermoglucosidasius host to achieve meaningful titers of acetone and/or butanone is unpredictable. Specification, pg. 97, 99- 100/ Tables 3 and 5 show titers produced by cells expressing different thiolases from diverse thermophiles with various second enzymes (Dde2, Tle2, Ghh2 in Table 3; Tle2 in Table 5) and Cac. Id. The results vary widely, with many candidates producing very low titers (e.g., Isop_2005: 4.2 mg/L butanone and 4.2 mg/L acetone; Slip_1985: 4.1/2.1 mg/L; Tcur_2087: 1.1/0.0 mg/L), while only a small subset support comparatively higher titers (e.g., GHH_c20420: 95.5 mg/L butanone and 109.6 mg/L acetone; Slip_0880:
Applicants submit that such results were not predictable from organism of origin, homology, or prior art disclosures. Applicants submit that these data not only demonstrate that enzyme identity critically determines functional expression and pathway flux in vivo at thermophilic temperatures, and that enzyme source or sequence identity does not reliably predict catalytic performance within a heterologous thermophilic host, defeating any inference that a skilled artisan could predict success based on organism, homology, or routine substitution. Applicants submit that the experimental outcomes in Tables 3 and 5 confirm that sequence identity alone is not predictive in this art.
Applicants submit that given the lack of any reasonable expectation of success of producing a titer of 0.8 g/L given the claimed sequences, a primafacie case of obviousness has not been established.
Applicants amendment of the claims and applicants complete argument is acknowledged and has been carefully considered, however, is found non-persuasive for the reasons previously made of record and for those reasons repeated herein.
Applicants submission that the cited references combination fail to disclose or suggest the desired titers recited in the amended claims or that such high titers could be achieved is not found persuasive. In response to applicants submission that Zeldes showed an acetone titer of less than 2.5 mM. or 0.29 g/L based up0n applicants calculaltion, this is not found persuasive as stated by applicants Zeldes is not used for its platform for acetone production, rather Shaw et al. is used for such. As stated previously, one of skill in the art before the effective filing date would have been motivated to substitute the enzymes taught by Uniprot Accession No. D7CLS5 (thiolase), Uniprot Accession No. A8F7H7 (acetate-CoA transferase subunit a), Uniprot Accession No. A8F7H6 (acetate-CoA transferase subunit b) and the Adc protein from C. acetobutylicum as taught by Zeldes et al. in the methods and thus cells taught by Shaw et al. for producing acetone.
It is noted that applicants acknowledge that the methods of Shaw and Sillers both discloses an acetone titer of 0.78 g/L at 55°C and with maltodextrin as the carbon source. Shaw, Fig. 6, strain M2212. It is also noted that an acetone titer of 0.78 g/L as disclosed by both Shaw et al. and Sillers et al. is very close if not the same given standard error to an acetone titer of 0.8 g/L as claimed.
In response to applicants submission that Zeldes discloses in vitro acetone production in a cell free environment and that there is no suggestion in Zeldes of acetone production within a cell (in the presence of acetyl-CoA) and/or butanone production within a cell (in the presence of acetyl-CoA and propionyl-CoA), by the same microbial production platform, this is acknowledged, however, as stated previously and above, Zeldes is not used as a platform for the obvious methods. As stated previously, one of skill in the art before the effective filing date would have been motivated to substitute the enzymes taught by Uniprot Accession No. D7CLS5 (thiolase), Uniprot Accession No. A8F7H7 (acetate-CoA transferase subunit a), Uniprot Accession No. A8F7H6 (acetate-CoA transferase subunit b) and the Adc protein from C. acetobutylicum as taught by Zeldes et al. in the methods and thus cells taught by Shaw et al. for producing acetone.
In response to applicants submission that the cited references do not provide a motivation to substitute the claimed sequences to arrive at the claimed titer, this is not found persuasive for the reasons previously stated. As previously stated, one of skill in the art before the effective filing date would have been motivated to substitute the enzymes taught by Uniprot Accession No. D7CLS5 (thiolase), Uniprot Accession No. A8F7H7 (acetate-CoA transferase subunit a), Uniprot Accession No. A8F7H6 (acetate-CoA transferase subunit b) and the Adc protein from C. acetobutylicum as taught by Zeldes et al. in the methods taught by Shaw et al. for producing acetone. One of skill in the art before the effective filing date would have been motivated to substitute the polynucleotides encoding the above enzymes for use in the methods taught by Shaw et al. The basis of the obviousness is based upon the motivation of one of skill in the art (quoting KSR, 550 U.S. at 415, 82 USPQ2d at 1395) combining prior art elements according to known methods to yield predictable results and simple substitution of one known element for another to obtain predictable results. In view of the teachings provided in any of Zeldes et al., Shaw et al., and Sillers et al. it would be obvious for a skilled person to select a suitable combination of i) acetyl-CoA acetyltransferase, ii) acetate CoA-transferase, and iii) acetoacetate decarboxylase for providing a synthetic pathway for the production of acetone.
In response to applicants submission that the simple recognition of other thiolase, CoA-transferase or acetoacetate decarboxylase sequences does not provide any motivation to substitute the sequences disclosed by Zeldes, Shaw, and Sillers to arrive at the claimed acetone titer, this is not found persuasive for the reasons stated previously and above, one of skill in the art before the effective filing date would have been motivated to substitute the enzymes taught by Uniprot Accession No. D7CLS5 (thiolase), Uniprot Accession No. A8F7H7 (acetate-CoA transferase subunit a), Uniprot Accession No. A8F7H6 (acetate-CoA transferase subunit b) and the Adc protein from C. acetobutylicum as taught by Zeldes et al. in the methods taught by Shaw et al. for producing acetone. One of skill in the art before the effective filing date would have been motivated to substitute the polynucleotides encoding the above enzymes for use in the methods taught by Shaw et al. The basis of the obviousness is based upon the motivation of one of skill in the art (quoting KSR, 550 U.S. at 415, 82 USPQ2d at 1395) combining prior art elements according to known methods to yield predictable results and simple substitution of one known element for another to obtain predictable results. In view of the teachings provided in any of Zeldes et al., Shaw et al., and Sillers et al. it would be obvious for a skilled person to select a suitable combination of i) acetyl-CoA acetyltransferase, ii) acetate CoA-transferase, and iii) acetoacetate decarboxylase for providing a synthetic pathway for the production of acetone. Further, as both Shaw et al. and Sillers et al. disclose an acetone titer of 0.78 g/L at 55°C and with maltodextrin as the carbon source, it is noted that an acetone titer of 0.78 g/L as disclosed by both Shaw et al. and Sillers et al. is very close if not the same given standard error to an acetone titer of 0.8 g/L as claimed. Thus such is not outside the limits of an expected titer of acetone produced.
In response to applicants submission that there is also no suggestion in Zeldes that the specific enzymes recited in the claims would function sufficiently in a cellular environment, nor that their expression in a thermophilic cell would yield acetone titers >0.8 g/L or produce butanone, this is not found persuasive for the reasons previously stated and repeated above.
In response to applicants submission that while Shaw and Sillers both disclose formation of acetone by engineered bacterial cells, turning to any of those documents would not motivate one of ordinary skill in the art arrive at the invention, as none of them lists any of the organisms S. lipocalidus, C. aurantiacus and P. lettingae as possible sources for enzymes for the synthetic pathway, neither do they mention production of butanone at thermophilic conditions, this is not found persuasive for the reasons previously stated.
In response to applicants submission that applicants submission that while the UniProt Sequences allegedly have 100% sequence identity to SEQ ID NOs: 7, 19, and 20, sequence identity alone does not establish functional equivalence or suggest any particular function in any particular environment, this is not found persuasive on the basis that each of the UniProt sequence identifies the functions of each of the proteins.
In response to applicants submission that Shaw discloses that expression of the acetone pathway from C. acetobutylicum, i.e. thiolase, acetate:acetoacetyl-CoAtransferase, and acetoacetate decarboxylase, into thermophilic T. saccharolyticum did not result in acetone production at temperatures >48°C, this is not found persuasive on the basis that while every specific enzyme and/or environment may have some required limitations, the ordinary artisan would know such and be able to make required adjustments in the system for the production of acetone at the highest possible level.
In response to applicants submission that the Office Action does not provide an articulated reason for why one of ordinary skill in the art would have a reasonable expectation of success to arrive at the claimed acetone titer by substituting the enzymes taught by the UniProt Sequences into the methods taught by Zeldes, Shaw, and Sillers, this is not found persuasive for the reasons previously stated and repeated above, the expectation of success is high based upon the high level of skill in the art in the area of genetic engineering and protein expression as exemplified by the teachings of Zeldes et al., Shaw et al., and Sillers et al. Further the basis of the obviousness is based upon the motivation of one of skill in the art (quoting KSR, 550 U.S. at 415, 82 USPQ2d at 1395) combining prior art elements according to known methods to yield predictable results and simple substitution of one known element for another to obtain predictable results. In view of the teachings provided in any of Zeldes et al., Shaw et al., and Sillers et al. it would be obvious for a skilled person to select a suitable combination of i) acetyl-CoA acetyltransferase, ii) acetate CoA-transferase, and iii) acetoacetate decarboxylase for providing a synthetic pathway for the production of acetone. Further, as both Shaw et al. and Sillers et al. disclose an acetone titer of 0.78 g/L at 55°C and with maltodextrin as the carbon source, it is noted that an acetone titer of 0.78 g/L as disclosed by both Shaw et al. and Sillers et al. is very close if not the same given standard error to an acetone titer of 0.8 g/L as claimed. Thus such is not outside the limits of an expected titer of acetone produced.
Thus claim(s) 19, 21, 22, 26-28, 30-33, 35-37 is/are rejected under 35 U.S.C. 103 as being unpatentable Zeldes et al. (Biotechnology and Bioengineering, Vol 115, No. 12, pp 2951-2961, Oct 23, 2018), Shaw et al., Biotechnology for Biofuels, Vol 8:75, May 2015, Sillers et al. US 20130273555, Uniprot Accession No. D7CLS5 Aug 2020, Uniprot Accession No. A8F7H7 Aug 2020 and Uniprot Accession No. A8F7H6 Aug 2020.
Remarks
No claim is allowed.
Conclusion
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.
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rgh
4/29/2026
/RICHARD G HUTSON/Primary Examiner, Art Unit 1652
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