DETAILED ACTION
Status of the Application
Claims 1-3, 8, 10-11, 14, 17-18 are pending.
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 1-2, 8, 10, 17-18 and cancellation of claims 4-7, 19-20 as submitted in a communication filed on 3/30/2026 is acknowledged.
As indicated in the Non Final action of 1/18/2024, Applicant elected the combination of substitutions M32Y, S34T and T36E for the Fc domain, and the combination of substitutions Q31R, N96K, and A136F for the DNase domain.
Claims 8, 18 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 12/18/2023.
Claims 1-3, 10-11, 14, 17 are at issue and will be examined to the extent they encompass the elected invention.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Rejections and/or objections not reiterated from previous office actions are hereby withdrawn.
Terminal Disclaimer
The terminal disclaimer filed on 3/30/2026 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any patent granted on Application Number 17/792,101 has been reviewed and is accepted. The terminal disclaimer has been recorded.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 1/14/2026 and 3/30/2026 are acknowledged. The submissions are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Objections
Claim 1 is objected to due to the recitation of “domain comprises a variant of a polypeptide of SEQ ID NO: 1”. The term “a polypeptide of SEQ ID NO: 1” implies a genus of polypeptides of SEQ ID NO: 1. Since there is only one polypeptide of SEQ ID NO: 1, the claim should be amended to recite “domain comprises a variant of the polypeptide of SEQ ID NO: 1”. Appropriate correction is required.
Claim Rejections - 35 USC § 112(b) or Second Paragraph (pre-AIA )
Claims 1-3, 10-11, 14, 17 were 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. In view of Applicant’s amendment of claim 1, this rejection is hereby withdrawn.
Claim Rejections - 35 USC § 112(a) or First Paragraph (pre-AIA )
Claims 1-3, 10-11, 14, 17 remain 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.
This rejection has been discussed at length in the prior Office action. It is maintained for the reasons of record and those set forth below.
Applicant argues that the claims have been amended. Applicant states that the BRI must be considered in light of the specification and as it would be interpreted by one of ordinary skill in the art. Applicant states that background publications provide guidance as to a relationship for structural guiding principles for DNase I enzyme function. Applicant cites Pan et al. (J. Biol. Chem. 273(29):18374-18381, 1998; cited in the IDS) as disclosing the effect of amino acid residue modifications in enzymatic activity and actin binding. Applicant also states that Posada et al. (WO 2018/005954 published 1/4/2018; previously cited) disclose a nuclease domain and provide an in vitro assay to determine enzymatic activity. Applicant states that Pan et al. provide in Figure 1 a structural model of the DNase I-actin interface and that Posada et al. provide a mutation to reduce sensitivity to actin. Applicant states that one of skill in the art would have contemplated in view of the teachings of Minter et al. (U.S. Publication No. 2015/0104450 published 4/16/2015; previously cited) related to Fc modifications, that the present disclosure provides adequate written description. Applicant refers to specific modifications to a human IgG1 Fc associated with half-life extension. Applicant refers to specific Figures in the specification as disclosing structural and functional information regarding DNase and Fc domains variants consonant with the scope of the claimed subject matter. Applicant states that the alignment shown in Figure 5 is informative of conserved residues. Applicant is of the opinion that one of skill in the art having considered the background publications and the guidance of specification, would appreciate that the inventors were in possession of the claimed subject matter.
Applicant’s arguments have been fully considered but not deemed persuasive to overcome the instant rejection. The Examiner acknowledges the amendments made to claim 1, MPEP § 2111, the teachings of the prior art and the teachings of the specification. However, the Examiner disagrees with Applicant’s contention that the entire genus of variants required by the claims is adequately described.
With regard to the argument that the BRI must be considered in light of the specification and as it would be interpreted by one of ordinary skill in the art, it is noted that the claims as amended require domains having any structure which are variants of the human DNase1 protein of SEQ ID NO: 1 and the Fc domain of SEQ ID NO: 4. When given the broadest reasonable interpretation to the claims without importing claim limitations from the specification, the amended claims still require a genus of constructs having essentially any structure because there is no structural limitation with regard to the DNase domain and Fc domain required by the constructs claimed. The only structural limitations recited are three substitutions in the DNase domain and three substitutions in the Fc domain. Therefore, there are only 3 amino acids defined in the DNase I domain and three amino acids defined in the Fc domain. The term human DNase1 domain does not by itself convey any particular structure because it is abundantly clear that the recited DNase1 domain is not limited to a naturally-occurring human DNase1 domain but rather a variant of the polypeptide of SEQ ID NO: 1. There is absolutely no indication as to how much structural variation within the polypeptide of SEQ ID NO: 1 is required for a domain to be considered “a human DNase1 domain”. How many modifications anywhere within the polypeptide of SEQ ID NO: 1 are the most one could have in the polypeptide of SEQ ID NO: 1 before a variant of the polypeptide of SEQ ID NO: 1 is no longer considered encompassed by the term “human DNase1 domain”? With regard to the Fc domain, the claim specifically states that the Fc domain is a variant of the polypeptide of SEQ ID NO: 4, without reciting any additional structural features beyond 3 substitutions. Therefore, contrary to Applicant’s assertions, the Examiner has considered the BRI in light of the specification and as it would be interpreted by one of ordinary skill in the art.
The teachings of Pan et al. and Posada et al. are acknowledged. However, the Examiner disagrees with Applicant’s contention that the prior art provides adequate support to the entire genus of variants of the polypeptide of SEQ ID NO: 1 encompassed by the claims. The Examiner acknowledges that Pan et al. provide some functional characterization of the DNase1 protein of SEQ ID NO: 1 including the effect of certain amino acid modifications on enzymatic activity and actin binding. The Examiner also acknowledges Figure 1 of Pan et al. and the enzymatic assay to determine DNase activity. However, it is noted that the polypeptide of SEQ ID NO: 1 is 282 amino acids long and Pan et al. as well as Posada et al. only provide the functional characterization of approximately 8 substitutions, which is a very small percentage of the entire structure of the polypeptide of SEQ ID NO: 1 (2.8% = 8x100/282). Figure 1 is a mere generic 3D model of the interaction between DNase1 and G-actin and its caption provides 6 positions in the polypeptide of SEQ ID NO: 1 that are associated with hyperactivity upon substitution with a basic residue. Neither Pan et al., Posada et al. or the specification disclose or teach additional modifications, or how additional modifications could alter the 3D structure such that the hyperactivity effect associated with the substitutions disclosed could be altered by these additional modifications. Similarly, the specification of the instant application also discloses a limited number of modifications to increase DNase1 activity, and is completely silent with regard to a structure/function correlation that would allow one of skill in the art to determine which variants of the polypeptide of SEQ ID NO: 1 could be used in the claimed construct. While Applicant argues that Figure 5 provides an alignment that provides conserved regions, it is noted that conserved regions are not necessarily associated with enzymatic activity. Because conserved regions can be associated with how closely related the sources (i.e., organisms) of the proteins in the alignment are, one cannot reasonably conclude that every protein having DNase1 activity would have those conserved regions found in Figure 5.
With regard to the argument that the teachings of Minter et al. disclose Fc modifications, and that the present disclosure provides adequate written description of the genus of Fc variants required, it is noted that the protein of SEQ ID NO: 4 is 227 amino acids long and Minter et al. as well as the specification disclose a minimal number of substitutions that would extent the half-life of the Fc domain. Neither Minter et al. nor the specification disclose a structure/function correlation that would allow one of skill in the art to envision the structure of any Fc domain that could be used in the claimed construct. Therefore, for the reasons of record and those set forth above, one cannot reasonably conclude that the entire genus of constructs claimed are adequately described by the teachings of the specification and/or the prior art.
Claims 1-3, 10-11, 14, 17 remain rejected 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 construct that comprises (i) a DNase domain that comprises all of SEQ ID NO: 1 except for substitutions that correspond to substitutions Q31R, N96K and A136F in the protein of SEQ ID NO: 1, and (ii) an Fc domain that comprises all of SEQ ID NO: 4 except for substitutions that correspond to substitutions M32Y, S34T and T36E in the protein of SEQ ID NO: 4, does not reasonably provide enablement for a construct that comprises (a) a human DNase domain having any structure and three substitutions that correspond to substitutions in the protein of SEQ ID NO: 1 selected from Q31R, N96K and A136F, and (b) an Fc domain having any structure and substitutions that correspond to substitutions M32Y, S34T and T36E in the protein of SEQ ID NO: 4. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
This rejection has been discussed at length in the prior Office action. It is maintained for the reasons of record and those set forth below.
Applicant argues that the lack of enablement issue raised is based on an erroneous BRI of the claims. Applicant submits that the ample structure function analysis of background publications such as Posada et al., Pan et al. and Minter et al. and the detailed structure function relationships and extensive experimental data guided by structural models detailed in the present application demonstrates that the evidence here exceeds what is needed to satisfy the enablement requirement. Applicant states that the amount of experimentation for confirmation as to whether a variant is within the scope of the claims is not undue. Applicant submits that the assays utilized by background publications and/or in the present application to confirm activity for variants within the scope of the claims are inexpensive and rapid, thus being within the guideposts provided to examiners in United States v. Telectronics for determining whether experimentation is undue.
Applicant’s arguments have been fully considered but not deemed persuasive to overcome the instant rejection. The Examiner acknowledges the amendments made to claim 1, the teachings of the prior art and those of the specification. However, the Examiner disagrees with Applicant’s contention that the claimed invention is fully enabled by the teachings of the specification and/or the prior art.
While Applicant argues that the instant rejection has been raised based on an erroneous BRI of the claims, it is reiterated herein that the amended claims still require constructs having essentially any structure because there is no structural limitation with regard to the DNase domain and the Fc domain. The only structural limitations recited are three substitutions in the DNase I domain and three substitutions in the Fc domain. There are only 3 amino acids defined in the DNase I domain and three amino acids defined in the Fc domain. The remaining structures of the DNase domain and Fc domain required by the construct are completely undefined.
As stated above, while Applicant states that Pan et al., Posada et al. and Minter et al. provide ample structure function analysis and the specification provides detailed structure function relationships and extensive experimental data guided by structural models, it is reiterated herein that Pan et al. and Posada et al. specifically disclose a limited number of substitutions in the polypeptide of SEQ ID NO: 1 and their effect on DNase activity and actin binding. These substitutions represent approximately 2.8% of the entire structure of the polypeptide of SEQ ID NO: 1. In the case of the Fc domain, the substitutions represent 1.3% of the entire structure of the polypeptide of SEQ ID NO: 4 (1.3% = 3x100/227; SEQ ID NO: 4 has 227 amino acids). There is no disclosure of a structure/function correlation to determine which additional modifications beyond those substitutions disclosed can be made to the proteins of SEQ ID NO: 1 and 4 to obtain variants that can be used to produce the claimed construct. As explained above, there is no disclosure of how additional modifications could alter the hyperactivity effect nor half-life extension effect found with the substitutions provided.
With regard to the argument that the amount of experimentation required to enable the entire genus of variants required is not undue because the prior art and the specification provides inexpensive and fast assays to confirm activity for variants within the scope of the claims, it is noted that the argument in the instant case is not the availability of enzymatic assays or the cost associated with an enzymatic assay. Instead, the issue is the essentially infinite number of variants one of skill in the art would have to test to determine which variants can be used in the claimed construct. Contrary to Applicant’s assertions, the amount of experimentation is immense because (i) neither the specification nor the prior art disclose the structural features required in any variant of the polypeptide of SEQ ID NO: 1 so that it can have DNase1 activity, and the structural features required in any variant of the polypeptide of SEQ ID NO: 4 so that it can impart the recited construct with increased half-life, and (ii) neither the specification nor the prior art provide the structural features required in any variant of the polypeptide of SEQ ID NO: 1 having the recited 3 substitutions and any variant of the polypeptide of SEQ ID NO: 4 having the 3 recited substitutions so that they can be used in the claimed construct. Variants of the polypeptides of SEQ ID NO: 1 and 4 having 3 defined amino acids via the specific substitutions recited in claim 1 allow for any combination of 279 amino acid modifications in the polypeptide of SEQ ID NO: 1 (279 = 282-3; SEQ ID NO: 1 has 282 amino acids), and any combination of 224 amino acid modifications in the polypeptide of SEQ ID NO: 4 (224 – 227-3; SEQ ID NO: 4 has 227 amino acids). It is reiterated herein that the total number of variants of the polypeptide of SEQ ID NO: 1 having up to 279 substitutions is 282!x19279/(282-279)!/279! or 2.18x10363 variants, while the total number of variants of the polypeptide of SEQ ID NO: 4 having up to 224 substitutions is 227!x19224/(227-224)!/224! or 5.3x10292 variants. Therefore, while it is agreed that assays are available to test the desired functionality, it was not routine in the art to test by a trial and error process for an essentially infinite number of proteins to find those with the desired functional characteristics. Since there is no indication that the three substitutions recited are all that is required to have a DNase domain and an Fc domain having the desired functional characteristics, and in the absence of some knowledge or guidance as to the structural features required for the desired cleavage activity and increased half-life, one of skill in the art would have to test an infinite number of proteins to enable the entire scope of the claims. This is not deemed routine experimentation. Therefore, for the reasons of record and those set forth above, one cannot reasonably conclude that the entire scope of the claims is fully enabled by the teachings of the specification and/or the prior art.
Claim Rejections - 35 USC § 103 (AIA )
Claims 1-3, 10-11, 17 remain rejected under 35 U.S.C. 103 as being unpatentable over Posada et al. (WO 2018/005954 published 1/4/2018) in view of Minter et al. (U.S. Publication No. 2015/0104450 published 4/16/2015).
This rejection has been discussed at length in the prior Office action. It is maintained for the reasons of record and those set forth below.
Applicant argues that Posada et al. relates to the development of binuclease fusion proteins and provides no direction to the combination of the recited substitutions. Applicant submits that the Office provides no motivation to arrive to the DNase1 variant comprising the recited substitutions, namely Q31R, N96K and A136F. Applicant states that one of skill in the art would be left to limitless trials and errors to arrive to the recited combination of substitutions recited in claim 1. Applicant states that the Office has not established predictable results citing MPEP 2143(I)(B). Applicant refers to the teachings of Pan et al., which is a reference cited by Posada et al., to indicate that the combinations of substitutions Q9R+E13R+N74K, A114F, and Q9R+E13R+N74K+A114F have been previously characterized. Applicant states that hyperactive variants were characterized by Pan et al. and that the hyperactivity increases progressively with additional positive charges up to 3+, with an additional benefit if the A114F is added. Applicant refers to the combination Q9R+E13R+N74K+A114F as having a 100 fold increase in potency compared to the wild type DNAse1. Applicant states that the combination recited in the claims which corresponds to the combination Q9R+N74K, A114F results in a 2+ charge, which is not an ideal combination according to Pan et al. Applicant states that the teachings of Posada et al. also teach the E13R+N74K+A114F+T205K mutant. According to Applicant, the teachings of Posada et al. are consistent with those of Pan et al. and thus there is no basis for predictable results for a composition having the recited 3 substitutions in claim 1. Applicant states that the teachings of Miner et al. do not cure the deficiencies of Posada et al. and refer to Fc modifications. Applicant refers to a post-filing reference by Stabach et al. (JCI Insight 9(14):e177003, pages 1-21; June 18, 2024; previously cited) to show that post filing data supports the argument of superior and unexpected results associated with the claimed subject matter. Applicant refers to the findings regarding the construct ID 1833 in support of the argument that it was unexpected, based on the teachings of Pan et al., to find that a DNase1 variant that does not have a 3+ charge yields the benefits disclosed by Stabach et al.
Applicant’s arguments have been fully considered but not deemed persuasive to overcome the instant rejection. The Examiner acknowledges the amendments to claim 1, the teachings of Pan et al. and Stabach et al. and MPEP 2143(I)(B). However, the Examiner disagrees with Applicant’s contention that the combined teachings of Posada et al. in combination with those of Minter et al. do not render the claimed invention obvious.
With regard to the argument that the Office provides no motivation to arrive to the DNase1 variant comprising the recited substitutions, namely Q31R, N96K and A136F and that one of skill in the art would be left to limitless trials and errors to arrive to the recited combination of substitutions recited in claim 1, it is reiterated herein that the substitutions Q9R, N74K, and A114F in the protein of SEQ ID NO: 20 of Posada et al. correspond to substitutions Q31R, N96K and A136F in the protein of SEQ ID NO: 1 of the instant application. See alignment previously provided. On page 30, lines 6-9, Posada et al. state “For example, a mutant human DNase can include one or more of the following substitutions: Q9R, E13R, T14K, H44K, N74K, N110R, T205K. In some embodiments, the mutant human DNase also includes an A114F substitution, which reduces sensitivity to actin (see US 6348343)”. Therefore, contrary to Applicant’s assertions, Posada et al. teach the combination of these three substitutions. It is reiterated herein that based on the formula previously provided by Applicant, there are 63 combinations of the 8 substitutions disclosed by Posada et al. that comprise these three substitutions (63 = 26 -1; 6 = E13R, T14K, H44K, N110R, T205K and Q9R+N74K+A114F). This is not the case of limitless trials and errors as asserted, or a case where the combination of substitutions is suggested. Posada et al. teach the combination of substitutions recited. It is unclear to the Examiner as to how the teachings of Posada et al. do not teach the specific combination of mutations recited in the claims when Posada et al. discloses 63 combinations of substitutions that comprise the substitutions that correspond to substitutions Q31R, N96K and A136F in the polypeptide of SEQ ID NO: 1. In the instant case, a single reference (Posada et al.) provides the combination of all the substitutions recited in claim 1. It should also be noted that as correctly asserted by Applicant, the reference by Pan et al. cited by Posada et al., discloses the mutant Q9R+E13R+N74K+A114F, as a hyperactive variant (same as Q31R+E35R+N96K+A136F in the instant application). Therefore, at the time of the invention, mutants of the polypeptide of SEQ ID NO: 1 that comprise the combination of substitutions recited was already known in the art.
With regard to the argument that the teachings of Pan et al. suggest that the combination Q9R+N74K+A114F results in a 2+ charge, which is not an ideal combination, it is noted that (i) neither Pan et al. nor Posada et al. teach that a mutant that comprises the combination of substitutions Q9R+N74K, A114F does not have increased DNase activity, or that a variant that has a 2+ charge is undesirable, and (ii) the claims are not limited solely to the three substitutions as evidenced by claim 18, which includes the combination Q9R+E13R+N74K+A114F, a combination that has a 3+ charge and has 100-fold increase in potency compared to the wild type DNase 1 according to Pan et al. With regard to the argument that there is no basis for predictable results for a composition having the recited 3 substitutions in claim 1 (Q9R+N74K+A114F), it is noted that as evidenced by Pan et al., all the variants that comprise Q9R+N74K have increased DNase activity according to Table 1 of Pan et al. As taught by Posada et al., the A114F substitution (A136F in the instant application) is only associated to a reduction in sensitivity to actin. Therefore, the teachings of Pan et al. or Posada et al. do not support the argument that it is unpredictable to expect a variant comprising the three substitutions recited to have increased DNase activity compared to the wild type human DNase1 of SEQ ID NO: 1.
With regard to the arguments of unexpected results and the post-filing data of Stabach et al., it is reiterated herein that one of skill in the art did not need to know the superior properties of the 1883 construct to find a motivation to combine the teachings of Posada et al. and Minter et al. to arrive to the claimed invention. As previously indicated, a construct comprising a human DNase domain having the recited substitutions was disclosed by Posada et al. and the motivation to replace the Fc domain in the constructs of Posada et al. with an Fc domain having the recited substitutions is found in the fact that Minter et al. teach that an Fc domain that comprises the YTE mutation, such as the Fc domain of SEQ ID NO: 59, provides an extended in vivo half-life that may improve therapeutic efficacy and/or may allow therapeutic benefits to be achieved at reduced or less frequent dosage. Minter et al. specifically teach an Fc domain having substitutions that correspond to substitutions M32Y, S34T and T36E in the protein of SEQ ID NO: 4, namely the Fc domain of SEQ ID NO: 59, which when linked to a therapeutic protein (CTLA-4) increased the stability and in vivo half-life of said therapeutic protein. This finding alone would have strongly motivated one of skill in the art to replace the Fc domain of Posada et al. with the Fc domain of Minter et al., thus arriving to the claimed invention. Therefore, the claimed construct is obvious because it was suggested by the prior art even though the particular benefit asserted by Applicant was not disclosed in the prior art. See MPEP 2144.09 (VII). Moreover, Table 2 of the Stabach reference discloses several constructs having the substitutions corresponding to substitutions Q31R, N96K and A136F in the polypeptide of SEQ ID NO: 1 and not all of these constructs have the same therapeutic effect. In addition, the 1833 construct has more than the three substitutions recited in claim 1. As such, one cannot reasonably conclude that the “unexpected” results obtained from the 1833 construct are solely associated to these three substitutions.
Claim 14 remains rejected under 35 U.S.C. 103 as being unpatentable over Posada et al. (WO 2018/005954 published 1/4/2018 in view of Minter et al. (U.S. Publication No. 2015/0104450 published 4/16/2015) and further in view of Sam et al. (Journal of Bioscience and Bioengineering 126(1):102-110, 2018).
This rejection has been discussed at length in the prior Office action. It is maintained for the reasons of record and those set forth below.
Applicant argues that the teachings of Posada et al., Minter et al. and Sam et al. fail to provide a suggestion or motivation to combine the references so as to produce the construct of claim 1. Applicant refers to the arguments previously presented with regard to Posada et al. and Minter et al. and states that Sam et al. do not cure the deficiencies of Posada et al. and Minter et al. Applicant states that claim 14 ultimately depends from claim 1 and should be free from rejection as amended claim 1 is also free from rejection for the reasons previously stated above.
Applicant’s arguments have been fully considered but not deemed persuasive to overcome the instant rejection. The Examiner acknowledges the amendments made to claim 1. However, the Examiner disagrees with Applicant’s contention that the teachings of Posada et al. and Minter et al. do not render the construct of claim 1 obvious over the prior art. See extensive discussion above as to the reasons why the invention of claim 1 is obvious over the teachings of Posada et al. and Minter et al. With regard to the argument that the teachings of Sam et al. do nothing to cure the deficiencies of Posada et al and Minter et al. and provide no motivation to combine the references to arrive to the construct of claim, it is noted that the teachings of Sam et al. were introduced to show that glycoproteins that comprise α(2,6) linked sialic acids would be more appropriate for the development of biopharmaceuticals for human use and that a CHO cell transfected with a human ST6GAL-1 gene to produce proteins having this type of glycosylation was known in the art at the effective filing date of the claimed invention. Therefore, for the reasons of record and those set forth above, one of skill in the art would conclude that the claimed invention is obvious over the prior art of record.
Double Patenting
Claims 1-5, 10-11, 14, 17 were provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 57-75 of copending Application No. 17/792,101. In view of Applicant’s submission of a terminal disclaimer disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any patent granted on Application Number 17/792,101, this rejection is hereby withdrawn.
Conclusion
No claim is in condition for allowance.
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 extension fee 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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Any inquiry concerning this communication or earlier communications from the examiner should be directed to DELIA M RAMIREZ, Ph.D., whose telephone number is (571) 272-0938. The examiner can normally be reached on Monday-Friday from 8:30 AM to 5:00 PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert B. Mondesi, can be reached at (408) 918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
/DELIA M RAMIREZ/Primary Examiner, Art Unit 1652
DR
June 23, 2026
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