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 .
Claims Status
The amendments and remarks filed 07/25/2025 are acknowledged and entered.
Claims 1, 3, 11-15, 17, and 19-27 are pending.
Claims 1, 3, 17, and 19 are amended.
Claims 2, 4-10, 16, 18, and 27 are canceled.
Claims 3, 21-23, and 25-27 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claims. Election was made without traverse on 12/19/2023.
Claims 1, 11-15, 17, 19-20, and 24 are under examination.
Withdrawn
The rejections of claims 17 and 19 under 35 U.S.C. 112(b) are withdrawn. Applicant has amended the claims to overcome the rejections.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 07/25/2025 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Maintained Rejections
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This rejection has been modified solely to address the amendment to claim 1 requiring that the first Fc domain and/or the second Fc domain comprise one or more mutations that permit heterodimerization.
Claims 1, 11-14, 17, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Bai (WO 2016073704; 05/02/2024 PTO-892) in view of Lo et al., 1998 (04/25/2025 PTO-892), Timans et al., 2004 (US 20040198955; 10/18/2024 PTO-892), and Kim (WO 2018030806; 04/25/2025 PTO-892).
Regarding claims 1 and 17, Bai teaches an IL27Fc fusion protein comprising a signal peptide, EB13, a PV or GS linker (flexible linker), P28, and Fc domain (first polypeptide chain) in N- to C- terminal orientation [0185; Figure 10A]. See below:
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Since this structure comprises only one EBI3 and one p28, this meets the limitation of “monovalent” as defined by Applicant as an IL27 receptor agonist that has only a single IL27 heterodimer (i.e., one EBI3xp28 heterodimer) [see 0061 of the instant specification]. Further, the p28 moiety necessarily comprises an IL27Rα binding domain and a gp130 binding domain of p28, and the EBI3 moiety necessarily comprises a p28 binding domain of EBI3 because these are inherent properties of p28 and EBI3. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)).
Further, Bai teaches that the fusion protein comprises a wild type human p28 peptide (residues 28-243 of SEQ ID NO: 142) [0048]. Thus, since the p28 moiety necessarily comprises an IL27Rα binding domain and a gp130 binding domain of p28 because this is an inherent property of p28, then this wild type human p28 peptide of Bai also necessarily comprises 95% sequence identity to an IL27Rα binding domain and/or a gp130 binding domain of a human p28 protein.
SEQ ID NO: 142 of Bai has 100% sequence identity to residues 28-243 of SEQ ID NO: 2 of the instant claim, which correspond to the amino acid sequence of interleukin-27 subunit alpha (p28) as evidenced by UniProt, 2020 (instant PTO-892) [see pages 4-5]. Thus, as the examiner stated above, and since SEQ ID NO: 2 of the instant claim comprises a wild type human p28 moiety, the p28 peptide of Bai necessarily comprises an amino acid sequence having at least 95% sequence identity to an IL27Ra binding domain and/or a gp130 binding domain of SEQ ID NO: 2.
However, Bai does not specifically teach that the first polypeptide chain comprises in N- to C-terminal orientation: (a) a first Fc domain; (b) the EBI3 moiety; and (c) the p28 moiety, that the EBI3 moiety comprises an amino acid sequence having at least 95% sequence identity to a p28 binding portion of SEQ ID NO: 1, or that the IL27Fc fusion protein comprises a second polypeptide chain comprising a second Fc domain associated with the first Fc domain to form an Fc heterodimer, wherein the first Fc domain and/or second Fc domain comprise one or more mutations that permit heterodimerization.
Lo teaches that the use of a signal-peptide-Fc as an N-terminal fusion partner can ‘fool’ the cellular processes to express and secrete many different types of proteins at a high level and that this fusion approach is superior to an X-Fc construct (i.e. C-terminal Fc) because the use of Fc at the N-terminus ensures that the Fc-X is directed efficiently through the secretory pathway [page 499, left column, second paragraph]. Lo further teaches that overall, the Fc-X construct (i.e. N-terminal Fc) achieves high level expression of proteins [page 499, right column, fourth paragraph].
Timans teaches SEQ ID NO: 10, which is the polypeptide sequence of EBI3 [0058].
SEQ ID NO: 10 of Timans has 100% sequence identity to SEQ ID NO: 1 of the instant claim.
Kim teaches heterodimeric Fc-fused proteins comprising a first Fc region and a second Fc region of a Fc region pair of an immunoglobulin while a subunit of a biologically active protein is bound to at least one of N-terminal or C-terminal of the first Fc region and/or the second Fc region, and the protein can be fused to the Fc [see Abstract]. Further, Kim teaches that the use of the heterodimeric Fc-fused proteins remarkably increases the in vivo half-life of a biologically active protein contained in the heterodimeric Fc-fused protein, and thus, various types of biological activities can be maintained for a long time in the body [see Abstract]. Kim also teaches that heterodimer Fc-based heterodimeric proteins (e.g. IL27) can be prepared by the structures below:
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[see page 32, Figure 2 of Kim]. Kim further teaches that the first Fc region and the second region are mutated so as to promote the formation of heterodimers [see paragraph 3].
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the IL27Fc fusion protein as taught by Bai to have the first Fc domain be an N-terminal Fc, as taught by Lo, thereby arriving at an IL27 fusion protein comprising a first polypeptide chain comprising in an N- to C- terminal orientation: the first Fc domain, the EBI3 moiety, and the p28 moiety. One would have been motivated to make this modification because Lo teaches that an N-terminal Fc (i.e. Fc-X construct) is superior to a C-terminal Fc (X-Fc construct) because it ensures that the Fc-X is directed efficiently through the secretory pathway and achieves high level expression of proteins. There would be a reasonable expectation of success in making this modification because this is a known structure in the art for Fc fusion proteins, as taught by Lo.
It further would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the EBI3 moiety of the IL27Fc fusion protein of Bai to specifically be the EBI3 as taught by Timans. One would have been motivated to use this sequence for the EBI3 moiety because it is a known sequence in the art, and it is obvious to use known variations in the prior art for predictable outcomes. See MPEP 2143 (F).
Additionally, it would have been obvious to modify the IL27Fc fusion protein of Bai to further comprise a second polypeptide chain comprising a second Fc domain associated with the first Fc domain to form an Fc heterodimer wherein the first Fc domain and/or second Fc domain comprise one or more mutations that permit heterodimerization, as taught by Kim. One would have been motivated to make this modification because Kim teaches that the use of the heterodimeric Fc-fused proteins remarkably increases the in vivo half-life of a biologically active protein contained in the heterodimeric Fc-fused protein. There would be a reasonable expectation of success in making this modification because this is a known structure in the art for heterodimeric Fc fusion proteins, as taught by Kim.
Claim 11 is included in this rejection because Bai teaches that Fc portion may comprise the hinge region and CH2 and CH3 domains of the human IgG1, IgG2, IgG3, IgG4, or IgA [0066]. Rath also teaches that the Fc domain comprises a hinge domain [see page 242, Figure 4].
Claims 12 and 14 are included in this rejection because Bai teaches that the use of IgG1 in the fusion protein is an exemplary IgG isotype source for an IgG Fc, and that other Fc subclasses may also be used based on the same design depicted in Figure 10 [0187]. Bai further teaches that the Fc domain can be human IgG1, IgG2, IgG3, and IgG4 [0066].
Claim 13 is included in this rejection because Bai teaches that the Fc region can be modified by replacing one or more amino acid residues with different amino acid residues to alter the effector functions of the Fc, such that the Fc portion is deficient (reduced) binding an Fcy receptor [0067].
Claim 24 is included in this rejection because Bai teaches a pharmaceutical composition comprising the fusion protein of the present disclosure formulated in any pharmaceutically acceptable carrier(s) or excipient(s) [0146].
Claims 1, 11-15, 17, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Bai (WO 2016073704; 05/02/2024 PTO-892) in view of Lo et al., 1998 (04/25/2025 PTO-892), Timans et al., 2004 (US 20040198955; 10/18/2024 PTO-892), and Kim (WO 2018030806; 04/25/2025 PTO-892), as applied to claims 1, 11-14, 17, and 24 above, and further in view of Rudge et al., (WO 2018058001; 05/02/2024 PTO-892).
The teachings of Bai, Lo, Timans, and Kim are above.
However, Bai, Lo, Timans, and Kim do not specifically teach that the Fc domain comprises the amino acid sequence of SEQ ID NO: 80.
Regarding claim 15, Rudge teaches SEQ ID NO: 1929, which is an antibody heavy chain constant region Fc domain [0169].
SEQ ID NO: 1929 of Rudge has 100% sequence identity to SEQ ID NO: 80 of the instant claim.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the first Fc domain in the IL27Fc fusion protein as taught by Bai, Lo, Timans, and Kim, to specifically be the Fc domain as taught Rudge. One would have been motivated to use this known sequence for the Fc domain because it is a known sequence in the art, and it is obvious to use known variations in the prior art for predictable outcomes. See MPEP 2143 (F).
Claims 1, 11-14, 17, 19, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Bai (WO 2016073704; 05/02/2024 PTO-892) in view of Lo et al., 1998 (04/25/2025 PTO-892), Timans et al., 2004 (US 20040198955; 10/18/2024 PTO-892), and Kim (WO 2018030806; 04/25/2025 PTO-892), as applied to claims 1, 11-14, 17, and 24 above, and further in view of UniProt, 2020 (instant PTO-892).
The teachings of Bai, Lo, Timans, and Kim are above.
However, Bai, Lo, Timans, and Kim do not specifically teach that the p28 moiety has an amino acid sequence with at least 95% sequence identity to SEQ ID NO: 2.
Regarding claim 19, UniProt teaches the sequence of IL27A (p28) [see page 8].
The sequence of UniProt has 100% sequence identity to SEQ ID NO: 2 of the instant claim.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the p28 moiety in the IL27Fc fusion protein as taught by Bai, Lo, Timans, and Kim, to specifically be the p28 moiety as taught by UniProt. One would have been motivated to use this sequence for the p28 moiety because it is a known sequence in the art, and it is obvious to use known variations in the prior art for predictable outcomes. See MPEP 2143 (F).
Claims 1, 11-14, 17, 20, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Bai (WO 2016073704; 05/02/2024 PTO-892) in view of Lo et al., 1998 (04/25/2025 PTO-892), Timans et al., 2004 (US 20040198955; 10/18/2024 PTO-892), and Kim (WO 2018030806; 04/25/2025 PTO-892), as applied to claims 1, 11-14, 17, and 24 above, and further in view of Rousseau et al., 2010 (05/02/2024 PTO-892).
The teachings of Bai, Lo, Timans, and Kim are above.
However, Bai, Lo, Timans, and Kim do not specifically teach that the IL27 receptor agonist has a variant p28 domain (b) comprising an amino acid sequence with at least 95% sequence identity to a gp130 binding domain of SEQ ID NO: 2 and one or more amino acid substitutions at the position corresponding to: (iii) amino acid W197 of full length human p28 or amino acid W195 of full length murine p28.
Regarding claim 20, Rousseau teaches introducing a W197A mutation into IL-27p28 and that this mutant was still able to interact with EBI3 (has IL27 activity), and did not have significant alterations to the IL-27p28 folding and structure [page 19422, right column, second paragraph]. Rousseau further teaches that the W197A IL-27 antagonist decreased the cell proliferation and STAT-1/STAT-3 tyrosine phosphorylation observed in response to IL-27 [page 19423, left column, first paragraph]. Rousseau also teaches a mouse equivalent of human W197A IL-27, murine W195A IL-27, and that the W195A mutant was able to antagonize the endogenous wild-type IL-27 in vivo and subsequently neutralize part of the liver inflammatory cascade [page 19423, left column, fourth paragraph – right column, second paragraph]. Rousseau further teaches that IL-27 antagonists can be used to down-modulate acute IL-27-driven Th-cell-mediated immune response [see Abstract].
While Rousseau teaches that the W197A mutation is antagonistic, and the claims are drawn to an IL27 receptor agonist, this still meets the limitation of the claimed structure. Applicant defines “IL27 receptor agonist” as a molecule comprising or consisting of an IL27 mutein and which has IL27 activity, where the IL27 activity can be greater than, lower than, or equal to the activity of wild type or recombinant IL27 [0050]. Thus, since the art teaches the claimed structure, then it must also have the same function. See MPEP 2112.01(II) which states “if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.”
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the IL27Fc fusion protein, as taught by Bai, Timans, and Kim, to comprise an amino acid substitution of W197A of full length human p28 or an amino substitution of acid W195A of full length murine p28, as taught by Rousseau. One would have been motivated to make this modification because Rousseau teaches that this mutation decreased the cell proliferation and STAT-1/STAT-3 tyrosine phosphorylation observed in response to IL-27, neutralizes part of the liver inflammatory cascade, and that IL-27 antagonists can be used to down-modulate acute IL-27-drive Th-cell-mediated immune response.
Response to Arguments
The rejections of claims 1, 11-15, 17, 19, 20, and 24 under 35 U.S.C. 103 over Bai, Timans, Kim, Lo, Rudge, UniProt, and Rousseau are maintained. On pages 8-9 of the remarks, Applicant argues that Kim only recites IL-27 twice, that IL-12 is the most preferred bioactive protein of the invention, and that a skilled artisan, to arrive at a molecule comprising an Fc heterodimer which is monovalent for IL27, would have to first select IL-27 from the list of proteins, then select a specific configuration from those depicted in Figure 2, and then further select a particular N- to C- terminal order of IL27 components, without any motivation or suggestion for making such selections. In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). These arguments are not persuasive because the Examiner only relied upon the teachings of Kim for the motivation as to why one skilled in the art would want to modify the protein of Bai to comprise a second Fc domain associated with the first Fc domain (of Bai) to form a heterodimeric Fc-fused protein. Additionally, alternatives are not an indication of nonobviousness and disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments. In re Susi, 440 F.2d 442, 169 USPQ 423 (CCPA 1971). See MPEP 2123. Applicant has not provided any objective evidence as to why one would avoid using the heterodimeric Fc structure of Kim with the protein of Bai, and the Examiner clearly articulated that there would have been a reasonable expectation of success in making this modification to the protein of Bai because this is a known structure in the art for heterodimeric Fc fusion proteins. See rejection above.
On page 9 of the remarks, Applicant argues that although Figure 2 generically depicts molecules having various heterodimeric configurations, Kim describes generation and evaluation of only a single type of heterodimeric molecule, named “mono-IL2-Fc” and that no data or results related to biological or other functional activity is provided for any other construct having an Fc heterodimer. Applicant further argues that the mono-IL12-Fc of Kim contains IL12, not IL27, each subunit is on a different polypeptide chain, and each subunit is present N-terminal to the Fc domains. Again, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). To reiterate, the Examiner did not rely upon Kim to teach the protein that is monovalent for IL27, but rather, relied upon the teachings of Kim for the motivation as to why one skilled in the art would want to modify the protein of Bai to comprise a second Fc domain associated with the first Fc domain (of Bai) to form a heterodimeric Fc-fused protein and do so with a reasonable expectation of success. These arguments are further not found persuasive because disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments (In re Susi, 440 F.2d 442, 169 USPQ 423 (CCPA 1971); see MPEP 2123), working examples are not required, and prior art is presumed enabled (see MPEP 2121). Additionally, while Kim did not test the biological or functional activity of other Fc heterodimer constructs, it is noted that the features upon which applicant relies (i.e., biological or functional activity) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Moreover, this does not undermine that one would have been motivated, with a reasonable expectation of success, to modify the protein of Bai to comprise the heterodimeric Fc fusion protein structure of Kim, as taught in Figure 2.
On page 10 of the remarks, Applicant continues to argue the mono-IL2-Fc construct as depicted in Figure 10(b) of Kim, stating that the construct has increased immune cell proliferation and increased tumor control, but also has reduced IL-12 signaling activity as compared to a bi-IL2-Fc, and that the starting point for any modifications to the IL27Fc fusion proteins of Bai would naturally have been the protein actually generated and characterized by Kim (i.e. the mono-IL12-Fc depicted in Figure 10). This is not found persuasive because again, art is art for all that it teaches and reduction to practice is not required. See MPEP 2121 and 2123. The structure of Figure 10 is a completely different structure than the one the Examiner relied upon in the rejection and Kim still explicitly teaches that the structures depicted in Figure 2, inclusive of the structure the Examiner did rely upon in the rejection, increases the in vivo half-life of a biologically active protein contained in the heterodimeric Fc-fused protein. Applicant further argues on page 11 that Timans fails to teach or suggest any protein which is monovalent for IL27 and comprises and Fc heterodimer. In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
On page 11 of the remarks, Applicant argues surprising and unexpected properties relating to a protein having the configuration as recited in instant claim 1, pointing to Table 7, page 157 of the specification, stating the protein had greater signaling activity relative to other constructs. This is not found persuasive because the features upon which applicant relies (i.e., greater signaling activity) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). Further, even if the claims did recite the alleged feature of greater signaling activity, the table does not depict results of a protein with the p28 and EBI3 on a single polypeptide chain with a homodimeric Fc domain. Therefore, the Examiner cannot make a determination of a trend that would lead to a conclusion of unexpected results. The burden is on Applicant to provide to the Examiner a trend proving the unexpected results. See MPEP 716.02(b). In view of the above, Applicant’s arguments of unexpected results are not persuasive to rebut the 103 rejection. Additionally, Applicant continues to argue the mono-IL12-Fc construct of Kim. The Examiner reiterates that this construct was not relied upon in the rejection and arguments pertaining to this specific disclosure of Kim have been thoroughly addressed above, will not be reiterated, and are incorporated herein.
On page 12 of the remarks, Applicant argues that the reference of Lo fails to cure the deficiencies of Bai, Kim, and Timans, and does not teach or suggest IL27 or any heterodimeric molecule. This is not found persuasive because no such deficiency exists. See above. Further, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Applicant again argues the alleged surprising and unexpected results, which have been addressed above and will not be reiterated and are incorporated herein. Further on page 12 of the remarks, Applicant argues that the reference of Rudge fails to cure the deficiencies of Bai, Kim, and Timans, and does not teach or suggest any molecule comprising IL27 at all, let alone the protein as recited in claim 1. This is not found persuasive because no such deficiency exists. See above. Further, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
On page 13 of the remarks, Applicant argues that the reference of UniProt fails to cure the deficiencies of Bai, Kim, and Timans, and does not teach or suggest any molecule comprising IL27 at all, let alone the protein as recited in claim 1. This is not found persuasive because no such deficiency exists. See above. Further, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Additionally on page 13 of the remarks, Applicant argues that the reference of Rousseau fails to cure the deficiencies of Bai, Kim, and Timans, and does not teach or suggest any molecule comprising IL27 and an Fc domain, let alone the protein as recited in claim 1. This is not found persuasive because no such deficiency exists. See above. Further, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
Conclusion
No claims are allowed.
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 Brittney E Donoghue whose telephone number is (571)272-9883. The examiner can normally be reached Mon - Fri 7:30 - 3:30.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at (571) 272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/B.E.D./Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675