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
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. This application is a 371 of PCT/US2021/040061 filed July 1, 2021, which claims the benefit of US Provisional Application No. 63/047,681 filed July 2, 2020. All claims have been given an effective filing date of July 2, 2020.
Election/Restriction
Applicant's election without traverse of Group I (Claims 1-4, 6, 14-16, 30, 32, 43, 56-58, 65, 69, 76, 80-81, 84, 86-87, 89-90, 93, 95-96, 100, 108-110, 113, 117-118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163) in the reply filed on December 22, 2025 is acknowledged.
Applicant’s species election of:
T3A, H16A, E61R, P65R, D84Y, C125S
SEQ ID NO: 270
Fc pair SEQ ID NOs: 48 and 64
Acute lymphoblastic leukemia (ALL)
in the reply filed on December 22, 2025 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the species election requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Claims 3, 6, 15-16, 30, 32, 43, 57-58, 164, 166, 168, 170, and 176-177 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions or species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on December 22, 2025.
Upon further consideration, Examiner withdraws the restriction requirement between the pending claims and Claims 3, 6, 15-16, and 57-58 as set forth in the Office action mailed on 09/25/25. Claims 3, 6, 15-16, and 57-58 are hereby rejoined and fully examined for patentability. In view of the withdrawal of the restriction requirement, applicant(s) are advised that if any claim presented in a divisional application is anticipated by, or includes all the limitations of, a claim that is allowable in the present application, such claim may be subject to provisional statutory and/or nonstatutory double patenting rejections over the claims of the instant application.
Claim Status
Claim listing filed on December 22, 2025 is pending. Claims 4-5, 7-13, 17-29, 31, 33-42, 44-55, 59-79, 82-83, 85, 88-89, 91-92, 94, 97-99, 101-107, 111-112, 114-116, 119, 121-128, 130-131, 133-141, 145-147, 149-152, 155-157, 159-162, 165, 167, 169, 171-175, and 178-188 are canceled. Claims 1, 3, 57, 90, and 117 are amended. Claims 30, 32, 43, 164, 166, 168, 170, and 176-177 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions or species. Claims 1-3, 6, 14-16, 56-58, 80-81, 84, 86-87, 90, 93, 95-96, 100, 108-110, 113, 117-118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163 are examined upon their merits.
Information Disclosure Statement
The information disclosure statements filed on 12/20/2022, 07/18/2023, 11/17/2023, 01/19/2024, 02/13/2024, 01/17/2025, and 12/22/2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Specification
The disclosure is objected to because of the following informalities: first line of paragraph [00228] recites "Example 16were" and there should be a space between “16” and “were” to recite “Example 16 were.”
The disclosure is objected to because the sequence listing is not incorporated by reference at the beginning of the specification. MPEP § 2413.04 states that since the "Sequence Listing XML" is not the text of the specification, but rather is sequence data in an XML file format, an incorporation by reference statement is needed to ensure that the content of the "Sequence Listing XML," submitted to the USPTO as an XML file, is considered part of the disclosure capable of providing 35 U.S.C. 112(a) support for the disclosure and any claims relating to nucleotide and/or amino acid sequences. The required incorporation by reference statement identifies: (i) the name of the file; (ii) the date of creation of the file; and (iii) the size of the file in bytes.
The abstract of the disclosure is objected to because line 1 recites “provided herein are polypeptide comprising a modified IL-2” and “provided herein are polypeptides comprising a modified IL-2” with “polypeptides” plural is correct. A corrected abstract of the disclosure is required and must be presented on a separate sheet, apart from any other text. See MPEP § 608.01(b).
Appropriate correction is required.
Claim Objections
Claim 148 is objected to because of the following informalities: lines 4-5 recite “wherein each Fc region comprises a mutations M252Y and M428L” and “wherein each Fc region comprises mutations M252Y and M428L” with the “a” deleted is correct. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 2, 14, 56, 118, 120, 153, and 158 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 2 recites “reduced affinity” and Claims 14 and 56 recite “reduces affinity.” It is clear that binding affinity can be measured by means known in the art prior to filing such as KD (specification paragraph [0065]), and the reduction is in comparison to wild-type IL-2; however, it is unclear what is encompassed by “reduce.” This term is indefinite relative terminology because it is unclear what the threshold of “reduce” is (MPEP § 2173.05(b)). The specification teaches that in some embodiments “reduce” means an overall decrease of 10% or greater, and in other embodiments “reduce” means an overall decrease of 50% or greater (paragraph [00100]). This definition lists non-limiting examples of the threshold of “reduce” in different scenarios, and one of ordinary skill would not understand the metes and bounds of “reduced affinity” as recited in the claims. For example, would prior art that recites a 20% reduction in binding affinity anticipate the instant claim limitations? Does the claim language encompass reductions that are not statistically significant? Due to the relative terminology of “reduce,” Claims 2, 14, and 56 are rejected as being indefinite.
Claim 14 recites “at least one substitution that recues affinity for CD132” and Claim 56 recites “at least one substitution that reduces affinity for CD25.” These phrases are considered functional language because the feature (a substitution) is defined by what it does (reduces affinity to CD132 or CD25) rather than by what it is (MPEP § 7173.05(g)). To determine if functional language is ambiguous, the following factors are considered: (1) whether there is a clear-cut indication of the scope of the subject matter covered by the claim; (2) whether the language sets forth well-defined boundaries of the invention or only states a problem solved or a result obtained; and (3) whether one of ordinary skill in the art would know from the claim terms what structure or steps are encompassed by the claim. These factors are examples of points to be considered when determining whether language is ambiguous and are not intended to be all inclusive or limiting (MPEP § 7173.05(g)). The instant claims recite a result obtained without any required structure. One of ordinary skill would not know from the claim terms what IL-2 substitutions are encompassed by the claims. Therefore, the metes about bounds of these substitutions cannot be readily determined, and Claims 14 and 56 are rejected as being indefinite for functional language.
Claim 118 recites wherein the polypeptide comprises at least one “antigen binding domain”; Claim 120 recites wherein the antigen binding domain specifically binds to a T-cell antigen, PD-1, or is an agonist or antagonist; and Claim 158 recites a first and second “antigen binding domain.” The phrase “antigen binding domain” is considered indefinite functional language because the feature (the domain) is defined by what it does (binds an antigen or is an agonist/antagonist) rather than by what it is (MPEP § 7173.05(g)). There are no structural limitations for the domain. The specification defines that the terms “antibody” and “antigen binding molecule” are used interchangeably in the broadest sense and encompass various polypeptides that comprise antigen binding domains including but not limited to conventional antibodies, single-domain antibodies, VHH-containing polypeptides, and fragments thereof (paragraph [0056]). This definition lists non-limiting examples of antibodies/antigen binding molecules but provides no structural definition for “antigen binding domains.” The broadest reasonable interpretation of “antigen binding domain” is that the domain can comprise any structure (antibody VH and VL domains, T-cell receptors, B-cell receptors, major histocompatibility complex molecules, etc.) as long as it functionally binds an antigen. Because the structural metes and bounds of “antigen binding domain” are unclear, Claims 118, 120, and 158 are rejected for indefiniteness. Note, Claims 129 and 132 are not rejected for indefiniteness because they recite structural limitations for the antigen binding domains.
Claim 153 recites the limitation "each Fc region" in line 1. There is insufficient antecedent basis for this limitation in the claim, because no Fc regions are defined in the claims upon which Claim 153 depends. Claim 153 is rejected for indefiniteness.
Note, Claim 2 recites “wherein the modified IL-2 has reduced affinity for CD122 compared to wild-type IL-2,” and this functional property is considered inherent to the structure of the modified IL-2 recited in Claim 1 (MPEP § 2112.01). Similarly, Claim 143 recites wherein the modified IL-2 binds a human IL-2R with an affinity at least 2-fold lower than the affinity of human wild-type IL-2, and this functional property is considered inherent to the structure of the modified IL-2 recited in Claim 1. In Claim 143, it is interpreted that “at least” precedes “3-fold, 4-fold, 5-fold, 6-fold, 7-fold, 8-fold, and 9-fold.” The Fc region substitutions in Claims 100 and 148 are interpreted in relation to Kabat amino acid numbering (specification paragraph [0042]).
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL. —The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1-3, 6, 14-16, 56-58, 80-81, 84, 87, 90, 93, 95-96, 100, 108-110, 113, 118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 1 is directed to a polypeptide comprising a modified IL-2 comprising substitutions H16A, E61R, P65R, and D84Y. Claims 3, 6, 15-16, and 57-58 recite wherein the modified IL-2 can comprise a genus of further amino acid substitutions at various residues. Claims 14 and 56 recite wherein the modified IL-2 can further comprise any substitutions that reduce affinity for CD132 or CD25. Claim 90 recites wherein the modified IL-2 comprises at least 90% identity to an amino acid sequence selected from SEQ ID NOs: 160 and 270-277. Claims 108 and 153 recite wherein the Fc region comprises at least 90% identity to an amino acid sequence selected from SEQ ID NOs: 47-83, 292, and 293. Claims 118, 120, 129, and 158 are directed to a genus of possible antigen binding domains. “At least 90% sequence identity” means that 10% of the amino acid residues can be inserted, deleted, or substituted with conservative or non-conservative changes. For example, 10% variation in SEQ ID NO: 270 (Claim 90) means that 13 amino acid residues can be altered in any combination (10% of 133 amino acid residues). Overall, the claims are directed to a genus of modified IL-2 polypeptides that comprises substantial amino acid variation in addition to a genus of possible Fc regions and a genus of possible antigen binding domains. The claims broadly encompass thousands of modified IL-2 polypeptides and fusion proteins thereof.
In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112, first paragraph, it is necessary to understand what Applicant has possession of and what Applicant is claiming. In order to provide adequate written description and evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof.
The specification evaluates nine species of modified IL-2 that comprise the required substitutions of Claim 1: SEQ ID NOs: 160 and 270-277 (Table 14 on page 87). Across SEQ ID NOs: 160 and 270-277, only five additional mutations are evaluated: L19A, L19N, M23T, E95Q, and S127D. Note, T3A and C125S mutations are also included but these substitutions are well understood in the art to improve stability without affecting biological function. Five additional IL-2 mutations are not sufficient to describe the genus of possible modified IL-2 polypeptides that are encompassed by the claims (10% variation or any substitution at residues L19, M23, N88, E95, Q22, R120, T123, Q126, S127, I129, S130, K43, Y45, I114, F42, R38, and/or L72). The specification specifically teaches that adding or removing one amino acid substitution can substantially alter function, and the effects of combining individual mutations are difficult to predict (paragraph [00233] and Table 14).
Further, the specification fails to teach how the Fc regions can be modified other than the “knobs-into-holes,” half-life extending, and effector null Fc region mutations understood in the art prior to filing (specification paragraphs [00135]-[00137]). No guidance is provided for how 10% of the Fc regions can be inserted, deleted, or substituted (Claims 108 and 153) other than these limited sets of known mutations, and 10% variation in SEQ ID NO: 48 comprises altering any combination of 22 amino acid residues (10% of 223 amino acids). Pertaining to the claimed genus of antigen binding domains, the specification teaches IL-2 fused to an anti-LAG3 VHH (Example 14), a PD-1-binding VHH (Example 25), a NKp46-binding VHH (Example 25), a CD8a-binding VHH (Example 25), and a γδTCR-binding VHH (Examples 27-28). However, five structural examples of antigen binding domains do not adequately represent the claimed genus of antigen binding domains that comprises any domain structure and binding to any antigen.
A "representative number of species" means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. See AbbVie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (MPEP § 2163.05.Ib). In the absence of sufficient recitation of distinguishing identifying characteristics or structure-to-function attributes for the entire genus of modified IL-2 polypeptides and fusion proteins thereof, the specification does not provide adequate written description of the claimed genera. Therefore, in view of the case law directed to an appropriate number of representative species, claims 1-3, 6, 14-16, 56-58, 80-81, 84, 87, 90, 93, 95-96, 100, 108-110, 113, 118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163 are rejected for insufficient written description.
Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. § 112 is severable from its enablement provision (see page 1115).
Claims 1-3, 6, 14-16, 56-58, 80-81, 84, 87, 90, 93, 95-96, 100, 108-110, 113, 118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163 are 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 the specific species of modified IL-2 polypeptides comprising SEQ ID NOs: 160 and 270-277 (Claims 86 and 117), does not reasonably provide enablement for the genus of modified IL-2 polypeptides comprising substantial amino acid variation and fusion proteins thereof comprising substantial variation in Fc regions and antigen binding domains. 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 use the invention commensurate in scope with these claims.
MPEP § 2164.01(a) states that there are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure
does not satisfy the enablement requirement and whether any necessary experimentation is
“undue”. These factors include, but are not limited to:
A) The breadth of the claims;
(B) The nature of the invention;
(C) The state of the prior art;
(D) The level of one of ordinary skill;
(E) The level of predictability in the art;
(F) The amount of direction provided by the inventor;
(G) The existence of working examples; and
(H) The quantity of experimentation needed to make or use the invention based on the content of the disclosure.
In re Wands, 8 USPQ2d, 1400 (CAFC 1988) and MPEP 2164.01.
The breadth of the claims and nature of the invention:
The nature of the invention is complex. As understood with the broadest reasonable interpretation, the claims encompass a genus of modified IL-2 polypeptides comprising amino acid substitutions at various residues (Claims 3, 6, 15-16, and 57-58), any substitutions that reduce affinity for CD132 or CD25 (Claims 14 and 56), or at least 90% identity to an amino acid sequence selected from SEQ ID NOs: 160 and 270-277 (Claim 90). Claims 108 and 153 recite wherein the Fc region comprises at least 90% identity to an amino acid sequence selected from SEQ ID NOs: 47-83, 292, and 293. Claims 118, 120, 129, and 158 are directed to a genus of possible antigen binding domains. “At least 90% sequence identity” means that 10% of the amino acid residues can be inserted, deleted, or substituted with conservative or non-conservative changes. For example, 10% variation in SEQ ID NO: 270 (Claim 90) means that 13 amino acid residues can be altered in any combination (10% of 133 amino acid residues). Overall, the claims are directed to a genus of modified IL-2 polypeptides that comprises substantial amino acid variation in addition to a genus of possible Fc regions and a genus of possible antigen binding domains. The broad scope of these claims encompasses thousands of modified IL-2 polypeptides and fusion proteins thereof.
When analyzing the scope of enablement, the claims are analyzed with respect to the teachings of the specification and are to be "given their broadest reasonable interpretation consistent with the specification." See MPEP 2111 [R-5]; Phillips v. AWH Corp., 415 F.3d 1303, 75 USPQ2d 1321 (Fed. Cir. 2005); and In re Hyatt, 211 F.3d 1367, 1372, 54 USPQ2d 1664, 1667 (Fed. Cir. 2000). Applicant always has the opportunity to amend the claims during prosecution, and broad interpretation by the examiner reduces the possibility that the claim, once issued, will be interpreted more broadly than is justified. In re Prater, 415 F.2d 1393, 1404-05, 162 USPQ 541, 550- 51 (CCPA 1969).
The state of the prior art and level of predictability in the art:
The level of predictability in the art depends, most importantly, on whether the claimed invention can be practiced by one of ordinary skill in the art. In AMGEN INC. ET AL. v. SANOFI ET AL. (No. 21-757, decided May 18, 2023), the Supreme Court held that Amgen was not enabled for “the entire genus” of antibodies that (1) “bind to specific amino acid residues on PCSK9,” and (2) “block PCSK9 from binding to [LDL receptors]” (872 F. 3d 1367, 1372) even though Amgen identified the amino acid sequences of 26 antibodies that perform these two functions. The case law applies to the instant claims which encompass a genus of modified IL-2 polypeptides fused to various Fc regions and/or antigen binding domains, yet the inventors have only disclosed nine species of modified IL-2 (SEQ ID NOs: 160 and 270-277 in Table 14) and five species of antigen binding domains (Examples 14, 25, and 27-28).
In Amgen, the Supreme Court has stated: “An antibody' s structure does much to dictate its function—its ability to bind to an antigen and, in some instances, to block other molecules in the body from doing the same. Different antibodies have different binding and blocking capacities based on the amino acids that compose them and their three-dimensional shapes.” See id., at 11–12. Despite recent advances, aspects of antibody science remain unpredictable. For example, scientists understand that changing even one amino acid in the sequence can alter an antibody' s structure and function. See id., at 14. But scientists cannot always accurately predict exactly how trading one amino acid for another will affect an antibody' s structure and function. Ibid. The unpredictability of amino acid mutations extends to polypeptide structure and function, such as IL-2 in the instant application. The instant specification further supports the case law by teaching that adding or removing one IL-2 amino acid substitution can substantially alter function, and the effects of combining individual mutations are difficult to predict (paragraph [00233] and Table 14).
The case law shows a continued lack of predictability even after the effective filing date of the instant invention, and there is no support in the Applicant’s disclosure leading one of ordinary skill to overcome the lack of predictability in the genus of amino acid variations claimed. The specification provides no guidance or direction for which 10% of the amino acid residues may be inserted, deleted, or substituted in the modified IL-2 and/or the Fc region such that the functional properties of the invention are preserved (reduced binding affinity for CD25, CD132, and/or CD122).
Level of skill in the art:
The level of skill would be high encompassing amino acid alterations, fusion protein science, immunotherapy, binding assays, etc.
Amount of direction provided by inventor and the existence of working examples:
The specification teaches nine species of modified IL-2 that comprise the required substitutions of Claim 1: SEQ ID NOs: 160 and 270-277 (Table 14 on page 87). Across SEQ ID NOs: 160 and 270-277, only five additional mutations are evaluated: L19A, L19N, M23T, E95Q, and S127D. Note, T3A and C125S mutations are also included but these substitutions are well understood in the art to improve stability without affecting biological function. Five additional IL-2 mutations are not sufficient to describe the genus of possible modified IL-2 polypeptides that are encompassed by the claims (10% variation or any substitution at residues L19, M23, N88, E95, Q22, R120, T123, Q126, S127, I129, S130, K43, Y45, I114, F42, R38, and/or L72).
The specification fails to teach how the Fc regions can be modified other than the “knobs-into-holes,” half-life extending, and effector null Fc region mutations understood in the art prior to filing (specification paragraphs [00135]-[00137]). No guidance is provided for how 10% of the Fc regions can be inserted, deleted, or substituted (Claims 108 and 153) other than these limited sets of known mutations. The claimed amino acid variation is substantial; for example, 10% variation in SEQ ID NO: 48 comprises altering any combination of 22 amino acid residues (10% of 223 amino acids).
The specification teaches IL-2 fused to an anti-LAG3 VHH (Example 14), a PD-1-binding VHH (Example 25), a NKp46-binding VHH (Example 25), a CD8a-binding VHH (Example 25), and a γδTCR-binding VHH (Examples 27-28). However, five structural examples of antigen binding domains do not adequately represent the claimed genus of antigen binding domains that comprises any domain structure and binding to any antigen.
The limited examples taught by the specification do not adequately represent the scope of modified IL-2 polypeptides and fusion proteins thereof that encompasses thousands of variations. A person having ordinary skill in the art would have to make a substantial inventive contribution in order to make and characterize a representative number of modified IL-2 polypeptides, modified Fc regions, and antigen binding domains to encompass the claimed genera.
The quantity of experimentation needed to make or use the invention based on the content of the disclosure:
In light of the unpredictability surrounding the claimed subject matter, the undue breadth of the claimed invention’s intended use, and the lack of adequate guidance, one wishing to make and practice the presently claimed invention would be unable to do so without engaging in undue experimentation. Given that structure is essential to function, a person having ordinary skill in the art would have to perform further experimentation to make the variants encompassed by the claims and screen their functional characteristics (binding affinity, stability, half-life, dimerization, etc.) in order to practice the invention commensurate with the scope of the claims.
The instant specification does not enable the invention to make and use the entire genus of modified IL-2 polypeptides and fusion proteins thereof; therefore, Claims 1-3, 6, 14-16, 56-58, 80-81, 84, 87, 90, 93, 95-96, 100, 108-110, 113, 118, 120, 129, 132, 142-144, 148, 153-154, 158, and 163 are rejected.
Double Patenting
Note, no provisional non-statutory double patenting rejection is made in view of US Application No. 17/418,458, because the copending claims do not recite wherein the modified IL-2 comprises a E61R substitution as required by instant Claim 1.
Allowable Subject Matter
Claims 86 and 117 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims. Modified IL-2 polypeptides comprising SEQ ID NOs: 160 and 270-277 are enabled and free of the prior art.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SARAH COOPER PATTERSON whose telephone number is (703)756-1991. The examiner can normally be reached Monday - Friday 8:00am - 5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at (571) 272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/SARAH COOPER PATTERSON/Examiner, Art Unit 1675
/STACEY N MACFARLANE/Examiner, Art Unit 1675