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 .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 56-70, alongside the species of a T cell, in the reply filed on 1 April 2026 is acknowledged.
Claims 71-75 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim.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 1 April 2026.
Applicant is reminded that upon the cancelation of claims to a non-elected invention, the inventorship must be corrected in compliance with 37 CFR 1.48(a) if one or more of the currently named inventors is no longer an inventor of at least one claim remaining in the application. A request to correct inventorship under 37 CFR 1.48(a) must be accompanied by an application data sheet in accordance with 37 CFR 1.76 that identifies each inventor by his or her legal name and by the processing fee required under 37 CFR 1.17(i).
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - The Incorporation by Reference paragraph required by 37 CFR 1.821(c)(1) is missing or incomplete. The file size must be listed in bytes. See item 1) a) or 1) b) above.
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
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 application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 56, 64, 66-67, and 69 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199).
Regarding claims 56 and 66, Vleminckx is directed towards a study concerned with the use of a vector (i.e., a polynucleotide) encoding a chimeric transcription factor (i.e., a chimeric polypeptide) consisting of a C-terminal ß-catenin transactivation domain fused to a DNA binding domain of an LEF-1 TCR protein that can be utilized to transcriptionally activate target luciferase reporter genes in a mammalian cells (Abstract; pg. 67-68; see Fig. 1). Vleminckx teaches that the direct fusion of the ß-catenin to the LEF-1 domain generated a sequence specific transcriptional activator in mammalian cells (pg. 66).
Vleminckx does not teach or suggest the use of a TCF1 domain (Claim 56).
Zhao is directed towards a study concerned with the constitutive activation of canonical Wnt pathways in memory CD8 T cells (Abstract). Zhao teaches that Wnt proteins are secreted, lipid-modified glycoproteins that activate multiple signal transduction pathways to regulate a variety of cellular activities, including cell fate determination, proliferation, and gene expression in T cells (pg. 1191). Zhao teaches that both TCF-1 and LEF-1 can form complexes with ß-catenin to activate transcription of Wnt target genes in T cells (pg. 1191-1192). Zhao teaches that there is a functional redundancy between TCF-1 and LEF-1 and a relatively dominant role of TCF-1 during T cell development (i.e., Zhao is interpreted as teaching that both TCF-1 and LEF-1 have identical, redundant, functions) (pg. 1192).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed TCF1 domain because it would have merely amounted to simple substitution of one known TCF domain for another to yield predictable results. Because each of the two TCF domains were used in a similar way, namely as a transcriptional activator of a target gene through its interaction with ß-catenin, then it would have been predictable to have used the TCF1 domain as the TCF domain present in the fusion protein in order to transcriptionally activate target luciferase reporter genes in a mammalian cells.
Regarding claim 64, Vleminckx teaches the use of an expression vector that comprises the polynucleotide and can encode the fusion protein (pg. 66-67; see Fig. 1).
Regarding claim 67, Vleminckx teaches that human kidney cells were transfected with the expression vector and a reporter plasmid (pg. 66).
Regarding claim 69, Vleminckx does not teach or suggest that the cell is derived from a T cell (Claim 69).
Zhao, as discussed above, teaches that both TCF-1 and LEF-1 can form complexes with ß-catenin to activate transcription of Wnt target genes in T cells (pg. 1191-1192). Zhao teaches that Wnt proteins are secreted, lipid-modified glycoproteins that activate multiple signal transduction pathways to regulate a variety of cellular activities, including cell fate determination, proliferation, and gene expression in T cells (pg. 1191).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed T cell because it would have merely amounted to simple substitution of one known cell for another to yield predictable results. Because each of the two cell types were used in a similar way, namely host cells for the expression of both a TCF domain and a ß-catenin to transcriptionally activate target genes within the host cell, then it would have been predictable to have used the T cell as the host cell in order to activate the expression of the target reporter genes.
Claim(s) 57-58 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199) as applied to claims 56, 64, 67, and 69 above, and further in view of Schultze (PG Pub No. US 2011/0097334 A1).
Regarding claims 57-58 and 63, Vleminckx in view of Zhao renders obvious claims 56, 64, 67, and 69 as described above. Further, it is noted that the instant specification teaches that the claimed SEQ ID NO: 2 is a TCF1 isoform 4S (pg. 18; see Table 2). Vleminckx further teaches that the chimeric polynucleotide could be expressed from an expression vector (i.e., at least the first nucleic acid is operably linked to a promoter) (Abstract; pg. 67-68; see Fig. 1).
Vleminckx in view of Zhao does not teach or suggest that the TCF1 domain comprises a TCF1 isoform 4S (Claim 57) or that the TCF1 domain comprises an amino acid sequence having at least 90% identity to the claimed SEQ ID NO: 2 (Claim 58). Vleminckx in view of Zhao does not teach or suggest the use of a first inducible promoter operably linked to the first nucleic acid encoding the TCF1 domain (Claim 63).
Schultze is drawn towards an invention concerned with marker genes for the identification of regulatory T cells (Abstract). Schultze teaches the use of an mRNA that encodes a TCF7 isoform 3 (i.e., a first nucleic acid encoding a TCF domain), wherein the translation of the mRNA results in a TCF domain that has 100% identity to the claimed SEQ ID NO: 2 (i.e., Schultze teaches the use of a TCF1 isoform 4S, as defined by the instant specification) ([0228]; see SEQ ID NO: 112 in attached sequence alignment).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed TCF1 isoform 4S domain comprising at least 90% identity to the claimed SEQ ID NO: 2 because it would have merely amounted to simple substitution of one known TCF1 domain for another to yield predictable results. Because each of the nucleic acids were used in a similar way, namely the encoding of a TCF1 domain, then it would have been predicable to have used the nucleic acid encoding the claimed SEQ ID NO: 2 within the polynucleotide encoding the chimeric polypeptide in order to transcriptionally activate target genes within the host cell of Vleminckx in view of Zhao.
Claim(s) 59 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199) as applied to claims 56, 64, 67, and 69 above, and further in view of Reya (PG Pub No. US 2002/0004241 A1) and Gan ("Interaction between JCV large T-antigen and β-catenin." Oncogene 23.2 (2004): 483-490).
Regarding claim 59, Vleminckx in view of Zhao renders obvious claims 56, 64, 67, and 69 as described above.
Vleminckx in view of Zhao does not teach or suggest that the β-catenin transactivation domain comprises an amino acid sequence having at least 90% identity to the claimed SEQ ID NO: 4 (Claim 59).
Reya is drawn towards a study concerned with the manipulation of levels of β-catenin in cells (Abstract). Reya teaches that nucleic acids encoding β-catenin transactivation domains may be introduced into target cells of interest ([0007]). Reya teaches the use of a mouse homolog of β-catenin transactivation domain that comprises a region that has 100% identity to the claimed SEQ ID NO: 4 at amino acids 695-781 of the protein ([0016]; see SEQ ID NO: 2 in attached sequence alignment).
Gan is drawn towards a study concerned with the interaction between a JCV large T-antigen and β-catenin (Abstract). Gan teaches that the C-terminus of a β-catenin domain is located at amino acids 695-781 (Abstract). Gan teaches that the transcriptional activation domain of β-catenin domain is located at amino acids 695-781 (pg. 485).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed β-catenin transactivation domain that comprises an amino acid sequence having at least 90% identity to the claimed SEQ ID NO: 4 because it would have merely amounted to simple substitution of one known C-terminal β-catenin transactivation domain for another to yield predictable results. Because each of the nucleic acids were used in a similar way, namely the encoding of a C-terminal β-catenin transactivation domain, then it would have been predicable to have used the nucleic acid encoding the β-catenin transactivation domain comprising an amino acid sequence with 100% identity to the claimed SEQ ID NO: 4 within the polynucleotide encoding the chimeric polypeptide in order to transcriptionally activate target genes within the host cell of Vleminckx in view of Zhao.
Claim(s) 60-61 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199) as applied to claims 56, 64, 67, and 69 above, and further in view of Rosmalen ("Tuning the flexibility of glycine-serine linkers to allow rational design of multidomain proteins." Biochemistry 56.50 (2017): 6565-6574) and Cheung (PG Pub No. US 2017/0210819 A1).
Regarding claim 59-60, Vleminckx in view of Zhao renders obvious claims 56, 64, 67, and 69 as described above.
Vleminckx in view of Zhao does not teach or suggest that the TCF1 domain is linked to the β-catenin transactivation domain via a linker having a length in the range of 2-20 amino acid residues (Claim 60), or wherein the linker comprises the claimed SEQ ID NO: 3 (Claim 61).
Rosmalen is drawn towards a review concerned with the use of glycine-serine linkers to allow for the rational design of multidomain proteins (Abstract). Rosmalen teaches that flexible linkers consisting of repeats of serine and glycine are widely used in the construction of multidomain proteins (pg. 6570). Rosmalen teaches that the combination of flexible and hydrophilic residues in these linkers prevents the formation of secondary structures and reduces the likelihood that the linkers will interfere with the folding and function of the protein domains (pg. 6565). Rosmalen teaches that two reporter proteins, ECFP and EYFP, were able to be linked to one another through the use of a glycine-serine linker and that the fluorescent activities of both proteins were not affected by the presence of the linker (pg. 6567; see Figure 1).
Cheung is drawn towards a study concerned with the use of bispecific binding molecules that specifically bind to HER2, a receptor tyrosine kinase, and to CD3, a T cell receptor, and mediate T cell cytotoxicity for managing and treating disorders, such as cancer (Abstract). Cheung teaches the use of a (G4S)2 linker that comprises 100% identity to the claimed SEQ ID NO: 3 ([0111]; see Table 1 and SEQ ID NO: 37 in attached sequence alignment).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the linker comprising the claimed SEQ ID NO: 3 present between the claimed domains because it would have merely amounted to simple substitution of one known method of fusing two heterologous proteins, namely direct fusion, for another, namely the use of a glycine-serine linker that comprises the claimed SEQ ID NO: 3. Because each of the fusion methods were used in a similar way, namely the fusion of two heterologous proteins in a manner that does not disrupt the secondary structures nor the function of the two proteins, then it would have been predicable to have used a linker the nucleic acid encoding the β-catenin transactivation domain comprising an amino acid sequence with 100% identity to the claimed SEQ ID NO: 3 within the polynucleotide encoding the chimeric polypeptide in order to transcriptionally activate target genes within the host cell of Vleminckx in view of Zhao.
Claim(s) 62 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199) as applied to claims 56, 64, 67, and 69 above, and further in view of Schultze (PG Pub No. US 2011/0097334 A1), Rosmalen ("Tuning the flexibility of glycine-serine linkers to allow rational design of multidomain proteins." Biochemistry 56.50 (2017): 6565-6574), Cheung (PG Pub No. US 2017/0210819 A1), Reya (PG Pub No. US 2002/0004241 A1), and Gan ("Interaction between JCV large T-antigen and β-catenin." Oncogene 23.2 (2004): 483-490).
Regarding claim 62, it is noted that the claimed SEQ ID NO: 1 comprises, 5’ to 3’, the claimed SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4 (Instant specification; see Table 2).
Vleminckx in view of Zhao does not teach or suggest the use of a chimeric amino acid sequence having at least 90% identity to the claimed SEQ ID NO: 1 (Claim 62).
However, regarding the claimed SEQ ID NO: 2, the obviousness of substituting the TCF1 isoform 4S is described above as applied to claim 57-58.
Regarding the claimed SEQ ID NO: 3, the obviousness of using a linker that comprises the claimed SEQ ID NO: 3 is described above as applied to claims 60-61.
Regarding the use of the claimed SEQ ID NO: 4, the obviousness of substituting the C-terminal β-catenin transactivation domain comprising a sequence with 100% identity to the claimed SEQ ID NO: 4 is described above as applied to claim 59.
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed SEQ ID NO: 1 because it would have merely amounted to simple substitutions of known TCF1 domains, known methods of fusing proteins through the use of a glycine-serine linker, and a known C-terminal β-catenin transactivation domain as discussed above and as applied to claims 57-61. The applicable obviousness rationales for the use of each of the claimed SEQ ID NOs: 2-4 within the fusion protein of Vleminckx in view of Zhao are discussed above as applied to claims 57-61.
Claim(s) 63, 65, 68, and 70 is/are rejected under 35 U.S.C. 103 as being unpatentable over Vleminckx ("The C-terminal transactivation domain of β-catenin is necessary and sufficient for signaling by the LEF-1/β-catenin complex in Xenopus laevis." Mechanisms of development 81.1-2 (1999): 65-74) in view of Zhao ("Constitutive activation of Wnt signaling favors generation of memory CD8 T cells." The Journal of Immunology 184.3 (2010): 1191-1199) as applied to claims 56, 64, 67, and 69 above, and further in view of Powell (PG Pub No. US 2021/0032661, filed 8 April 2019).
Regarding claims 63, 65, 68, and 70, Vleminckx in view of Zhao renders obvious claims 56, 64, 67, and 69 as described above.
Regarding claims 63 and 65, Vleminckx further teaches that the chimeric polynucleotide could be expressed from an expression vector (i.e., the first and second nucleic acids are operably linked to promoters) (Abstract; pg. 67-68; see Fig. 1).
Vleminckx in view of Zhao does not teach or suggest that the polynucleotide further comprises an inducible promoter linked to the first nucleic acid (Claim 63). Vleminckx in view of Zhao does not teach or suggest that the vector is an adenoviral vector (Claim 65).
Powell is drawn towards an invention concerned with the use of a viral vector for expression of a transgene and an effector (Abstract). Powell teaches the use of a vector encoding an inducible promoter linked to an effector protein selected from a regulatory element ([0006], [0015]), wherein the regulatory element may be TCF7 ([0021]). Powell teaches that the vector may be an adenoviral vector ([0022]).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed inducible promoter operably linked to the TCF1 domain and adenoviral vector because it would have merely amounted to a simple substitution of one known promoter within a vector that could drive expression of a TCF protein for another. Because each of the vectors were used in a similar way, namely for the expression of TCF a protein, then it would have been predicable to have used an inducible promoter operably linked to the TCF1 domain within an adenoviral vector for the expression of the fusion protein in order to transcriptionally activate target genes within the host cell of Vleminckx in view of Zhao.
Regarding claims 68 and 70, Vleminckx in view of Zhao does not teach or suggest that the cell further comprises a nucleic acid encoding a CAR (Claim 68). Vleminckx in view of Zhao does not teach or suggest the use of a pharmaceutical composition comprising the cell of claim 67 and a pharmaceutically acceptable excipient (Claim 70).
However, Powell further teaches that cancers can be treated with T-cells that express chimeric antigen receptors and that designer T cells (i.e., engineered immune cells), wherein the T-cells express the CAR through the use of a nucleic acid operably linked to a constitutive promoter, respond specifically to antigen-positive cancer cell lines and retain CAR mediated killing of the cancerous cells ([0313]). Powell teaches that the engineered immune cells may be administered to a subject in combination with a pharmaceutically acceptable excipient as a pharmaceutical composition ([0280]).
Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have arrived at the requirements of the claimed T-cell encoding a CAR and present within a pharmaceutical composition because it would have merely amounted to a simple combination of known prior art elements according to known methods to yield predictable results. Since Powell teaches the use of T-cells for a similar purpose as Vleminckx in view of Zhao, namely the expression of proteins from T-cells, then one would have had a reasonable expectation of success in modifying the T-cell of Vleminckx in view of Zhao such that it expressed a CAR and retained its ability to express the chimeric polypeptide. And because Powell teaches that the expression of a CAR on the T-cell alongside the use of a pharmaceutically acceptable excipient allows for the targeted treatment of cancers, one would have been motivated to do so.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KYLE T REGA whose telephone number is (571)272-2073. The examiner can normally be reached M-R 8:30-4:30, every other F 8:30-4:30 (EDT/EST).
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Neil Hammell can be reached at 571-270-5919. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/KYLE T REGA/Examiner, Art Unit 1636
/NEIL P HAMMELL/Supervisory Patent Examiner, Art Unit 1636
Prosecution Insights