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 .
Claim Status
Claims 1-13 as filed on 26 February 2024 are pending and under examination.
Information Disclosure Statement
The information disclosure statement filed 02/26/2024 fails to comply with the provisions of 37 CFR 1.97, 1.98 and MPEP § 609 because no copies attached of Foreign references 1-2 and 4. It has been placed in the application file, but the information referred to therein has not been considered as to the merits. Applicant is advised that the date of any re-submission of any item of information contained in this information disclosure statement or the submission of any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the statement, including all certification requirements for statements under 37 CFR 1.97(e). See MPEP § 609.05(a).
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-13 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 1 recites the limitation "wherein a lysine residue included in the light chain CDR" in line 6. There is insufficient antecedent basis for this limitation in the claim. Claim 1 has 3 light chain CDRs meaning “the light chain CDR” lacks antecedent basis. Further, claim 1 does not provide sequences for the CDRs of the light chain so the reference to a lysine to be substituted lacks antecedent basis and can refer to any amino acid position in the light chain CDRs.
Thus, claim 2, which depends from claim 1 recites the limitation "wherein the lysine (k) residue included in the light chain CDR sequences” also lacks antecedent basis.
Furthermore, claim 2 states that wherein the lysine (k) residue included in the light chain CDR sequences is K24 or K30 of the light chain CDR" in line 2. Because instant claims 2 and base claim 1 do not provide a sequence for a light chain or any of the CDRs. Therefore, it is unclear what the sequence is the claimed K24 or K30 referencing.
Claim 3 provides possible amino acids to be substituted with the lysine, but fails to correctly identify the lysine that lacks antecedent basis in claim 1 from which it depends.
Claim 4 provides sequences for the CDRs of CDR1 being instant SEQ ID NO: 4, CDR2 being instant SEQ ID NO: 5, and CDR3 being instant SEQ ID NO: 6. None of these sequences contain a lysine (K) amino acid and thus do not correct the lack of antecedent basis.
Claims 5-13 do not provide additional sequence information to determine the lysine or CDR referred to in claim 1 from which they depend.
The claims as read would refer to any MUC1 binding antibody with light chain CDRs that comprise any non-lysine amino acids.
For the purpose of search examiner has interpreted “the light chain CDR” that comprises a lysine substitution as light chain CDR1 meaning claim 1 is examined as:
“An anti-MUC1 antibody or an antigen-binding fragment thereof that specifically binds to a polypeptide comprising a contiguous amino acid sequence within a C- terminal extracellular domain of MUC1, and comprises one or more of a heavy chain variable region including a heavy chain CDR1, a heavy chain CDR2, or a heavy chain CDR3; and a light chain variable region including a light chain CDR1, a light chain CDR2, or a light chain CDR3, wherein light chain CDR1 comprises at least one amino acid that is not a lysine (k).”
Regarding claim 2, without a reference sequence comprising lysines and at least 30 amino acids “K24” and “K30”. Examiner cannot determine metes and bounds of the claim even in view of the specification or art. Claim 2 was not further examined on the merits.
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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Claims 1 and 3-13 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.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or it may be satisfied by the disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
Scope of the Claimed Genus
Claim 1 is to a MUC1 binding antibody or antigen binding fragment that binds the C-terminal extracellular domain of MUC1 and comprises one or more heavy chain that comprise HCDR 1, 2, and 3 and a light chain that comprises LCDR 1, 2, and 3 and wherein an amino acid of light chain CDR1 comprises at least 1 amino acid that is not a lysine.
Claim 3 requires the non-lysine amino acid of the light chain CDR1 is an arginine, histidine, aspartic acid, glutamic acid, glycine, alanine, valine, methionine, phenylalanine, tyrosine, tryptophan, leucine, or isoleucine. It does not provide requirements for the location within the light chain CDR1 that is not a lysine and does not limit any heavy chain CDRs or light chain CDRs 2 and 3.
Claim 4 requires the heavy chain comprise HCDR 1, 2, and 3 of instant SEQ ID NO: 1, 2 and 3 respectively, and LCDR 1, 2, and 3 of instant SEQ ID NO: 4, 5, and 6. Instant SEQ ID NO: 4 is XASQDIXSYLS with 2 variable amino acids which can be substituted with any amin acids.
Claims 5-13 provide no limitations on the sequence of the CDRs of the MUC1 binding antibody.
Summary of Species Disclosed in the original specification
Applicant discloses 4 antibodies: PAb001 which was mutated to produce three MUC1 binding antibodies that comprise the mutations 1) HCDR 1, 2, and 3 of SEQ ID NO: 1, 2, and 3 with LCDR 1, 2, and 3 of SEQ ID NO: 4 where both Xs are an Arginine (R) and would then be RASQDIRSYLS, SEQ ID NO: 5, and SEQ ID NO: 6, respectively; and 2) HCDR 1, 2, and 3 of SEQ ID NO: 1, 2, and 3 with LCDR 1, 2, and 3 of SEQ ID NO: 4 where the first X is an Arginine (R) and the second X is a Glycine (G) and would then be RASQDIGSYLS, SEQ ID NO: 5, SEQ ID NO: 6, respectively; and 3) HCDR 1, 2, and 3 of SEQ ID NO: 1, 2, and 3 with LCDR 1, 2, and 3 of SEQ ID NO: 4 where the first X is an Arginine (K) and the second X is a Arginine (R) and would then be KASQDIRSYLS, SEQ ID NO: 5, SEQ ID NO: 6, respectively.
PAb001 comprises HCDR 1, 2, and 3 of SEQ ID NO: 1, 2, and 3, respectively, with LCDR 1, 2, and 3 of SEQ ID NO: 4 where both Xs are a Lysine (L) and would then be LASQDILSYLS, SEQ ID NO: 5, and SEQ ID NO: 6, respectively.
These are shown in Figures 1-5 along with their binding activity to MUC1.
State of the Relevant Art
MUC1 is a 200 to 500 nm transmembrane glycoprotein that comprises multiple domains including a number of glycosylated extracellular domains (Choi (US 20200024361 A1) (PTO-892)) ([0002]). Choi further teaches MUC1 is located at the cell surface of the apical membrane of normal epithelial cells and in the linear or luminal epithelial cells of numerous organs. MUC1 forms a physical barrier that protects the basal epithelial from dehydration, pH changes, pollen, and microorganisms ([0002]). The C terminal of MUC1 is cleaved into two fragments and in cancers one fragment is isolated from cancer cells and enters the blood while the other remains cell-bound to cancer cells ([0004]). The presence of MUC1 on cancer cells sends a continuous proliferation signal ([0004]). The C-terminal extracellular domain of MUC1 is a known target of antibodies for use in treatment of cancer (Abstract and claim 1).
It has been well established in the art that the formation of an intact antigen-binding site in a conventional antibody requires the association of the complete heavy and light chain variable regions of a given antibody, each of which comprises three CDRs (or hypervariable regions) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro et. al., Front. Immunol. 2018; 8:1751 (PTO-892) (see Section “The IgG Molecule” in paragraph 1 and Figure 1). While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule”, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7). But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure of each monoclonal antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). The epitope of an antibody does not provide structure or sequence information about the antibody that binds it.
Further, the skilled artisan has long recognized that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Brown et al., J. Immunol., 156(9):3285- 91 (1996) (PTO-892). Brown teaches that although a single amino acid change in CDR2 of heavy chain of a particular antibody was tolerated, the antibody lost binding upon introduction of two amino acid changes in the same region. Brown, p. 3290 and Tables 1 and 2. Table 1 of Brown shows that even a conservative substitution does not ensure that functionality of the antibody is retained. These older citations are supported my more recent discoveries of why these substitutions change antibody activity. Marvin et. al., Biochemistry, 42(23):7077-7083 (2003) (“Marvin” PTO-892) teaches that changes to the heavy and light chains altered binding affinity (Table 2) with changes to the CDR having large impacts but the changes with the largest impact were from residues in the CDR, but not from ones interfacing with the antigen ( Page 7081 in col 1 “Conclusions and Discussion” and Page 7082 in Figure 4).
This is confirmed by Chiu et al., Antibodies, 8(55):1-80. (2019) (“Chiu” PTO-892). Chiu teaches that the complementarity-determining regions (HCDRs 1-3 and LCDRs 1-3) determine antigen binding requiring specific sequences and orientation of those sequences to properly form tertiary structures that can recognize and bind antigens (Page 4 in 1.2.2 first and last paragraphs and Figure 3). Chiu teaches that antibody modeling with known LCDRs 1-3, HCDR1 and HCDR2 could not predict HCDR3. The field has shown repeatedly over decades that Structure-Based antibody engineering is unable to predict antibody sequences (Page 6 in 1.2.6, Pages 10-11 in Section 2 in particular second paragraph of page 11). Chiu notes the advancement in antibody engineering but notes it is still not possible to predict the point mutations that would improve affinity in both antibodies and multispecific molecules (Page 51 in lines 6-12).
In general, absent at least the conserved structure of the CDRs of the heavy chain and light chain of an antibody, the skilled artisan generally would not be able to visualize or otherwise predict an antibody with a particular set of functional properties would look like structurally. An epitope does not inform one of skill in the art of the structure of the antibody that binds it and a partial structure of only some CDRs or some of the CDR sequences does not provide sufficient information to identify the undefined CDR identity.
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that 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.
The specification discloses 4 MUC1 binding antibodies with fully defined CDR sequences of the heavy and light chain.
Given the variability encompassed by the genus of antibodies that bind MUC1 where changes to the CDRs change the binding activity in unpredictable ways the described species cannot be considered representative of the genus as the description of an antibody with its fully defined CDRs only provides written description on that antibody and not ones with varying CDR sequences.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. To meet this requirement in the instant case, the specification must describe structural features that the skilled artisan as of the effective filing date would have expected to convey the claimed binding activity.
As described above the structure in an antibody that provides its binding activity
is the set of 6 CDRs. As changes to the amino acids of the CDRs change its function, the CDRs of the disclosed antibodies do not disclose additional antibodies. The epitope of an antibody, no matter how specific, does not provide any structure for the CDRs of an antibody that binds that epitope.
Conclusion:
For all of the reasons presented above, one of skill in the art would not know which of the CDR combinations of the claims would meet the structural and functional requirements of the claims. The applicant has not provided a representative number of species for all antibodies that bind the epitope of the C terminus extracellular domain of MUC1 of claim 1 or the partially defined CDRs of claims 3 and 4. The functional structure of an antibody are its 6 CDRs that provide its binding activity based on the sequences of those CDRs, the CDRs of one antibody do not provide one of skill in the art with the functional CDRs of additional antibodies so the variability of the CDRs of the rejected claims mean there is no structure/function correlation, and the disclosed species do not provide written description for additional antibodies. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as claimed.
This rejection could be overcome by limiting the claims to specific combinations
of six CDRs that applicant has shown written description for. The antibodies that have written description in the specification and appear to be free of the art are shown below.
HCDR1
HCDR2
HCDR3
LCDR1
LCDR2
LCDR3
SEQ ID NO:
1
2
3
4
5
6
Antibody 1
Substitutions for (X)
None
X1=R X2=R
None
Antibody 2
X1=R X2=G
Antibody 3
X1=K X2=R
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1 and 3-13 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Choi (US 20200024361 A1) (PTO-892).
Regarding claims 1 and 3-4, Choi teaches anti-MUC1 antibodies that comprise a light chain CDR1 that comprises amino acids other than lysine (Abstract and Table 2). Choi teaches the CDRs of the heavy and light chain match the CDRs of instant SEQ ID NO: 1-6 as required by claims 3-4. Choi teaches the antibody binds the C-terminal extracellular domain of MUC1 (claim 1). The sequence match for the heavy and light chain are shown below. The second alignment below shows that the light chain CDR1 comprises amino acids other than lysine including serine as required by claims 1 and 3-4.
PNG
media_image1.png
151
519
media_image1.png
Greyscale
PNG
media_image2.png
164
544
media_image2.png
Greyscale
Regarding claim 5, Choi teaches the antibody as part of an antibody-drug conjugate (Example 32 and claim 7).
Regarding claim 6, Choi teaches a bispecific comprising the antigen binding fragment (claims 11-13).
Regarding claims 7-9, Choi teaches the anti-MUC1 as part of a CAR-T immune cell ([0094]).
Regarding claims 10-11, Choi teaches the treatment of pancreatic and breast cancers using the anit-MUC1 antibody (Figures 4-6 and 20 and Examples 9 and 17).
Regarding claim 12, Choi teaches a method of diagnosing cancer using the antibody ([0137], Example 24, and claim 16).
Regarding claim 13, Choi teaches a method of preparing the anti-MUC1 antibody by an expression vector comprising a nucleic acid encoding the antibody in a host cell being cultured (claims 21-24 and 27 and Example 2).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1, 3-4, and 6 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. Patent No. 11472887 (Reference Patent). Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claims 1 and 3-4, the reference patent recites the CDRs of the heavy and light chain match the CDRs of instant SEQ ID NO: 1-6 as required by claims 3-4. Choi teaches the antibody binds the C-terminal extracellular domain of MUC1 (claim 1), light CDR1 comprises non-lysine amino acids.
Regarding claim 6, the reference patent recites a bispecific antibody of that binds MUC1 (claims 3-4).
Claims 1, 5, and 7-13 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 of U.S. Patent No. 11472887 (Reference Patent) in view of Choi (US 20200024361 A1) (PTO-892).
Regarding claim 1, the reference patent recites the CDRs of the heavy and light chain match the CDRs of instant SEQ ID NO: 1-6 as required by claims 3-4. Choi teaches the antibody binds the C-terminal extracellular domain of MUC1 (claim 1), light CDR1 comprises non-lysine amino acids.
Regarding claims 10-11, the reference patent recites a pharmaceutical composition for treating cancer claim 5).
Regarding claim 12, the reference patent recites a composition for diagnosing cancer using the anti-MUC1 antibody (claim 6).
The reference patent does not recite an antibody-drug conjugate, a CAR-NK cell, a method of treating or diagnosing cancer with the anti-MUC1 antibody with the active step of administering the antibody to a patient or a sample, or the method of preparing the anti-MUC1 antibody.
These deficiencies are filled by Choi.
Choi teaches the same anti-MUC1 antibody of the reference patent.
Regarding claim 5, Choi teaches the antibody as part of an antibody-drug conjugate (Example 32 and claim 7).
Regarding claims 7-9, Choi teaches the anti-MUC1 as part of a CAR-T immune cell ([0094]).
Regarding claims 10-11, Choi teaches the treatment of pancreatic and breast cancers using the anit-MUC1 antibody (Figures 4-6 and 20 and Examples 9 and 17).
Regarding claim 12, Choi teaches a method of diagnosing cancer using the antibody ([0137], Example 24, and claim 16).
Regarding claim 13, Choi teaches a method of preparing the anti-MUC1 antibody by an expression vector comprising a nucleic acid encoding the antibody in a host cell being cultured (claims 21-24 and 27 and Example 2).
It would have been obvious at the time the application was filed to combine the anti-MUC1 antibody of the reference patent with the CAR-T and methods of diagnosis, treatment, and production of Choi. One of skill in the art would have been motivated to find additional applications for the MUC1 binding antibody of the reference patent and Choi teaches the same MUC1 binding antibody of the reference patent.
Regarding claims 5 and 7-9, the combination of the anti-MUC1 of the reference patent with the antibody-drug conjugate and CAR-T immune cell comprising the antibody of the reference patent would have been obvious as the anti-MUC1 antibody of the reference antibody and Choi are the same. There would have been a reasonable expectation of success as the MUC1 binding antibody of the reference patent and Choi are the same and Choi teaches their successful use in the ADC and CAR-T.
Regarding the method of treating pancreatic cancer of claims 10-11, the reference patent recites a pharmaceutical composition for use in the treatment for cancer. The reference patent teaches everything but the active method step of the treatment claim thus teaching towards the combination with the method of Choi and making the combination obvious. There would have been a reasonable expectation of success as the reference patent recites a pharmaceutical composition for use in a method of treatment and Choi teaches a method using the same anti-MUC1 antibody.
Regarding claim 12, the reference patent recites a composition for use in the diagnosis for cancer. The reference patent teaches everything but the active method step of the treating a biological sample of the claim thus teaching towards the combination with the method of Choi and making the combination obvious. There would have been a reasonable expectation of success as the reference patent recites a composition for use in a method of diagnosis and Choi teaches a method using the same anti-MUC1 antibody.
Regarding claim 13, one of skill in the art would have been motivated to use known in the art methods of producing the antibody of the reference claims. Choi provides a known in the art method of producing the same antibody of the reference patent making the combination obvious. There would have been a reasonable expectation of success as Choi provides a method of producing the same antibody of the reference patent.
Conclusion
No claims allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to FRANCESCA EDGINGTON-GIORDANO whose telephone number is (571)272-8232. The examiner can normally be reached Mon - Fri 8:00 - 5:00.
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, Julie Wu can be reached at 571-272-5205. 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.
/F.E./Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
Prosecution Insights