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 .
Claims 1, 2, 5-9, 14-17, 28-32, and 37-40 are pending and being examined on the merit.
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.
Claim 15 is 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.
Claims 15 recite Markush-type language such as "selected from the group consisting of", but the group of linkers are not closed off as required for a proper Markush group. A conjunction, like the term “and”, is missing between the last two species of linkers. Note MPEP 803.02.
Claim 15 recites a Markush group for the linker includes mc-Val-Cit-pAB, mc-Val-Cit-pABC, mc-Val-Cit, and NH2-(PEG)m-Val-Cit, and NH2-(PEG)m-Val-Cit-pAB, wherein “m is an integer from 1 to 8”. “m is an integer from 1 to 8” is referencing the m of NH2-(PEG)m-Val-Cit, and NH2-(PEG)m-Val-Cit-pAB. However, it is unclear what “mc”, “pAB” and “pABC” of mc-Val-Cit-pAB, mc-Val-Cit-pABC, and mc-Val-Cit are referencing. Instant specification defined the dipeptide is valine (Val)-citrulline (Cit) (paragraph 0104), but there no definition for “mc”, pAB, and pABC.
Thus, the metes and bounds are unclear.
For the purpose of expedited prosecution, using the definition of mc in Sahin (US20180117174A1), mc of claim 15 is interpreted as maleimidocaproyl (paragraph 0273) for examination.
Regarding claim 2, The instant specification defined the term “humanized antibody” as an antibody that MAY comprise CDR regions derived from a human antibody, and rest parts derived from one or several human antibody (paragraph 0056). Thus, the term humanized antibody also includes limitations from the act recognized definition which is a humanized antibody is an antibody comprising a human framework region and CDR sequences from non-human species. Because the term humanized antibody of claim 2 requires the limitation Thus, the limitation of claim 2 is definite.
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 28-32, 37-39 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.
The claimed invention. The nature and scope of the claimed invention at issue is a method of treating cancer comprised of administering a conjugate comprising an antibody comprising three CDR regions having SEQ ID NOs:1-3 OR CDR regions having SEQ IDNOs:4-6. These claims required that the antibody binds to an antigen on tumor cells to induce a cytotoxic response. As defined by claim 29, the antibody may bind to CLDN18.2. Thus, the instant claimed method requires administration of an antibody that binds to an antigen on cancer cells and is comprised of a partial structure.
State of the prior art. It is well established in the art that the formation of an intact antigen-binding site in an antibody usually 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) that provide the majority of the contact residues for the binding of the antibody to its target epitope (Almagro, Frontiers in Immunology, 2018:8, 1751; specifically page 3, “The IgG Molecule”; Figure 1). Sela-Culang (Frontiers in Immunology, 2013, 4:302) further teaches, “A major focus in analyzing the structural basis for [antigen] recognition has been in identifying the exact boundaries of the CDRs in a given [antibody]. It is a common practice to identify paratopes through the identification of CDRs” (page 3, left column, “CDRs Identification”).
Chiu (Antibodies, 2019, 8(55):1-80) 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, 1.2.2 first and last paragraphs; figure 3). Chiu teaches that antibody modeling with known LCDRs 1-3, HCDR1 and HCDR2 could not predict HCDR3. Structure-Based antibody engineering is unable to predict antibody sequences (page 6, see 1.2.6, pages 10-11, see Section 2, in particular second paragraph of page 11). Chiu notes the advancement in antibody engineering but states it is still not possible to predict the point mutations that would improve affinity in both antibodies (page 51, lines 6-12).
Although the prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is aptly noted that the art is characterized by a high level of unpredictability, since the skilled artisan still cannot accurately and reliably predict the consequences of amino acid substitutions, insertions, and deletions in the antigen-binding domains. Ni (The Protein Journal, 2024, 43:683-696) teaches, “Mutations, even one mutation, introduced in the CDRs through [somatic hypermutation] can change the binding properties and repertoire of antibodies. However, how just one-point mutation can dramatically change the recognition profiles of the antibody is still unclear” (Introduction). Furthermore, while affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody, those techniques involve trial-and-error testing and the changes that maintain or improve affinity are unpredictable to those of ordinary skill in the art (Almagro, pages 3 and 6-7).
Antibodies that target Claudin 18.2 (CLDN 18.2) have been described in the arts. Ugur (US20180117174A1) teaches 11 different CLDN 18.2 antibodies (paragraph 0171-0184). These are conventional antibodies that comprise 6 distinct CDR sequences (Table 1). These sequences are not interchangeable.
Scope of species disclosed in original specification. The disclosure teaches SYJS001 antibody comprising CDR sequences of SEQ ID NOs:1-6 (example 1; table 1). The instant disclosure does not teach antibodies comprising VH sequences that can pair with a VL comprising SEQ ID NO:4-6; nor VL sequences that pair with a VH comprising SEQ ID NO:1-3 to form a functional antibody to bind to cancer cells.
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. While the disclosure appears to describe one antibody (see Table 1), it does not permit a skilled artisan to visualize the structure of a subgenus of antibodies that comprise a VH comprising SEQ ID NO:1-3s, or VL comprising SEQ ID NOs:4-6 that can bind to cancer cells to treat cancer.
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.
Accordingly, the disclosure only provides adequate written description for an antibody comprising SEQ ID NOs:1-6 that can bind to cancer cells to mediate a therapeutic effect.
Conclusion. For all of the reasons presented above, one of skill in the art would not know which of the countless other antibodies encompassed by the highly general structural requirements of the claims would also possess the required functional activity of binding to a cancer cell comprising a VH comprising SEQ ID NO:1-3 or VL comprising SEQ ID NO:4-6. 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, the Applicant did not possess the full subgenus genus of antibodies as broadly claimed at the time the application was filed.
Claims 1-2, 5-9, 14-17, 28-32 and 37-40 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 to generate a functioning antibody comprising SEQ ID NO:1-6, does not reasonably provide enablement for generating an antibody comprising either SEQ ID NOs:1-3 OR SEQ ID NOs:4-6. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to the invention commensurate in scope with these claims.
Factors to be considered in determining whether reasonable amount of experimentation to make and use a claimed invention, and reasonableness in any case will depend on the nature of the invention and the underlying art." Amgen Inc. et al. v. Sanofi et al., 598 U.S. 594, 596, 2023 USPQ2d 602 (2023) (MPEP2164.06). MPEP 2164.01(a) discussed the factors to consider for assessing enablement:
(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.
This invention is in a class of invention which the CAFC has characterized as "the unpredictable arts such as chemistry and biology". Mycogen Plant Sci., Inc. v. Monsanto Co., 243 F.3d 1316, 1330 (Fed. Cir. 2001).
The instant claims encompasses a conjugate comprising an antibody comprising either SEQ ID NOs:1-3 or SEQ ID NO:4-6, or a method treating comprised of administering said antibody.
It is well documented in the prior art that during B-cell development, the VH genes are rearranged to generate a functional VH polypeptide that pairs with a surrogate light chain comprising VpreB and l5 light chain to form a pre-B receptor (Janeway, Immuno Biology The immune system in Health and Disease, 4 edition, 1999, pages 195-209; figure 6.2 and 6.9 in particular). The association of the VH polypeptide with the surrogate light chain stabilizes the VH polypeptide, which is required for expression on the cell surface. B cells lacking the expression of a surrogate light chain do not produce functional VH polypeptides (Janeway, page 205, paragraphs 1 and 2 in particular). Following stable VH expression, the VL genes are rearranged in the developing B cell to generate a functional VL polypeptide, which then replaces the surrogate light chain to form a functional antibody comprising a VH-VL (Janeway, figure 6.2 in particular). The teachings of Janeway shows that both the VH and VL polypeptides need to be expressed in the same cell in order to produce stable VH and VL polypeptides to form an antibody.
Furthermore, Wijesuriya (Protein Expression and Purification, 2018, 149:75-83) showed that the expression level of the VH polypeptide is dependent on the expression of the VL in the same cell (see 3.5 Antibody engineering to improve mAB B-c expression in particular). Wijesuriya showed that laboratories have altered the expression levels and sequences of the VL to improve the expression of the VH and overall antibody production (abstract; see discussion in particular). These data shows that similar to antibody production in B cells, expression of an engineered VH polypeptide requires the expression of a VL polypeptide.
Even the examples of the instant application disclosed an antibody comprising 6 CDR sequences comprising SEQ ID NOs:1-6 (example 1; table 1). The instant specification has not shown and the prior art does not teach that it is possible to form an antibody when with only a VH alone or a VL alone to generate a stable VH and VL polypeptides to form a functional antibody.
In light of state of the art and these references, the specification fails to teach how to make and use the broadly claimed invention without reasonable amount of experimentation.
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.
Claim(s) 1, 2, 5, 7, 17, 28 and 29 is/are rejected under 35 U.S.C. 102(a)(1) or 102(a)(2) as being anticipated by Li (US20220041712A1, published on February 3, 2020, earliest priority date is February 1, 2019).
Regarding claims 1, 2, and 5, Li teaches Hu-10, a human anti-CLDN18.2 antibody comprising the VH amino acid sequences of SEQ ID NO:203 (same as instant SEQ ID NO:7), which comprises the same CDR sequences as instant SEQ ID NOs:1-3, and VL amino acid sequences of SEQ ID NO:204 (same as instant SEQ ID NO:8), which comprises the same CDR sequences as instant SEQ ID NOs:4-6 (paragraphs 0385, 0420; example 1). Regarding claim 7, Li teaches an antibody drug conjugate comprising said antibody and a cytotoxin (paragraph 0492; 0497-0498; figure 1). Regarding claims 17, 28, and 29, Li teaches administering a pharmaceutical composition comprising said antibody drug conjugate and a pharmaceutically acceptable carrier to treat CLDN18.2 positive cancer (paragraphs 0497, 0504-0507). Li teaches that Hu-10 binds strongly to CLDN18.2 (paragraph 0119; figure 4b; Table 6) expressed on pancreatic ductal adenocarcinomas (paragraph 0204 and 0556), or gastric cancer cells (paragraph 0558). Li further teaches that Hu-10 induces ADCC (table 7) and endocytosis (table 9).
Alignment of instant SEQ IN NO:7 and SEQ ID NO:203 of Li:
PNG
media_image1.png
613
535
media_image1.png
Greyscale
Alignment of instant SEQ IN NO:8 and SEQ ID NO:204 of Li:
PNG
media_image2.png
606
586
media_image2.png
Greyscale
Claim Rejections - 35 USC § 103
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 text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
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) 1, 2, 5, 7-9, 14-17, 28-32, 37, and 39-40 and is/are rejected under 35 U.S.C. 103 as being unpatentable over Sahin (US20180117174A1) and Li (US20220041712A1, published on February 3, 2020, earliest priority date is February 1, 2019).
Regarding claims 1, 7-9,16 and 39, Sahin teaches antibody drug conjugate, including antibody-vcMMAE conjugates, wherein the antibody binds to the extracellular domain of CLDN18.2 and vc is a Val-Cit linker and drug is MMAE (paragraphs 0010, 0245, and 0264). Regarding claim 14, Sahin teaches that the antibody of the antibody drug conjugate is attached to the linker via amine groups (paragraph 0032). Regarding claim 17, Sahin teaches a pharmaceutical formulation comprising the antibody-drug conjugate of the invention, and a pharmaceutically acceptable diluent, carrier or excipient (paragraph 0034). Regarding claim 40, Sahin teaches a kit comprising a container comprising the antibody drug conjugate (paragraph 0035). Regarding claims 15 and 16, Sahin specifically teaches IMAB362-vcMMAE (same as Ab-(L-U)n, wherein n=1), an anti-CLDN18.2 antibody conjugated to MMAE via cleavable Val-Cit (vc) linker (paragraph 0020). Sahin teaches that the linker can also be maleimidocaproyl (mc) or Val-Cit, or a combination of these in succession (paragraph 0273). Regarding claims 28-32, Sahin teaches administering teaches IMAB362-vcMMAE to bind CLDN18.2 positive cancer cells, including adenocarcinomas of the stomach, gastric, or pancreatic duct (paragraphs 0006-0012, and 0021). Regarding claim 37, Sahin teaches that the method of treating cancer further comprised of administering a cytostatic drug (paragraph 0327).
Sahin does not teach that the antibody-vcMMAE conjugates is comprised of (1) an anti-CLDN18.2 antibody comprising the CDR sequences of SEQ ID NOs:1-6; a VH and VL sequences of SEQ ID NOs: 7 and 8; or (2) a linker comprising mc-Val-Cit. However, these deficiencies are made up in Sahin and Li.
The teachings of Li are described above.
One of ordinary skill in the art before the effective filing date would have been motivated to substitute the IMAB362, anti-CLN18.2 antibody, of IMAB362-vcMMAE of Sahin with the anti-CLN18.2 antibody comprising SEQ ID NOs:203 and 204 of Li to form an antibody drug conjugate comprising anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE in order to generate an art equivalent antibody drug conjugate to treat gastric or pancreatic ductal adenocarcinomas. Sahin teaches an IMAB362-vcMMAE that is administered to treat gastric or pancreatic ductal adenocarcinomas, and Li teaches and antibody drug conjugate comprising anti-CLN18.2 comprising SEQ ID NOs:203 and 204. One of ordinary skill in the art before the effective filing date would have had a reasonable expectation of success for substituting the IMAB362, anti-CLN18.2 antibody, of IMAB362-vcMMAE of Sahin with the anti-CLN18.2 antibody comprising SEQ ID NOs:203 and 204 of Li to form an antibody drug conjugate comprising anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE, because the anti-CLN18.2 antibody comprising SEQ ID NOs:203 and 204 of Li specifically binds to CLN18.2 on cancer cells and stimulates endocytosis to deliver the toxin.
Regarding claim 15, one of ordinary skill in the art before the effective filing date would have been motivated to modify the linker of anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE CLN18.2 antibody of combined teachings of Sahin and Li to comprise mc-vc (same as mc-val-cit) linker, because Sahin teaches that the linker joining MMAE to antibodies could be a combination of mc and vc. One of ordinary skill in the art before the effective filing date would have had a reasonable expectation of success for modifying the linker to form anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-mc-vcMMAE, an art equivalent of anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE, because Sahin teaches that the linker can be either mc or vc, or a combination of them.
Claim(s) 6 and is/are rejected under 35 U.S.C. 103 as being unpatentable over Sahin (US20180117174A1) and Li (US20220041712A1, published on February 3, 2020, earliest priority date is February 1, 2019) as applied to claims 1 and above, and further in view of Kumar (US20170281711A1).
The teachings of Sahin and Li are described above.
Combined teachings of Sahin and Li does not teach an antibody comprising the same sequence as instant SEQ ID NOs:9 and 10. However, these deficiencies are made up in Kumar.
Kumar teaches an antibody comprising the amino acid sequences of SEQ ID NOs:68 and 75, wherein the constant region of SEQ ID NO:68 is the same as the constant region of SEQ ID NO:9, and constant region of SEQ ID NO:75 is the same as instant SEQ ID NO:10 (see alignment below).
Alignment of instant SEQ ID NOs:9 and SEQ ID NO:68:
PNG
media_image3.png
635
540
media_image3.png
Greyscale
Alignment of instant SEQ ID NO:10 with SEQ ID NO:75 of 20170281711
PNG
media_image4.png
353
661
media_image4.png
Greyscale
One of ordinary skill in the art before the effective filing date would have been motivated to substitute the constant regions of anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE with the constant regions of an antibody of SEQ ID NOs:58 and 75 of Kumar to order to generate an art equivalent antibody drug conjugate comprising anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE with a complete VH and VL sequences that have the same sequence as instant SEQ ID NOs:9 and 10. The combined teachings of Sahin and Li teaches anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE that comprise the same VH and VL sequence as instant SEQ ID NOs:7 and 8, and Kumar teaches an antibody comprising a full VH and VL sequences that comprise a constant region that is the same the constant region of SEQ ID NOs:9 and 10. It is well accepted in the arts to modify the constant regions of antibodies.
One of ordinary skill in the art before the effective filing date would have had a reasonable expectation of success for substituting the constant regions of anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE with the constant regions of an antibody of SEQ ID NOs:58 and 75 of Kumar to generate an art equivalent antibody drug conjugate comprising anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE with a complete VH and VL sequences that have the same sequence as instant SEQ ID NOs:9 and 10, because the combined teachings of Sahin and Li teaches anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE that comprise the same VH and VL sequence as instant SEQ ID NOs:7 and 8, and Kumar teaches an antibody comprising a full VH and VL sequences that comprise a constant region that is the same the constant region of SEQ ID NOs:9 and 10.
Claim(s) 37 and 38 is/are rejected under 35 U.S.C. 103 as being unpatentable over Sahin (US20180117174A1) and Li (US20220041712A1, published on February 3, 2020, earliest priority date is February 1, 2019) as applied to claims 1 and 37 and above, and further in view of Zhang (Chinese Journal of Cancer Research, 2020;32(2):263-270).
The teachings of Sahin and Li are described above.
Sahin and Li do not teach a method of treating gastric cancer comprised of administering an antibody-vcMMAE conjugates comprising anti-CLDN18.2 antibody comprising the CDR sequences of SEQ ID NOs:1-6, and oxaliplatin. However, these deficiencies are made up in Zhang.
Zhang teaches treating gastric cancer comprised of administering zolbetuximab, an anti-CLD18.2 antibody, and epirubicin, oxaliplatin and capecitabine (EOX) (abstract). Zhang reaches that the combination therapy extended overall survival with tolerable safety events.
One of ordinary skill in the art before the effective filing date would have been motivated to modify the method of treating gastric cancer comprised of administering anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE of Sahin and Li with further administering EOX of Zhang in order to aggressively treat gastric cancer. The combined method of Sahin and Li teach a method of treating gastric cancer comprised of administering anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE, and Zhang teaches that EOX enhanced the therapeutic effects of anti-CLN18.2 antibody to treat gastric cancer. One of ordinary skill in the art before the effective filing date would have had a reasonable expectation of success for combining anti-CLN18.2 (comprising SEQ ID NOs:203 and 204)-vcMMAE of Sahin and Li with EOX of Zhang to treat gastric cancer, because Zhang teaches that EOX enhanced the therapeutic effects of anti-CLN18.2 antibody to treat gastric cancer.
Conclusion
No claims allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JULIE WU whose telephone number is (571)272-5205. The examiner can normally be reached M-F 9-5PM.
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, Patricia Mallari can be reached at 571-272-4729. 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.
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643