DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on April 9, 2026 has been entered.
Claim 2 has been canceled.
Claims 1 and 3-20 are pending.
Claims 4 and 5 stand withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on August 12, 2025.
Claims 1, 3, and 6-20 are currently under consideration as they read on the elected species of L234A and axial spondyloarthritis.
3. 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.
4. Claims 1, 2, and 6-20 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 for the reasons of record.
The claims are drawn to a method of treating arthritis including axial spondyloarthritis or a method of treating pain associated with an inflammatory condition in a subject in need thereof by administering to the subject an effective amount of a pharmaceutical composition comprising a bispecific anti-inflammatory IgG antibody comprises a TREM1 VH domain and a VL domain, an IL-17 binding VH domain and VL domain, and a heterodimeric Fc region comprise a first constant region and a second constant region, wherein the administration is effective to treat one or more symptoms associated with TNFα mediated inflammation and wherein contacting cells in vitro with the bispecific antibody results in a lower secretion of TNFα as compared to contacting comparable cells with a combination of a monospecific antibody that binds TREM1 and IL-17.
The specification discloses that human IL-17 family has IL-17A, IL-17B, IL-17C, IL-17D, IL-17E, and IL-17F and also discloses the amino acid sequences for each family member (e.g. see [0100] and Table 1). IL-17 cytokines are involved in proinflammatory response. The specification further discloses VH CDRs and VH sequences in Tables 2 and 3 in page 26-27 of the specification as-filed. The specification discloses triggering receptor expressed on myeloid cells (TREM1) belons to the Ig superfamily of receptors and is highly expressed on subsets of myeloid cells including neutrophils, monocytes, and macrophages and is implicated in innate and adaptive immune function by amplifying inflammatory response (e.g. see [0113] in page 32 of the specification as-filed). The specification further discloses the amino acid sequences of CDRs of the VH and VL of anti-TREM1 antibodies (e.g. see pages 33-51 of the specification as-filed).
There is insufficient written description in the specification as-filed of the engineered a bispecific anti-inflammatory IgG antibody comprising a TREM1 binding VH and VL and an IL-17 binding VH and VL for the method of treating arthritis or axial spondyloarthritis as recited in the instant claims.
Applicant’s arguments in conjunction with the Vemuri declaration under 37 CFR 1.132 have been fully considered but have not been found persuasive.
Applicant and the Vemuri declaration states:
the anti-IL-17 binding domains and the anti-TRIM binding domains were well known in the art at the time the instant invention was filed, including the anti-IL-17 antibody secukinumab comprising VH of SEQ ID NOs:9 and SEQ ID NO:11 and anti-IL-17 antibody ixekizumab comprising VH of SEQ ID NOs:10 and 12, also in Tables 13 and 17 in the specification as-filed.
at the time the instant invention was filed, monospecific IgG antibodies that bind TREM1 and monospecific IgG that bind IL-17 were well-known to scientists working in the field of antibodies.
In Example 2 in the instant specification, applicant disclosed a framework for evaluating the specificity of and cellular response and shows the bispecific IgG causes a greater reduction in TNFα secretion as compared to a combination of monospecific anti-TREM1 antibody and monospecific anti-IL17 antibody, which is surprising and unexpected.
Example 3 provides proof of concept for a future phase 1 trail for the bispecific antibody.
One of ordinary skill in the art would understand that the exemplified bispecific IgG is not limited to the particular exemplary antibody but rather apply to any domain that binds IL-17 and domain that binds TREM1 would also be expected to be useful for reducing TNFα secretion and treating an inflammatory condition.
Scientists can select any well-known monospecific antibody that binds TREM1 and IL-17 to make bispecific anti-inflammatory antibody and select antibodies that would cause greater reduction in TNFα secretion as compared to a combination of the monospecific antibodies. The well-known monospecific antibodies are disclosed in prior art such as Pincetic et al. (US 2025/0092131), FIGS. 15A-15J, FIGS. 16A-16J, or Pashine et al. (US 2022/0327139 and US 2024/0228615).
As such, the Vemuri declaration asserts that the rejection should be withdrawn.
This is not found persuasive for following reasons:
Contrary to applicant’s assertion, once again the generic recitation of VH and VL without setting forth at least the minimal structure of the binding domains do not have sufficient written description support in the instant specification. A definition by functions, e.g. TREM1 binding and IL-17 binding and newly added limitation of “wherein the administration is effective to treat one or more symptoms associated with TNFα mediated inflammation in the subject and wherein contacting cells in vitro with the bispecific inflammatory IgG antibody results in a lower secretion of TNFα…”, does not suffice to define the genus because it is only an indication of what the bispecific anti-inflammatory IgG antibody does rather than what it is.
The Vemuri declaration is relying upon certain biological activities and the disclosure of a limited representative number of species of bispecific IgG antibody having specific VH and VL amino acid sequences for each of the binding domains
to support an entire genus of diverse and unrelated TREM1 binding VH and CL and IL-17 binding VH and VL.
The instant invention encompasses the use of any bispecific anti-inflammatory IgG comprising TREM1 binding VH and VL and IL-17-binding VH and VL that result in anti-inflammatory, effective to treat one or more symptoms associated with TNFα mediated inflammation, and lower secretion of TNFα as compared to combination of the respective monospecific antibodies. Yet the specification does not provide sufficient written description as to the identifying structural features of said bispecific anti-inflammatory IgG antibodies and the correlation between the chemical structure and the desired binding and inhibitory function.
Contrary to the assertion made by Vemuri declaration that the antigen binding site of the antibodies do not matter so long as they bind TREM1 or IL-17 they can be combined to produce the recited bispecific IgG to treat inflammation, note that it is known that an anti-TREM1 antibody can be agonistic (mimics its natural signaling and promote myeloid cell activation and cytokine release) and antagonistic (binds TREM1 without activating it and prevents ligand bindings and block downstream signaling). For example, Li et al. (Pharmacological Research 2024, 204;107212:1-16) teach that PY159, an agonistic TREM1 monoclonal antibody elicited proinflammatory effect reflected in upregulation of proinflammatory cytokines including TNF (e.g. see left col. in page 10).
Therefore, the species of antibodies disclosed in the specification are not reasonably representative of the species of all possible TREM1 binding VH and VL domain and an IL-17 binding VH and VL domain because of the structural diversity found in antibodies that bind the same antigen as discussed by for example Edwards et al., Llyod et al., and Goel et al. discussed previously. Further, as has been discussed before, identifying an antibody simply on the basis of what it binds and what it does rather than by identifying the sequence/structure of the antibody in question is generally insufficient to provide sufficient written description of the antibody in question.
Further, one cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481, 1483.
Here, contrary to applicant and the Vemuri declaration’s reliance on published antibodies, note that applicant appears to believe that any monospecific anti-TREM1 antibodies including those listed in publications after the effective filing date of the instant application (June 22, 2023) such as Pincetic et al. (US 2025/0092131) or Pashine et al. (US2024/0228615) can be relied upon to provide written description support for the instant application.
There is insufficient written description of the claimed bispecific anti-inflammatory IgG antibodies broadly encompassed by the claimed invention. There is a lack of disclosure of sufficient relevant identifying characteristics coupled with a known or disclosed correlation between function and structure of the broadly diverse compounds employed in the claimed methods.
Furthermore, secondary considerations such as the surprising and unexpected results asserted in the Vemuri declaration are immaterial to rebut the lack of written description support for the claimed bispecific anti-inflammatory IgG antibodies.
Not having “the bispecific anti-inflammatory IgG antibodies” which have been specifically named or mentioned in a sufficient manner that provides sufficiently detailed, relevant identifying characteristics … i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics, one is left to select from the myriad of possibilities from antibodies solely defined by the antigens of TREM1 and IL-17 with insufficient guides indicating or directing that this particular selection should be made rather than any of the many other which could be made or selected.
Contrary to the assertion made by the Vemuri declaration that any or all monospecific anti-TREM1 antibody or monospecific anti-IL-17 antibody can be used for the selection, note that while they may lead to numbers games about how many compounds can be disclosed by the use of generic formulas or screening assays, they do little to provide the statutory written description required for patent claims to actual inventions.
As such, applicant’s arguments have not been found persuasive.
5. Claims 1, 2, and 6-20 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention for the reasons of record.
The claims are drawn to a method of treating arthritis including axial spondyloarthritis or a method of treating pain associated with an inflammatory condition in a subject in need thereof by administering to the subject an effective amount of a pharmaceutical composition comprising a bispecific anti-inflammatory IgG antibody comprises a TREM1 VH domain and a VL domain, an IL-17 binding VH domain and VL domain, and a heterodimeric Fc region comprise a first constant region and a second constant region, wherein the administration is effective to treat one or more symptoms associated with TNFα mediated inflammation and wherein contacting cells in vitro with the bispecific antibody results in a lower secretion of TNFα as compared to contacting comparable cells with a combination of a monospecific antibody that binds TREM1 and IL-17.
The specification discloses that human IL-17 family has IL-17A, IL-17B, IL-17C, IL-17D, IL-17E, and IL-17F and also discloses the amino acid sequences for each family member (e.g. see [0100] and Table 1). IL-17 cytokines are involved in proinflammatory response. The specification further discloses VH CDRs and VH sequences in Tables 2 and 3 in page 26-27 of the specification as-filed. The specification discloses triggering receptor expressed on myeloid cells (TREM1) belons to the Ig superfamily of receptors and is highly expressed on subsets of myeloid cells including neutrophils, monocytes, and macrophages and is implicated in innate and adaptive immune function by amplifying inflammatory response (e.g. see [0113] in page 32 of the specification as-filed). The specification further discloses the amino acid sequences of CDRs of the VH and VL of anti-TREM1 antibodies (e.g. see pages 33-51 of the specification as-filed).
However, 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.
Applicant’s arguments in conjunction with the Vemuri declaration under 37 CFR 1.132 and various legal citations have been fully considered but have not been found persuasive.
The Vemuri declaration has been addressed above. Applicant further argues that the claims have been amended to add the limitations of effective to treat on e or more symptoms associated with TNFα mediated inflammation and in vitro lower secretion of TNFα (see amended claim 1). Applicant asserts that the recited bispecific antibody binds TREM1 and IL-17 simultaneously, where on the surface of TREM1 and IL-17 it binds is inconsequential, anywhere will do. Applicant argues again that the specification disclosed methods of making multispecific antibodies in, e.g. [0089] and [0093], and provide nexus between the bispecific antibody and reduction in inflammation, as well as in vitro working examples, e.g. in FIG. 2B. Thus, applicant asserts that the necessary experiments are less than Amgen. Therefore, applicant argues that the rejection should be withdrawn.
This is not found persuasive because there is insufficient evidence either in the specification or in the Vemuri declaration to show that where the bispecific antibody binds do not matter in correlating with the function of anti-inflammatory, once again, it is known that
anti-TREM1 antibodies can be agonist or antagonist, and the antagonist anti-TREM1 antibodies not agonist antibodies activate TREM1 in solution or synergizing with TREM1 ligands [(e.g. see left col. in page 3 in Pincetic et al. (US 2025/0092131, reference of record)].
Also, as discussed above, it is known that an anti-TREM1 antibody can be agonistic (mimics its natural signaling and promote myeloid cell activation and cytokine release) and antagonistic (binds TREM1 without activating it and prevents ligand bindings and block downstream signaling). For example, Li et al. (Pharmacological Research 2024, 204;107212:1-16) teach that PY159, an agonistic TREM1 monoclonal antibody elicited proinflammatory effect reflected in upregulation of proinflammatory cytokines including TNF (e.g. see left col. in page 10).
Moreover, contrary to applicant’s assertion, there is no working examples of the claimed method of treating arthritis and axial spondyloarthritis in a subject by administering the engineered bispecific anti-inflammatory IgG antibodies comprising a TREM1 binding VL and VL and an IL-17binding VH and VL, wherein the administering is effective to treat one or more symptoms associated with TNFα mediated inflammation and wherein contacting cells in vitro results in a lower secretion of TNFα secretion.
Applicant is relying upon certain biological activities and the disclosure of a limited representative number of species such as structurally defined anti-TREM1 antibodies and anti-IL-17 antibodies in an in vitro experiment to support an entire genus of diverse and structurally unrelated bispecific antibodies. The instant invention encompasses any bispecific antibodies that results in the desired lower secretion of TNFα in vitro yet the instant specification does not provide sufficient guidance and direction as to the structural features of said bispecific antibodies other than the structurally defined ones and the correlation between the chemical structure and the desired binding and inhibitory function.
The scope of the required enablement varies inversely with the degree of predictability involved and in cases involving unpredictable factors such as physiological activity more may be required. See MPEP 2164.03 and 2164.02.
Given the relatively incomplete understanding in the biotechnological field involved and the lack of a reasonable correlation between the narrow disclosure in the specification and broad scope of protection sought in the claims; the lack of enablement is deemed appropriate. See MPEP 2164.08.
6. 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.
7. 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.
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.
8. Claims 1, 3 and 6-20 are rejected under 35 U.S.C. 103 as being unpatentable over Pincetic et al. (US 2020/0131264) in view of Wendling et al. (Expert Opinion on Biological Therapy, 2019, 19;1:55-64), Yang et al. (US 2021/0061925), and Labrijn et al. (Nature Review 2019, 18;585-608) as evidenced by the disclosure in pages 76-77 of the instant specification as filed for the reasons of record.
Pincetic et al. teach Triggering receptor expressed on myeloid cells (TREM1) consists of an ectodomain with a single Ig V-type domain, a transmembrane region, and a short cytoplasmic tail, and can produce pro-inflammatory mediators such as TNF (e.g. see [0004]). Pincetic et al. teach antagonistic anti-TREM1 antibody specifically binds and inhibit TREM1 activities (e.g. see [0022] and [0169]) which can inhibit the pro-inflammatory mediator production induced by TREM1.
Pincetic et al. teach anti-TREM1 antibodies comprises a VH and a VL, and a pharmaceutical composition comprises the antibodies (e.g. see Abstract, [0016], claims 111-133, and [0036]).
Pincetic et al. further teach that that anti-TREM1 antibodies are human IgG1 and can have amino acid substitutions including L234A, L235A, and P329A (e.g. see [0025]). Pincetic et al. teach that TREM1 is involved in arthritis and anti-TREM1 antibody can be used to treat multiple inflammatory disorders where excessive myeloid cell activation or survival is pathogenic such as arthritis (e.g. see [0007], [0013], [0037], [0306], Example 22).
Pincetic et al. teach the anti-TREM1 antibodies can be in a bispecific form recognizing a first antigen and a second antigen (e.g. see [0195] and [0231]). Pincetic et al. teach heterodimeric antibody having different substitutions in first CH3 region and the second CH3 region (e.g. see [0349]). Pincetic teaches oral administration of the antibodies (e.g. see [0400]).
The reference teachings differ from the instant invention by not describing an IL-17 binding VH and VL and treating axial spondyloarthritis.
Wendling et al. teach anti-IL-17A monoclonal antibodies for the treatment of ankylosing spondylitis (see Title). Specifically, Wendling et al. teach:
PNG
media_image1.png
160
388
media_image1.png
Greyscale
Wendling et al. teach that a body of evidence for implication of IL-23/Th17 pathway in the pathogenesis of ankylosing spondylitis (AS) and it was also known that elevated serum levels of IL-17 was found in AS patients (e.g. see left col. in page 56). Wendling et al. teach that one of the cellular targets of IL-17 is TNFα which causes inflammation (e.g. see Table 2 in left col. in page 56).
Yang et al. teach a bispecific antibody comprising a VH chain A and VL chain A forming a first antigen binding domain and a VH chain B and a VL chain B forming a second antigen binding domain, and a heterodimeric Fc region comprising two constant regions, e.g. see FIG. 1A or copy below:
PNG
media_image2.png
558
460
media_image2.png
Greyscale
Yang et al. teach that the two Fc region is heterodimeric with one Fc comprises amino acid substitutions L234A, L235A, and P329A and the Fc is from human IgG1 (e.g. see [0530]). Yang et al. teach that bispecific antibody that binds to various antigens including TREM1 and IL17 (e.g. see claim 120). Yang et al. teach that the binding protein is useful for neutralizing cytokine activities and treating inflammatory disorders (e.g. see [0546]).
Labrijn et al. teach that an attractive bispecific feature is their potential for novel functionalities, activities that do not exist in mixtures of the parental antibodies. The physical linkage of the two binding specificities creates a dependency that can be temporal, with binding events occurring sequentially or spatial, with binding events occurring simultaneously (e.g. see Abstract and Fig. 5).
As evidenced by the instant specification, the claimed SEQ ID NO:199 is the amino acid sequence of the naturally occurring human IgG Fc region (e.g. see pages 76-77 of the specification as-filed). Therefore, Yang’s human IgG1 from which the L234A, L235A, and P329A were made from would inherently have the same amino acid sequences of SEQ ID NO:199 as recited in the instant claims.
It would thus be obvious to one of ordinary skill in the art at the time the invention was filed to combine the teachings of the prior art to make a bispecific antibody comprising two antigen binding domains, each comprises a VH and a VL that binds TREM1 and IL-17 as well as two heterodimeric Fc regions and administered the bispecific antibody to treat arthritis including axial spondyloarthritis.
On of ordinary skill in the art would have been motivated to do so, and have a reasonable expectation of success, because Pincetic et al. teach anti-TREM1 antibody and its bispecific form having Fc mutations is useful for treating arthritis, Wendling et al. teach that monoclonal anti-IL-17 antibodies are effective in treating ankylosing spondylitis. An ordinary skill in the art would have been motivated to combine the available anti-TREM1 antibody and the anti-IL-17A antibody both known to treat arthritis following the methods of producing bispecific antibody having two heterodimeric Fc region to produce a bispecific anti-TREM1 and anti-IL-17A antibody with the Fc mutations that facilitate the formation of heterodimers. Given that the anti-TREM1 antibody and the anti-IL-17 antibody were each known to be anti-inflammatory, the bispecific anti-TREM1xIL-17 antibody would also be anti-inflammatory and to be effective in treating TNFα mediated inflammation and capable of lower secretion of TNFα when contacting cells in vitro.
Given the well-known therapeutic effects of the antibodies targeting TREM1 and IL-17A in treating arthritis including ankylosing spondylitis, an ordinary skill in the art would be able to administer a bispecific antibody that binds both TREM1 and IL-17A in a method of treating arthritis with a reasonable expectation of success.
Given that the combined teachings of the prior art yielded the same method of treating arthritis by administering the same bispecific antibody, the prior art methods would have inherently achieved the same results as the instantly claimed methods, e.g. directly inhibits TREM1 activity or indirectly inhibits TREM1 activity by reducing TREM1 expression by reducing IL-17 activity or reduces a level of IL-17, as recited in, e.g. claims 7-10 and 12).
Applicant’s arguments have been fully considered but have not been found persuasive.
Applicant argues that none of the reference teach that the bispecific antibody that binds TREM1 and IL-17 will cause an unexpected and surprising reduction in TNFα secretion as compared to a combination of monospecific TREM1 binding and IL-17 binding antibodies as shown in FIG. 2B and in the Vemuri Declaration. As such, applicant asserts that the rejection should be withdrawn.
This is not found persuasive for following reasons:
Contrary to applicant’s arguments of unexpected results based upon FIG.2B, note that the feature of the structurally defined single bispecific antibody as shown in FIG. 2B is not commensurate in scope with the instant claims that are broadly drawn to a bispecific IgG antibody that comprises a TREM1 binding VH and VL and an IL-17 binding VH and VL.
Further, contrary to applicant’s reliance on the unexpected results, note that unexpected properties do not necessarily guarantee that a new compound is nonobvious. While a “marked superiority” in an expected property may be enough in some circumstances to render a compound patentable, a “mere difference in degree” is insufficient. And “differences in degree” of a known and expected property are not as persuasive in rebutting obviousness as differences in “kind”—i.e., a new property dissimilar to the known property.
Here, it was known that anti-TREM1 antibody and anti-IL-17 antibody can inhibit proinflammatory cytokines such as TNFα. For example, Pincetic et al. teach antagonistic anti-TREM1 antibody specifically binds and inhibit TREM1 activities (e.g. see [0022] and [0169]) which can inhibit the pro-inflammatory mediator production induced by TREM1 including TNFα. Wendling et al. teach that IL-17 was found to be pathogenic in AS patients (e.g. see left col. in page 56) and that one of the cellular targets of IL-17 is TNFα which causes inflammation (e.g. see Table 2 in left col. in page 56). Thus, anti-IL-17 antibody would be expected to inhibit IL-17 function thereby inhibit its cellular targets including TNFα. Given that both monospecific anti-TREM1 and anti-IL-17 antibodies were known to be able to reduce the proinflammatory cytokine TNFα, it would be expected that the bispecific antibody would also lower the TNFα more.
Furthermore, given that the bispecific antibody can simultaneously engage TREM1 and IL-17 as compared to the two monospecific antibodies and in view of the known benefit of having novel features that do not exist in mixtures of the two monospecific antibodies (disclosed by Labrijn et al.), the results shown in FIG. 2B in the instant application (lower secretion of TNFα as compared to a combination of the two monospecific antibodies) would be expected.
As such, applicant’s arguments have not been found persuasive.
9. No claim is allowed.
10. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHUN DAHLE whose telephone number is (571)272-8142. The examiner can normally be reached Mon-Fri 6:30am-4:00pm.
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, Misook Yu can be reached at 571-272-0839. 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.
/CHUN W DAHLE/Primary Examiner, Art Unit 1641
Prosecution Insights