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 .
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 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.
Status of Claims
Claims 1, 6-7, 9, 13-17, 19 and 21 are pending. Claims 13-14 are withdrawn. Claims 1, 6-7, 9, 15-17, 19 and 21 are currently under examination.
Withdrawn Rejections
In light of the amendments, the objection is hereby withdrawn.
In light of canceled claims 23-24, the 35 U.S.C. 112(b) rejection is hereby withdrawn.
In light of the amendments, the Enablement rejection over claims 1, 6-7, 9, 15-17 and 19 are hereby withdrawn.
Maintained Rejections
Claim Rejections - 35 USC § 112
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.
Enablement
Claim 21 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabled for detecting a capsid polypeptide of a non-enveloped virus of the family parvoviridae in a sample from a subject in a sandwich immunoassay comprising contracting said sample with a base, wherein said contacting said sample with a base comprising incubating the sample at pH at least 10.5 and at most 14, neutralizing the sample contacted the base to a pH 6 to 9 before detecting said capsid polypeptide of the sample, does not reasonably provide enablement for detecting a capsid polypeptide in a sandwich immunoassay with the sample at pH at least 10.5 to at most 14. 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.
As set forth in In re Wands, 858 F .2d 731, 8 USPQ2d 1400 (Fed. Cir. 1988), enablement requires that the specification teach those in the art to make and use the invention without undue experimentation. Factors to be considered in determining whether a disclosure would require undue experimentation include 1) the nature of the invention, 2) the state of the prior art, 3) the predictability or lack thereof in the art, 4) the amount of direction or guidance present, 5) the presence or absence of working examples, 6) the quantity of experimentation necessary, 7) the relative skill of those in the art, and 8) the breadth of the claims.
The nature of the invention relates to detecting a capsid polypeptide of a non-enveloped virus of parvoviridae in a sample through a sandwich immunoassay that requires a pre-treatment condition with a base to produce a sample at a pH of at least 10.5 to 14.
The claims are broad because they encompass detecting a specific capsid polypeptide in the sample at a pH of at least 10.5 to 14. One skilled in the art would recognize that it is not possible to perform an immunoassay for a specific affinity with the claimed pH without first neutralizing the extreme condition in the sample for immunoassay detection. Meanwhile, the instant specification only discloses in Table 2 that detection of the capsid polypeptide is at pH 6 to 9. However, Applicant does not disclose a sensitivity detection of sample at a high pH of above 9 to 14. The specification provides no direction to guide the skilled artisan to perform immunoassay for detecting capsid polypeptide at the claimed pH range.
In particular, Matikainen et al. teach that antibodies bound readily to antigen from pH 4 to 9, but had a reduced binding efficiency at more extreme pH conditions (see abstract). Binding was reduced at extreme pH conditions, possibly due to denaturation of antibodies and such denaturation, as well as dissociation of antibody-antigen complexes at extreme pH conditions (see pg. 215, para. 1 of Discussion). (“Effect of pH on Reactivity of Monoclonal Antibodies to Chlamydia”, Journal of Immunological Methods, vol. 75 (1984), pgs. 211-216).
As is appreciated in the art, one skilled in the art would face an undue burden of examination in extrapolating the data presented regarding the immunoassay detection of capsid polypeptide in a sample of high pH condition. The specification fails to enable the skilled artisan to employ a sandwich immunoassay for detecting a capsid polypeptide at high pH conditions. In particular, the specification only provides guidance to neutralizing the sample to pH 6 to 9 before performing said immunoassay.
In summary, the prior art recognizes that at extreme pH conditions will denature and dissociate proteins and antibody-antigen complexes. Coupled with the direction/guidance or lack thereof presented in instant specification regarding immunoassay detection at high pH conditions, there would be an undue experimentation to extrapolate data for the detection of capsid polypeptide.
Written Description
Claims 1, 6-7, 9, 15-17, 19 and 21 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 MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of an application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient.” MPEP § 2163. While all of the factors have been considered, a sufficient amount for a prima facie case are discussed below.
Further, to provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include: a) the scope of the invention; b) actual reduction to practice; c) disclosure of drawings or structural chemical formulas; d) relevant identifying characteristics including complete structure, partial structure, physical and/or chemical properties, and structure/function correlation; e) method of making the claimed compounds; f) level of skill and knowledge in the art; and g) predictability in the art.
Meanwhile, claim 1 is drawn to a method for detecting a capsid polypeptide of a non-enveloped virus of the family Parvoviridae in a sample from a subject in a sandwich immunoassay comprising contacting the sample with a base that comprises incubating said sample at a pH of at least 10.5 and at most 14; and detecting the capsid polypeptide of said virus in said sample, wherein the capsid polypeptide is from VP1, VP2 and combinations thereof (claims 1, 6-7, 9, 15-19). Claim 21 is drawn to a method detecting a capsid polypeptide of a non-enveloped virus of the family Parvoviridae in a sample from a subject in a sandwich immunoassay, wherein the improvement comprises contacting the sample with a base and pre-incubating the sample and base at a pH of at least 10.5 to at most 14 prior to detecting.
These claims as a whole are generic to using any sandwich immunoassay (i.e., any capturing probe) for alkaline-treated capsid polypeptide i.e., pH at least 10.5 and at most 14. Explicitly in the claims is that such sandwich immunoassay must possess certain functional characteristics; namely, said immunoassay detects specific claimed capsid polypeptide in or after harsh treatment (i.e., high pH).
Meanwhile, the specification discloses that previously immunological diagnosis of Parvovirus B19 in blood samples was used with acidic pretreatment, aimed at disassembling viral particles in order to increase sensitivity of the assay. However, acid treatment causes a reversible denaturation, allowing at least partial re-assembly of viral particles. Moreover, potentially confounding immunoglobulins from the blood sample may renature as well and , thus, are not effectively removed and the chaotropic salt may disturb the detection reaction and, if removed, may allow renaturation of capsids and confounders (see page 2, lines 6-15, as filed specification dated 05/05/2021). In this particular case, the specification has disclosed that when using harsh conditions to pretreat the sample certain unpredictable conditions may occur and disturb the detection reaction.
However, the specification fails to provide a representative number of species for the claimed generic immunoassay having the desired binding properties for detecting specific capsid polypeptides (claim 1) or all capsid polypeptides (claim 21) using harsh conditions (i.e., basic pH conditions). Noted that even if Applicant overcomes the enablement rejection (see above), the skilled artisan would not be able to visualize or recognize the identities of members of the genus based on examples of monoclonal anti-Parvovirus B19 capsid antibodies disclosed in Table 1 because the specification has not disclosed diverse chemical structures of said monoclonal anti-Parvovirus B19 capsid antibodies (see instant Table 1).
Protein chemistry is unpredictable. In particular, the specification discloses a prescreening of monoclonal antibodies prior to the sandwich immunoassay in alkaline conditions (see (c-d) of pages 27 and 28). The pre-screening process has selected monoclonal antibodies that are 100% reactive to native VLP. However, Table 1 also shows that when pretreated samples of VLP were added against the selected antibodies, low binding affinities for certain antibodies such as antibodies of 2.053, 2,073, and 2.077 or inconclusive data. Even at a small scale of selected monoclonal antibodies that are 100% reactive to native VLP, these antibodies may lack the binding affinity to pretreated basic solution sample. Thus, the specification fails to describe a representative number of species with respect to the claimed generic antigenic properties to detect the capsid polypeptide with the claimed pH treatment.
For example, Matikainen et al. teach that antibodies bound readily to antigen from pH 4 to 9, but had a reduced binding efficiency at more extreme pH conditions (see abstract). Binding was reduced at extreme pH conditions, possibly due to denaturation of antibodies and such denaturation, as well as dissociation of antibody-antigen complexes at extreme pH conditions (see pg. 215, para. 1 of Discussion). (“Effect of pH on Reactivity of Monoclonal Antibodies to Chlamydia”, Journal of Immunological Methods, vol. 75 (1984), pgs. 211-216, of record 892 dated 07/17/2025).
In particular, as stated in the prior art, the nature of the antibody-antigen complexes and antigen proteins are impacted by the use of extreme pH conditions such as denaturation. Meanwhile, the specification has disclosed that harsh condition produces structural changes such as denaturation to the capsid polypeptide which alter the structure of said capsid polypeptide. Meanwhile, the specification has not provided enough evidence that any generic antibody would be able to detect said capsid polypeptide after the sample has been pretreatment with extreme basic solution.
In summary, the specification fails to provide adequate written description for the genus of “sandwich immunoassays”, as said assay is being described in terms of desired functional properties (i.e., detecting the capsid polypeptide of a sample during or after high pH treatment). Based on the nature of the invention and a disclosure of a small subset of specific monoclonal antibodies, a skilled artisan would not be able to envision the genus of chemical structures for detecting a capsid polypeptide in a sample treated with high pH solutions such that certain affinity chemical structures of the capsid polypeptide against the antibody would be denatured. The person would not be able to predict the outcome of antigen-antibody complexes without a representative number of species. Therefore, the specification does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the claimed invention.
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 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.
Claims 1, 6-7, 9, 15-17, 19 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Kumagai et al. (JP2008145181, published 06/26/2008, of record 892 07/17/2025) in view of Yuan et al. (“Canine Parvovirus Capsid Assembly and Differences in Mammalian and Insect Cells”, Virology, vol. 279, pgs. 546-557, published 2001, see IDS submitted on 02/09/2018).
With respect to claims 1, 15, 17 and 21, Kumagai teaches a parvovirus B19 antigen test comprising treating blood sample (see abstract). Kumagai teaches an attempt to increase the sensitivity of the parvovirus B19 antigen test, an immunological measurement method was used and the sample was treated with an acid or denaturing agent to increase the reactivity of the antigen (see para. [0004] of page 4). Kumagai teaches measuring anti-parvo virus IgM antibody in the sample (see abstract). Kumagai teaches the parvovirus B19 has no envelope, single-stranded DNA and structural proteins (VP1 and VP2), which make up the capsid (see para. [0002] of page 1). Hence it would read on the capsid polypeptide is VP1, VP2 or combinations. Kumagi teaches an acid or denaturing agent to increase the reactivity of the antigen (see para. [0004] of para. 4). Kumagi also teaches using sodium hydroxide (see para. [0026] of pg. 37). Kumagai teaches detecting using a sandwich immunoassay (see page 8 or para. [0036] of page 52). Kumagi teaches the sandwich assay is used with monoclonal anti-parvovirus B19 antibodys (see para. [0014] of pg. 17). Kumagi teaches preparation of parvovirus antigen-immobilized in reaction solution pH 7.0 buffer solution (see para. [0033] of pg. 47). Kumagai teaches during the architect assay, the pH is at 7.0 (see bottom of pg. 48). Meanwhile, Kumagi teaches guanidine, quinidine salt, or a derivative thereof added for the sample has a pH range 4.5 to 6.5 (see para. [0012] of pg. 15). Kumagi also teaches physiological measurement results were obtained (see pg. 14, middle of para. 1).
Kumagai does not teach contacting the sample with a base comprises incubating the sample at a pH of at least 10.5 and at most 14 and does not explicitly teach neutralizing the sample contacted with the base to a pH between 6 to 9 before or during detecting said capsid polypeptide and wherein denatured polypeptides generated in step (a) are not solubilized by addition of a chaotropic agent.
Yuan teaches examining a capsid polypeptide with the expression of VP1 and VP2 or only VP2 of a non-enveloped virus from the family Parvoviridae (Abstract and Fig. 6). Yuan teaches capsids treated with pH < 3.0 or pH > 11.0 to release VP1 and VP2 monomers, as well as complexes with the sizes of VP dimers, trimers, and pentamers (see pg. 550, right col., para. 1; and Fig 6 C, empty capsid and Fig. 6D). Yuan further teaches that after high-pH treatment only small amounts of the trimer were seen (pg. 550, right col., para. 1). Yuan teaches detecting VP1 or VP2 with rabbit anti-VP1/VP2 antibodies (see Fig. 6, caption). Yuan teaches monoclonal antibody (see pg. 554, right col., para. 2).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to have pre-treated the sandwich immunoassay of detecting parvovirus B19 antigens as taught by Kumagai with a basic solution to produce a pH > 11.0 as taught by Yuan because Kumagai recognizes the attempt to increase the sensitivity of the parvovirus B19 immunological antigen test is to pretreat the sample with an acid or denaturing agent to increase the reactivity of the antigen and Yuan teaches that prior to detecting VP1 and VP2 through immunoassay (western blot) the parvovirus capsid can be treated with either low pH < 3.0 (acid) or pH > 11.0 (base) to release VP1 and VP2 structures. Therefore, it would have been obvious to the person to have pretreated the sample of Kumagai with a basic solution to release VP1 and VP2 and neutralizing the sample to pH 6-9 before or during detection because Kumagai teaches that the measurement results were detected under physiological pH and the pretreatment of acid or denaturing agent increases reactivity of the antigen and Yuan recognizes that low pH < 3.0 (acid) and pH > 11.0 (base) treatments release VP1 and VP2 structures for immunoassay detection. The person would have also performed a basic treatment because acidic and basic treatments are recognized to release VPI and VP2.
Additionally, it would have been obvious to the person forming a basic pretreatment for the sample to have not solubilized the sample with a chaotropic agent because Kumgai teaches that the guanidine chaotropic agent produces an acidic pH condition.
The person would have reasonably expected success in using a base for preteatment in Kumagai’s sandwich immunoassay because Kumagai recognizes using acid treatment prior to assay detection and it has been recognized by Yuan that acidic and basic treatments release VP1 and VP2 structures for immunoassay detection.
With respect to claim 6, Kumagai teaches a parvovirus B19 antigen test comprising treating the sample i.e. blood serum plasma (see abstract and para. [0002] of pg. 2).
With respect to claim 7, Kumagai teaches a preparation of activator solution with sodium hydroxide (see pg. 37, para. [0027]). Kumagai does not explicitly teach step (a). However, it would have been obvious to have used sodium hydroxide as the base at pH of at least 10.5 and at most 14 because Kumagai and Yuan both recognize a denaturing agent before immunoassay.
With respect to claim 9, Kumagi teaches incubate to specifically react the antigen in the sample with the antibody on the microparticle (see pg. 33, para. [0023]). However, Kumagi and Yuan do not teach incubating the sample in the presence of the base for at least 2 minutes. It has long been settled to be no more than routine experimentation for one of ordinary skill in the art to discover an optimum incubation time for a result effective variable in denaturing/dissociating for immunoassay detection. “[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation” Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). “No invention is involved in discovering optimum ranges of a process by routine experimentation.” Id. at 458, 105 USPQ at 236-237. The “discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art.” As stated above, Kumagi recognizes incubation for immunoassay and Yuan teaches an effective basic condition to release VPI and VP2 for immunoassay detection (i.e., Western blot). Therefore, it would have been obvious for the person of ordinary skill to discover the optimum effective incubation time in using a base for immunoassay detection.
With respect to claim 16, Kumagai teaches a parvovirus B19 antigen test comprising treating the sample i.e. blood serum plasma (see abstract and para. [0002] of pg. 2).
With respect to claim 19, Kumagi does not explicitly teach not removing any polypeptide denatured by said contacting from said sample. Yuan teaches after treated with pH > 11.0 to release VPI and VP2 structures, not removing any polypeptides denatured by said contacting from said sample (see Fig. 6C and caption).
With respect to claim 21, see above in claim 1.
Response to Arguments
Applicant's arguments filed 11/17/2025 have been fully considered but they are not persuasive.
Enablement rejection
Applicant argues on page 6 of the Remarks that the amendments overcome the enablement rejection.
The argument is not found persuasive for claim 21 as the claim is an independent claim that does not have all the limitation to overcome the enablement rejection as set forth above.
Written description rejection
Applicant argues on page 7 that the claim has been amended to recite neutralization to pH 6-9 before or during detection. Thus, the detection occurs at neutral pH after alkaline pretreatment and neutralization. Applicant furth argues that Table 1 demonstrates that all tested antibodies work after alkaline treatment. Applicant argues that variation in signal intensity does not negate written description. Applicant argues on page 8 that chemical structures are not required for method claims. The claims are directed to a method of detection using a sandwich immunoassay, not to specific antibody compositions. The specific chemical structures of the antibodies are not limitations of the claimed method.
The arguments are not found persuasive for the following reasons. Even though sandwich immunoassays are recognized in the art for detection, the artisan would also recognize that sandwich immunoassays are based on the quality of the antibody and target structures for detection. In other words, if the structures of the antibodies are not significant in detecting an alkaline-pretreated capsid polypeptide of a non-enveloped virus of the family Parvoviridae, then the specification would have used (1) polyclonal antibodies and (2) a screening for the quality of monoclonal antibodies from specific hybridoma cells would have not been emphasized and produced in the instant specification (i.e., Table 1 and Example 1). Meanwhile, the specification only performed monoclonal anti-Parvovirus B19 capsid antibodies for the claimed reactions. Therefore, structures of the antibodies and targets are important in sandwich assays for detecting a method that requires alkaline-pretreated conditions.
Additionally, as evidenced by the art references only monoclonal antibodies against polypeptides VP1 and VP2 were used for immunoassays, not polyclonal antibody.
35 U.S.C. 103 obviousness rejection
Applicant argues pages 9-13 that (1) the amended claims recite a novel three-step sequential process not taught or suggested by the prior art, (2) the references fail to teach or suggest the critical neutralization step, (3) Yuan’s methodology cannot inform sandwich immunoassay development due to fundamental technical incompatibility, (4) the references address fundamentally different problems with incompatible technical objectives, (5) the claimed invention achieves unexpected dual benefits, and (6) the rejection improperly relies on hindsight reconstruction.
The arguments are not found persuasive for the following reasons. First, claim 21 is maintained as it has not been amended to recite the three-step sequential process.
With respect to claim 1 and its dependent claims, the arguments are not found persuasive. With respect to arguments (1) and (2), Kumagai recognizes that samples were treated with an acid or a denaturing agent to increase the reactivity of the antigen and measurement results were performed at physiological pH (i.e., about 7.0). Therefore, it would have been obvious to pretreated a sample and neutralizes the sample before or during detection for measurements. With respect to arguments (3)-(4) and (6), even though Yuan teaches a different assay for detecting VP1 and VP2, the obviousness rejection is not employing the assay of Yuan but rather recognizes that Yuan uses a wide range of pH (acidic and basic) conditions to release VP1 and VP2 for detection. Meanwhile, Kumagai recognizes sandwich assay for detecting VP1 and VP2 with a pretreatment condition such as acid solution. If both acid and basic solution are able to release VP1 and VP2 for detection, then it would have been obvious to try to release VP1 and VP2 via basic solution. Therefore, it is not hindsight because Kumagai recognizes a pretreatment condition that involves acid for detecting VP1 and VP2 and Yuan teaches that both acidic and basic solutions release VP1 and VP2 for immunoassay detection.
With respect to the arguments of (5) that the claimed invention achieves unexpected dual benefits, the arguments are not found persuasive because, as stated above, it would have been obvious to have used alkaline-treated solution for sandwich assay detection. However, the claims do not require the dual benefits as stated by the arguments. Meanwhile, Applicant has not provided evidence that commensurate in scope with the claimed subject matter. For example, the dual benefits would require a specific alkaline pretreatment reagent (see Tables 1-2) and a specific Parvovirus target (Tables 1-2). The only alkaline-treated solution that performed the dual benefits is NaOH. To show unexpected results, the evidence must be (1) commensurate in scope with the claimed subject matter, In re Clemens, 622 F.2d 1019, 1035, 206 USPQ 289, 296 (CCPA 1980), (2) show what was expected, to "properly evaluate whether a … property was unexpected", and (3) compare to the closest prior art. Pfizer v. Apotex, 480 F.3d 1348, 1370-71, 82 USPQ2d 1321, 1338 (Fed. Cir. 2007).
Conclusion
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/N.P.N/Examiner, Art Unit 1678
/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678