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 .
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.
Priority
The present application was filed as a proper National Stage (371) entry of PCT Application No. PCT/US21/55071, filed 10/14/2021, which claims benefit under 35 U.S.C. 119(e) to provisional application No. 63/092,483, filed 10/15/2020.
.
Information Disclosure Statement
The information disclosure statement (IDS) filed 04/14/2023 has been considered, initialed and is attached hereto.
Status of the Claims
Claims 1-11, 13 and 16-18 are pending; claims 3-11, 13, 16 and 18 are amended; claims 12, 14, 15 and 19-76 are canceled. Claims 1-11, 13 and 16-18 are examined below.
The Examiner notes the application includes 4 sets of claims, 04/14/2023. Of the claim sets, 2 of the claim sets (10 pages) each appear to be original claims, and 1 set (4 pages) appears to be the amendment of these original claims. The additional claim set (3 pages) appears to be a different version of original claims, inconsistent with the other two original claim sets, and the amended version of those original claim sets. The 4 page amended claims appear to Applicant’s intended claims (consistent with the 10 page original claims, and with the earlier filed National Stage entry), and as such it is this 4 page claim set that is examined presently.
Applicant is reminded that amendments to a claim must be made by rewriting the entire claim with all changes (e.g., additions and deletions), except when the claim is being canceled. Each amendment document that includes a change to an existing claim, cancellation of an existing claim or addition of a new claim, must include a complete listing of all claims ever presented, including the text of all pending and withdrawn claims, in the application. The claim listing, including the text of the claims, in the amendment document will serve to replace all prior versions of the claims, in the application. 37 CFR 1.121.
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.
Claims 1-9, 11, 13 and 16-18 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 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.
Claim 1 (and see further claim 16, which recites a system comprising the antibody of claim 1) recites “a monoclonal antibody, or antigen binding fragment thereof, comprising a variable region comprising:
a) a complementarity-determining region (CDR) comprising at least about 70% sequence identity to one or a combination of: amino acid sequence of SEQ ID NO: 3, SEQ ID NO: 4or SEQ ID NO: 5; or
b) a CDR comprising at least about 70% sequence identity to the amino acid sequence of SEQ ID NO: 8, SEQ ID NO: 9 or SEQ ID NO: 10.”
Regarding the breadth of independent claim 1, the claim merely requires that a variable region include a CDR (singular), and that CDR is not limited to one selected from just those sequences as recited, but rather any sequence having at least 70% identity to any of said sequences.
Although claim 1 fails to limit the antibody to any particular type of functional/binding requirements beyond that it is an antibody/binds an antigen (see “monoclonal antibody” and “antigen-binding fragment thereof”, see however, claim 13 discussed in more detail further below in the rejection), the claims still encompass an extremely large and variable number of possible monoclonal antibodies, or antigen-binding fragments, thereof. The limitation “having at least 70% identity” may appear somewhat limiting, however is actually potentially enormous in scope because it actually encompasses an extremely large and variable number of possible amino acid sequences comprising a (or a number of) deletions, substitutions or additions at any position. Notably, SEQ ID No. 3 has 8 amino acid residues, SEQ ID No. 4 is 7 residues in length, SEQ ID No. 5 is 9 residues in length, SEQ ID No. 8 is 7 residues in length, SEQ ID No. 9 is 3 residues in length and SEQ ID No. 10 is 10 residues in length. The recited language encompasses all of the sequences meeting the structural requirements that are also monoclonal antibodies/ antigen binding fragments thereof.
The recited language is much larger in scope as compared to what Applicant had possession of as supported by Applicant’s originally filed disclosure.
Specifically, Applicant’s originally filed specification supports only that Applicant was in possession of a singular species of monoclonal antibody, namely identified in the originally filed specification as “rabbit monoclonal antibody Clone #30” (anti-PIF antibody), having heavy chain variable region comprising CDR1 that is SEQ ID No. 3, CDR2 that is SEQ ID No. 4, CDR3 that is SEQ ID No.5, and light chain variable region comprising CDR1 that is SEQ ID No. 8, CDR2 that is SEQ ID No. 9 and CDR3 that is SEQ ID No. 10 (see for example, the originally filed specification at pages 77-79, Examples 1 and 2). Applicant’s originally filed specification only supports this one specific example, having the claimed CDRs (having all 6 CDR sequences as recited in the claims) in the order indicated at the examples.
Regarding claim 13, the claim recites that the monoclonal antibody is “a rabbit monoclonal antibody”, and further recites functional limitations, namely “wherein the monoclonal antibody is capable of binding to a preimplantation factor (PIF), or an immunogenic fragment or epitope thereof, and wherein the monoclonal antibody is specific to the PIF comprising the amino acid sequence of SEQ ID NO. 11”. The claims encompass a large possible genus of antibodies (see as discussed previously above), the genus now defined by both the limited structural and now functional limitations. Beyond the specific 6 CDRs indicated in Applicant’s actual reduction, there is no correlation between structure and function such to support that any antibody, having at least one of the claimed CDRs (see as discussed above, claim 1 encompassing antibodies having only one single CDR, or a single CDR having at least 70% identity with those CDRs claimed by sequence) would retain the necessary claimed functional ability.
Even further, regarding the claimed monoclonal antibodies and the additional language recited at claim 13, it appears Applicant’s single disclosed monoclonal species (referred to as Clone #30), shows binding to the full length PIF peptide (SEQ ID NO. 11) see the originally filed specification at page 79 (100% recovery to the full length PIF peptide, about 3.8% recovery to PIF peptide P1-14 and no reactivity to the rest of the peptides studied). As a result, Applicant does not appear to be in possession of a monoclonal antibody as claimed that binds an “immunogenic fragment or epitope thereof” (see also the claim limitations of 13 addressed further below under 35 U.S.C. 112(b)).
The level of skill in the art is high. In particular, the methods for making and/or screening monoclonal antibodies (with desired binding properties) were well known in the art at the time of the invention. However, knowing how to produce/generate monoclonal antibodies (as referenced in the originally filed specification at pages 43-44) does not support or provide evidence that Applicant is in possession of any and all possible species beyond that single disclosed species provided in Applicant’s actual reduction to practice (namely, monoclonal antibody clone # 30, having the 6 identified CDRs).
Amgen Inc. v. Sanofi further notes, pointing to Ariad Pharms., Inc. v. Eli Lilly & Co., 94 USPQ2d 1161 (Fed Cir. 2010):
To show invention, a patentee must convey in its disclosure that it “had possession of the claimed subject matter as of the filing date.” Id. at 1350. Demonstrating possession “requires a precise definition” of the invention. Id. To provide this “precise definition” for a claim to a genus, a patentee must disclose “a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Id.
Amgen at pages 7-8.
In this case, the disclosure of a single species is insufficient to represent the claimed genus of monoclonal antibodies having the recited functional properties. There is substantial variability in the genus. Since there are a substantial variety of compounds possible within the genus, without disclosure of any common partial structure or other sufficient identifying characteristics of the genus (for example, all 6 CDRs, OR the sequence for the heavy and light chain variable regions), the examples do not constitute a representative number of species and do not sufficiently describe the genus claimed.
It is not within the skill of the art to predict any and all substitutions that would result in products that retain the binding properties of a parent antibody. The art recognizes that structure (of a particular antigen to which an antibody/antibody fragment binds) is not necessarily a reliable indicator of function. As a result, knowing that the antibodies bind SEQ ID NO. 11 is not sufficient detail to provide structure specific to the antibodies themselves.
The teachings of Harlow et al. (Antibodies, A Laboratory Manual, Cold Spring Harbor laboratory, 1988, pages 25-26 and 37-59, cited herewith) which describe how the steps of the humoral immune response to an immunogen are dependent on APC, T-cell and B-cell recognition and processing of the immunogen in ways well known in the art to be highly unpredictable and heavily influenced by the particular immunogen and the specifics of the immunization protocol. Harlow et al. teach that even small changes in structure, such as loss of a single hydrogen bond, can profoundly affect antibody-antigen interaction (p. 25, last paragraph to page 26, second paragraph).
The principles laid out in Harlow are further illustrated in the teachings of Edwards et al. ("The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS" J. Mol. Biol. (2003) 334, 103–118, DOI: 10.1016/j.jmb.2003.09.054), which shows the immense combinatorial flexibility and capacity of the human antibody repertoire to generate binding sites to an individual protein antigen, the B-lymphocyte growth factor known as “BLyS” (see entire document). Edwards describes in detail how the breadth of antibody structures against a given immunogen can be influenced by the immunization and/or selection methods (see Discussion Section). Moreover, the teachings of Mach 7,728,114, of record, at Example 1 provide an example of the diversity of immunization protocols.
As yet another example to illustrate the potential scope of the genus of antibodies encompassed by the instant claims, consider the teachings of Meyer et al. (“New Insights in Type I and II CD20 Antibody Mechanisms-Of-Action With a Panel of Novel CD20 Antibodies”, British Journal of Haematology, 2018, 180, 808–820, |https://doi.org/10.1111/bjh.15132). Meyer describes the core binding region of the well-known anti-CD20 antibody rituximab corresponds to amino acid residues 170ANPS173, wherein N171 is the key residue for binding. By contrast, the OBZ and B1 anti-CD20 antibodies share an overlapping epitope with rituximab (170ANPSEKNSP178); however, in contrast to rituximab residues at positions 176–178 contribute the most to binding (see page 809, left col., 2nd full paragraph).
Meyer also described the production and characterization of a panel of new anti-CD20 antibodies which were shown to bind epitopes contained within or nearby the rituximab 170ANPS173 epitope but to bind to different residues than rituximab binds in this region (see page 811, “New CD20 mAbs with overlapping, but distinct epitopes,” see also page 815-16 bridging paragraph).
More particularly, Meyer teaches the newly created anti-CD20 mAbs m1 and m2 were found to bind within but also in the vicinity of the rituximab binding site (m1 and m2) and elsewhere (m2):
“detailed epitope mapping was performed for both mIgG2c-CD20 mAbs m1 and m2, by using PepScan technology. We identified the critical residues of m1 to be 168EPANPSEK175 by using linear (Figure S2A) and circular (Fig 2C, left) peptides with a positional amino acid scan covering the larger extracellular loop. Also, for m2, a signal decrease below the WT binding signal occurred within the 168EPANPSEK175 sequence motif but the binding signal to the linear (Figure S2B) and circular (Fig 2C, right) peptide was rather low. This suggests that the epitope of both mAbs is located on the larger loop in the same region, however their binding characteristics are different. The data suggests that m1 binds a linear epitope, whereas m2 binds to a conformational epitope.” (see ibid). While these antibodies bind within or nearby the rituximab 170ANPS173 epitope they do so with heavy and light chain CDRs non-homologous to those of rituximab.
Thus, even if multiple antibodies bind epitopes within the same small region of a given polypeptide it is not uncommon for said antibodies to bind to different amino acids even within said small region and for said antibodies to have structurally dissimilar CDRs.
As further illustration of the unpredictability in the art, Brown et al. (“Tolerance of single, but not multiple, amino acid replacements in antibody VH CDR 2: a means of minimizing B cell wastage from somatic hypermutation?”, J Immunol. 1996 May;156(9):3285-91), describes how a one amino acid change in the VHCDR2 of a particular antibody was tolerated whereas, the antibody lost binding upon introduction of two amino changes in the same region (at 3290 and Tables 1 and 2).
One cannot visualize or recognize the identities of the members of the genus that exhibit the claimed functional property (binds antigen, specifically antigen as recited at claim 13 for example).
The only disclosed common structural features, common to the members of the genus, which are responsible for conferring the desired function are the claimed 6 CDRs.
Recent court cases have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See AbbVie Deutschland GmbH v. Janssen Biotech. Inc. as well as Amgen v. Sanofi, as discussed above. Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it.
Claim 2 is substantially similar to claim 1 (claim 1 discussed in great detail previously above), and differs from claim 1 in the claim 2 recites that the antibody comprise a CDR from a) and b), however for the same reasons as discussed above, the claimed limitations are much broader in scope than that which Applicant’s disclosure supports as in Applicant’s possession.
Similarly, referring to claims 3 and 4, the claims limit to only 2 CDRs (2 for the heavy chain variable region, claim 3; 2 for the light chain variable region, claim 4), and for the same reasons as discussed above, the claims encompass a genus of antibody much broader in scope than that which Applicant’s disclosure supports as being in Applicant’s possession.
While claims 5 and 6 together would indicate all 6 CDR sequences consistent with those in Applicant’s actual reduction to practice, each of claims 5 and 6 separately (depending from claim 1) only disclose half of the structure responsible for binding/consistent with Applicant’s disclosed species for which they possessed at the time.
Claims 8 and 9 encompass not only heavy and light chain variable regions of SEQ ID Nos. 2 and 7, but see also the claims recite language as discussed previously above, “comprising at least about 70% sequence identity to SEQ ID NO…” (see as discussed above, at least 70% identity encompasses other different sequences having substitutions, deletions and additions). For the same reasons as discussed previously above, these encompass a large and variable genus larger in scope than that which is supported by Applicant’s disclosure.
In summary, without all 6 CDRs or the full sequence for the heavy and light chain variable regions, there is insufficient structure for binding. As discussed in detail above, the prior art recognizes that polypeptides with even a single amino acid difference may have dramatically different biological activity, and further speaks to the unpredictability regarding antigen binding (binding to PIF, for example).
For all of these reasons, the skilled artisan would not reasonably conclude that the inventor(s), at the time the application was filed, had possession of the full scope of the claimed invention.
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 13 and 16-18 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 13 recites “wherein the monoclonal antibody is capable of binding to a preimplantation factor (PIF), or an immunogenic fragment or epitope thereof, and wherein the monoclonal antibody is specific to the PIF comprising the amino acid sequence of SEQ ID NO: 11” , the language “an immunogenic fragment or epitope thereof” and “is specific to PIF comprising… SEQ ID NO. 11” is indefinite claim language because SEQ ID NO. 11 is indicated by Applicant’s originally filed specification as “The full length PIF” (see page 37, “full length PIF is a 15-amino acid peptide having the sequence of MVRIKPGSANKPSDD (SEQ ID NO: 11)”. See further, Applicant’s disclosure at page 37 recites “"Specific to a full length PIF," as used herein, means that the monoclonal antibody, or the antigen-binding fragment thereof, binds specifically to the full length of PIF, but not derivatives of PIF in different length.”. The recited language is indefinite because it is unclear how the antibody can be both capable of binding an immunogenic fragment or epitope of PIF but also be limited to being specific for only the full-length PIF sequence, SEQ ID NO: 11.
Claim 16 recites at step a) “one or a plurality of monoclonal antibodies of claim 1”, the language “one or a plurality” is indefinite claim language because it is unclear whether “one or a plurality” is referring to a plurality of antibodies that are the same antibody species. For example, the claim could mean one single antibody from the species encompassed by the language at claim 1, the single (1) antibody immobilized on a solid support, or the language could mean one species of antibody, as in multiple of the single species (one type of antibody) are immobilized on the solid support, or it could mean (regarding a plurality) a plurality of different species of the many antibodies encompassed by the language recited at claim 1, immobilized on the solid support (plurality meaning a solid support comprising a plurality of different species antibodies encompassed by claim 1 immobilized thereon). Because the claim has multiple conflicting meanings, the boundaries of what is and is not encompassed is unclear, and as such the claim is indefinite.
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 and 11 are rejected under 35 U.S.C. 102(a)(1)/102(a)(2) as being anticipated by Barghorn et al., US PG Pub NO. 2011/0256138A1.
Barghorn et al. anticipates the claim by teaching a monoclonal antibody comprising a variable region comprising a CDR comprising an amino acid sequence of SEQ ID NO: 9 (see Table 1 regarding monoclonal antibody 4D10, CDR-H2 (VIWRGGRIDYNAAFMS, see also underlined SEQ ID NO. 27 at page 26 of Barghorn). The CDR of Barghorn comprises a sequence that is the same (100%) to claimed SEQ ID NO. 9 of the present application). Notably claim 1 of the present application is not limited to a CDR, the CDR “consisting of” one of the claimed sequences (or to a CDR that is one of the claimed sequences); rather the claim merely requires that the antibody have a CDR that includes one of the claimed sequences (or includes a sequence that is at least 70% sequence identity with at least one of the claimed sequences). See MPEP 2111.03 regarding transitional phrases (comprising is considered synonymous with “including” or containing”, is inclusive or open-ended).
Regarding claim 11, see para [0117], Barghorn teach antibody comprising heavy and light chain constant regions.
Claim(s) 1, 11, 16 and 17 are rejected under 35 U.S.C. 102(a)(1)/102(a)(2) as being anticipated by Dugas et al., WO2018/232278A2.
Dugas et al. anticipates the claim see at para [0148], teaching a monoclonal antibody having a light chain CDR2 having a sequence that includes claimed SEQ ID NO. 4 (see SEQ ID NO. 62, page 167 (table), of Dugas, the second CDR of Dugas’s antibody “IINTGGSAYYTNWA”, which contains the claimed CDR sequence SEQ ID NO. 4 (INTGGSA). The antibody of Dugas anticipates the claim because Dugas is teaching a monoclonal antibody comprising a variable region comprising a CDR with a sequence that has 100% identity with the claimed sequence (the prior art has a CDR that has, within their CDR, a sequence that is the same as Applicant’s SEQ ID NO. 4).
Regarding claim 11, Dugas teach the antibodies of their invention comprising constant regions (teaching intact antibodies, e.g., para [0113], [0260]).
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.
Claim(s) 16 and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Barghorn et al. in view of Fuh et al., US PG Pub No. 2012/0322982A1, Oo et al., US PG Pub No. 2017/0097345A1 and Zuk et al., US Patent No. 4,208,479.
Barghorn et al. teach at paras [0235] and [0236] assay systems for detecting amyloid-beta globulomer, including competition immunoassay using unlabeled antibody (see as addressed previously above) and labeled antigen which reads on Applicant’s substrate.
However, Barghorn fails to clearly indicate that the antibody is provided on a solid support.
Fuh et al. is an example in the art performing competitive assay (competitive ELISA), see for example para [0136], teaching immobilized (unlabeled antibody reagent) on a solid support (Maxisorb plate), adding labeled antigen that binds the antibody (which reads on substrate, as claimed by Applicant), Fuh et al. teaching measurement with a spectrophotometer (paras [0135] and [0136]).
Although Fuh et al. doesn’t teach providing the components together as a system, it was already known in the art to provide products together as a system for sample analysis (see for example, Oo et al., for example at the claims, providing a system comprising an assay plate and a detection component, such as a spectrophotometer (claims 12, 16 and 17 of Oo et al., also paras [0006] and [0057], for applications such as diagnostics, screening, research, e.g., detecting presence of analyte para [0058]).
For example, Zuk et al. teach that in performing assays it is a matter of substantial convenience, as well as providing significant enhancement in accuracy to provide the reagents combined in a kit (column 22, lines 20-68).
It would have been prima facie obvious to one having ordinary skill before the effective filing date of the claimed invention to have provided the competitive assay of Barghorn et al. as monoclonal antibody immobilized on an assay plate because competitive ELISA is an art recognized competitive binding format known and available to those of ordinary skill in the art, so it would have been an obvious matter of applying a known technique to a known product. See Barghorn teach methods such as ELISA, further teaching binding format can be competitive assay format, Barghorn differs in that it is silent as to whether the competitive ELISA comprises antibody immobilized on a solid support; however, see Fuh, it was known in the art when performing competitive ELISA to provide unlabeled reagent immobilized on a solid support, using labeled antigen (substrate for the binding reagent) for detection. It would have been predictable to have provided the antibody immobilized on the solid support (and considering this is a competitive binding format alternative to non-competitive ELISA recognized in the art, and because Barghorn already teach assay formats including ELISA (plate based assay formats), one having ordinary skill would also have a reasonable expectation of success, modifying the format to accommodate competitive assay).
Further, it would have been obvious to one of ordinary skill in the art to provide the competitive assay components (antibody, plate, spectrophotometer for reading results) together in the form of a system as in Oo et al. form for convenience and accuracy as taught by Zuk et al., one of ordinary skill having a reasonable expectation of success since the prior art teaches providing components together not only results in convenience but improved accuracy (as such, providing together would not be expected to inhibit or interfere with the intended assay).
Regarding claim 17, see the combination of the cited art in detail above, including spectrophotometer.
Allowable Subject Matter
Claim 10 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening.
Correspondence
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ELLEN J MARCSISIN whose telephone number is (571)272-6001. The examiner can normally be reached M-F 8:00am-4:30pm.
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, Bao-Thuy Nguyen can be reached at 571-272-0824. 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.
/ELLEN J MARCSISIN/ Primary Examiner, Art Unit 1677