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 .
Continued Examination Under 37 CFR 1.114
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03-20-2026 has been entered.
Claim Status
The amendment, filed 03/20/2026, has been entered. Claims 39-46, 49-68 are pending and under examination. Claims 1-38, 47, and 48 are cancelled.
Withdrawal of Objections/Rejections
Previous objection and rejection to claim 47 is moot due to claim cancellation.
The amendment has overcome the objection to claim 39, the objection has been withdrawn.
Previous rejections of claims 39-46 and 49-68 under 35 U.S.C. 112(a), “New Matter” is withdrawn in view of applicant’s arguments/remarks entered on 3/20/2026.
Previous rejection of claims 39-46 and 49-68 under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Golz et al. is withdrawn in view of applicant’s arguments/remarks entered on 3/20/2026.
Applicant’s Arguments and Response to Arguments
“VI. New Rejections Under 35 USC 112(a)- Written Description”
Regarding claims 39-46 and 49-68, under 35 USC 112(a), Applicant states that each currently amended independent claim commonly identifies the target and/or immunogen as consisting essentially of SEQ ID NO: 2 . Applicant states that, applicant is in possession of a genus of antibodies having structures representing the functional characteristics of the claimed invention, “wherein the inhibitor has at least 50% inhibition of DPP3 enzymatic activity”. The applicant points to portions of the Specification, where a certain number of antibodies are disclosed and argues that such disclosure demonstrates possession of the genus of the claimed antibodies. However, mere possession of seven clones of antibodies does not constitute possession of the entire genus of antibodies that would satisfy the functional limitations claimed of 50% inhibition of DPP3 enzymatic activity. .
“VII. Double Patenting”
Regarding applicants’ arguments regarding non-statutory double patenting, the arguments were considered in light of the newly amended and/or new claims. With regards to the argument that currently amended claims 39-42 and 55 recite claim elements that are not recited in claims 1-4 of the ‘094 patent. This argument is not persuasive. Applicant did not identify what elements are distinct enough to make the claims sets patentably distinct from each other. Accordingly, the rejection is maintained for reasons of record.
Applicant’s request to hold the double patenting rejections based on the ‘094 patent in abeyance until the claims are in condition for allowance is denied. Only compliance with objections or requirements as to form not necessary for further consideration of the claims may be held in abeyance until allowable subject matter is indicated. The amended claims do not overcome the double patenting rejection for reasons identified in the double patenting rejection below.
“VIII. Dependent Claims”
Applicant presents no separate arguments for the dependent claims, stating that they are also patentable. Accordingly, the rejections for the dependent claims are maintained.
Maintained: Claim Interpretation
The following is a quotation of 35 U.S.C. 112(f):
(f) Element in Claim for a Combination. - An element in a claim for a combination may be
expressed as a means or step for performing a specified function without the recital of
structure, material, or acts in support thereof, and such claim shall be construed to cover the
corresponding structure, material, or acts described in the specification and equivalents
thereof.
The claims in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be
understood by one of ordinary skill in the art. The broadest reasonable interpretation of
a claim element (also commonly referred to as a claim limitation) is limited by the
description in the specification when 35 U.S.C. 112(f) is invoked.
As explained in MPEP § 2181, subsection I, claim limitations that meet the
following three-prong test will be interpreted under 35 U.S.C. 112(f):
(A) the claim limitation uses the term "means" or "step" or a term used as a substitute for "means" that is a generic placeholder (also called a nonce term or a nonstructural term having no specific structural meaning) for performing the claimed
function;
(B) the term "means" or "step" or the generic placeholder is modified by functional language, typically, but not always linked by the transition word "for" (e.g.,
"means for") or another linking word or phrase, such as "configured to" or "so
that"; and
(C) the term "means" or "step" or the generic placeholder is not modified by sufficient structure, material, or acts for performing the claimed function.
Use of the word "means" (or "step") in a claim with functional language creates a
rebuttable presumption that the claim limitation is to be treated in accordance with 35
U.S.C. 112(f). The presumption that the claim limitation is interpreted under 35 U.S.C.
112(f), is rebutted when the claim limitation recites sufficient structure, material, or acts
to entirely perform the recited function.
Absence of the word "means" (or "step") in a claim creates a rebuttable presumption that the claim limitation is not to be treated in accordance with 35 U.S.C. 112(f). The presumption that the claim limitation is not interpreted under 35 U.S.C.
112(f), is rebutted when the claim limitation recites function without reciting sufficient
structure, material or acts to entirely perform the recited function.
Claim limitations in this application that use the word "means" (or "step") are
being interpreted under 35 U.S.C. 112(f) except as otherwise indicated in an Office
action. Conversely, claim limitations in this application that do not use the word "means"
(or "step") are not being interpreted under 35 U.S.C. 112(f) except as otherwise
indicated in an Office action.
Regarding, claim 55:
a means for generating cells expressing an antibody using the protein DPP3 peptide is an antigen and consists essentially of SEQ ID NO:2.
a means for recombinantly producing polynucleotides encoding the monoclonal antibody derived from the DNA encoding the antibody in step a),
a means for culturing cells expressing the polynucleotides encoding the monoclonal antibody derived from the DNA encoding the antibody in step a), and
a means for purification of the monoclonal antibody from the supernatant of the cultured cells.
Because these claim limitation(s) are being interpreted under 35 U.S.C. 112(f) they are
being interpreted to cover the corresponding structure described in the specification as
performing the claimed function, and equivalents thereof. However, if applicant does
not intend to have these limitations interpreted under 35 U.S.C. 112(f) applicant may:
(1) amend the claim limitation(s) to avoid it/them being interpreted under 35 U.S.C. 112(f) (e.g., by reciting sufficient structure to perform the claimed function); or (2)
present a sufficient showing that the claim limitation(s) recite(s) sufficient structure to
perform the claimed function so as to avoid it/them being interpreted under 35 U.S.C.
112(f).
Maintained Rejection: 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.
Claims 39-68 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. This is a written description rejection.
As amended instant claims are drawn to methods for treating heart failure, chronic heart failure, acute heart failure, myocardial infarction, infection that is microbial, infection that is viral, sepsis, cardiogenic shock, septic shock, comprising administering to a subject in need thereof an effective amount of an inhibitor of enzymatic activity of DPP3, wherein the inhibitor has at least 50% inhibition of DPP3 enzymatic activity, and wherein said inhibitor is purified from the supernatant of a cultured cell that has been propagated from a production cell, wherein said production cell is obtained by a process comprising:
Claim 39: isolating a recombinant single chain F-Variable domain (scFV) against a DPP3 peptide from a human naive antibody gene libraries HAL 7 /8, wherein said human naive antibody gene libraries have been screened with a panning strategy b) generating monoclonal scFV expressing Escherichia coli (E. coli) strains with the eluted phages from one or more rounds of panning, c) selecting the inhibitor from the supernatant from the cultivation of the E. coli strains obtained in b), wherein the inhibitor is a recombinant monoclonal scFV antibody, d) determining an amount of inhibition of DPP3 enzymatic activity by the inhibitor, and e) selecting a production cell that expresses the monoclonal scFV antibody that binds to DPP3 and has at least 50% inhibition of DPP3 enzymatic activity; and
Claim 40: a) isolating of recombinant single chain F-Variable domain (scFV) against a DPP3 peptide from a human naive antibody gene library wherein said human naive antibody gene library was screened with a panning strategy, generating monoclonal scFV expressing bacterial strains with the eluted phages from one or more rounds of panning, c) selecting said inhibitor from the supernatant from the cultivation of the bacterial strains obtained in step b), wherein the inhibitor is a recombinant monoclonal scFV antibody, d) determining an amount of inhibition of DPP3 enzymatic activity by the inhibitor, and e) selecting a production cell that expresses the monoclonal scFV antibody that binds to DPP3 and has at least 50% inhibition of DPP3 enzymatic activity; and
Claim 41: similarly added limitation regarding “…wherein said DPP3 inhibitor is provided by purification from the supernatant of a cultured cell that has been propagated from a production cell, wherein said production cell is obtained by a phage display method”; and
Claim 42: a) fusing activated B-cells from a mammal previously immunized with a protein comprising the sequence of DPP3 or a DPP3 peptide, wherein the DPP3 peptide is a fragment of the DPP3 protein thereof, or with a conjugate of said DPP3 peptide and a carrier protein, with cells of a myeloma cell line, wherein the fused cells result in hybridoma cells, b) culturing the hybridoma cells, c) screening said hybridoma cells for antibodies that bind to the DPP3 protein or to the DPP3 peptide, and that have at least 50% inhibition of DPP3 enzymatic activity, d) choosing hybridoma cells expressing antibodies that bind to the DPP3 protein or to the DPP3 peptide, and that have at least 50% inhibition of DPP3 enzymatic activity, e) recombinantly producing polynucleotides encoding monoclonal antibodies derived from the DNA encoding the antibodies in step d), wherein the inhibitor is a recombinant monoclonal antibody, and f) introducing the polynucleotides encoding the monoclonal antibodies into cells that results in said cultured cell.
Claim 55: a means for generating cells expressing an antibody using a DPP3 peptide, wherein the DPP3 peptide is an antigen and consists essentially of SEQ ID NO: 2; a means for recombinantly producing polynucleotides encoding the monoclonal antibody derived from the DNA encoding the antibody in step a); a means for culturing cells expressing the polynucleotides encoding the monoclonal antibody, and a means for purification of the monoclonal antibody from the supernatant of the cultured cells.
The independent claim constitutes a "broad generic claim” based on the lack of guidance regarding the actual structures required (i.e. the antibody inhibitors are claimed only by their functional ability to bind to a small peptide, i.e. DPP3, but are not actually claimed by any required structure per se); The claimed genus has substantial variation because of the numerous alternatives permitted.
However, the specification does not provide adequate written description to identify the broad genus of the claims because, inter alia, the specification does not disclose a correlation between the necessary structure of the antibody inhibitor, and the claimed function to be maintained (i.e. at least 50-60% inhibition of DPP3 enzymatic activity; minimum binding affinities); and thus, the specification does not distinguish the claimed genus from others, except by function. Although the term “antibody” does impart some structure, the structure that is common to antibodies is generally unrelated to its antigen-binding function; therefore, correlation is less likely for antibodies than for other molecules. Accordingly, the specification does not define any structural features commonly possessed by members of the genus because, while the description of an ability of a claimed antibody inhibitor may generically describe that molecule's function, it does not describe the molecule itself. A definition by function does not suffice to define the genus because it is only an indication of what the antibody inhibitor does, rather than what it is; therefore, it is only a definition of a useful result rather than a definition of what achieves that result. In addition, because the genus of antibody inhibitors, is highly variable (i.e. each different protein capable of binding to a particular structure would necessarily have a unique sequence; see MPEP 2434), the functional characteristic of binding to something specific, even if highly specific, is insufficient to describe the genus. Further, given the highly diverse nature of antibodies, particularly in the CDRs, even one of skill in the art cannot envision the structure of an antibody inhibitor by only knowing its binding characteristics. Thus, the specification does not provide substantive evidence for possession of this large and variable genus, encompassing a potentially massive number of antibody inhibitors claimed only by a functional characteristic. Accordingly, the specification cannot adequately describe uses (e.g. therapeutic methods) of such antibody inhibitors.
Further, MPEP §2163 states that if a biomolecule is described only by a functional characteristic (as in the instant case), without any disclosed correlation between function and structure of the sequence (as in the instant case), it is not sufficient for written description purposes, even when accompanied by a method of obtaining the claimed sequences. MPEP §2163 does state that for a generic claim the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. If the genus has a substantial variance (as in the instant case), the disclosure must describe a sufficient variety of species to reflect the variation within that genus. Although the MPEP does not define what constitutes a sufficient number of representative species, the courts have indicated what does not constitute a representative number to adequately describe a broad genus. The courts determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus (e.g. see In re Gostelli, 872, F.2d at 1012, 10 USPQ2d at 1618).
Furthermore, the disclosure of only one or two species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure "indicates that the patentee has invented species sufficient to constitute the gen[us]; emphasis added. "See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) "[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated."). "A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when ... the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).
Accordingly, the specification also does not provide adequate written description to identify the broad genus of the claims for methods of using antibody inhibitors, claimed only by functional characteristics and not structures per se, because inter alia, it does not describe a sufficient number and/or a sufficient variety of representative species to reflect the breadth and variation within the claimed genus. The specification describes the generation of antibodies and determination of DPP3 binding ability including stating that several murine antibodies were produced and screened by their ability of binding human DPP3 in a sandwich or activity assay and that antibodies raised against GST-tagged human DPP3 or DPP3-peptides were produced via standard antibody production methods (see Example 3; and Table 3). Ultimately, however, it appears that the instant specification only adequately described one antibody having both the claimed structural and functional features (see mAb-pep1-DPP3 in Table 3 with consistently at least 50% inhibition).
Therefore, the specification does not adequately describe cultured cells, in general or for E. coli specifically, that have been propagated from production cells using eluted phages from one or more rounds of panning, and/or wherein the inhibitor so produced is a recombinant monoclonal scFv antibody having at least 50% (or at least 60%) inhibition of DPP3 enzymatic activity and binding minimum affinities of 10-7 M. The specification does not adequately describe hybridoma cells and/or recombinant production of polynucleotides back-translated from “antibodies derived from antibodies” produced in such a manner. The specification does not adequately describe what constitutes “antibodies derived from the DNA encoding the antibody”. The specification does not adequately describe humanizing the antibodies expressed by the hybridoma cells by transferring one or more of the CDRs to a human immunoglobulin (e.g. does not adequately describe the CDRs to be transferred), and/or wherein the antibodies expressed by the selected hybridoma cells provide the CDRs and act as a donor and the human immunoglobulin provides framework regions and acts as an acceptor. The specification does not adequately describe the processes for providing the antibody inhibitors having the claimed functional properties.
Consequently, based on the lack of information within the specification, there is evidence that a representative number and a representative variety of the numerous therapeutic methods comprising the use of antibody inhibitors had not yet been identified and thus the specification represents little more than a wish for possession; See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406 (written description requirement not satisfied by merely providing "a result that one might achieve if one made that invention"); In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming a rejection for lack of written description because the specification does "little more than outline goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate"). Therefore, one of skill in the art would not conclude that Applicant was in possession of the broad and highly variable genus.
With regards to the state of the art, the use of antibody inhibitors for therapeutic methods remain under development, thus necessarily unpredictable. For example, Sela-Culang et al. 2013 (The structural basis of antibody-antigen recognition; Frontiers in Immunology 4(302):1-13) teach the hypervariable loops within the variable domains of antibody polypeptides are widely assumed to be responsible for antigen recognition while the constant domains are believed to mediate effector activation, but that recent analysis indicates that their clear functional separation between the two regions is an over-simplification (see abstract). Sela-Culang et al. teach some residues within the CDRs may not participate in antigen binding and some residues outside the CDRs (e.g. in framework regions and in the constant domains) often contribute critically to the integration with the antigen (see abstract). Sela-Culang et al. teach understanding the role of each structural element is essential for successful engineering of binding polypeptides (e.g. page 2, left column). Sela-Culang et al. teach almost all of the residues predicted to be part of an epitope may be considered as correct predictors as they will bind to some antibodies but also are false predictors as they don’t bind to the others and accordingly that predicting that a residue is not in an epitope may be either a true negative or a false negative depending on the anybody considered (page 2, right column). Sela-Culang et al. teach each CDR has its own unique amino-acid composition different from the composition of the other CDRs and that each CDR has a unique set of contact preferences favoring certain amino acids over others (page 5-6, bridging). Sela-Culang et al. teach the combined action of all six CDRs is the evolutionary response of the immune system that enables the antibody polypeptide to recognize virtually any surface patch on the antigen (page 6). As example, with regards to antibodies directed to DPP3 peptide SEQ ID NO:2 of the instant application, Golz teaches antibodies directed to a SEQ ID NO:2 (see Figure 2) which includes the epitope sequence of the instant application. Assuming arguendo, antibodies produced according to Golz et al. would result in antibodies that will naturally inhibit DPP3 with the same functional properties claimed in the instant application. However, the peptide sequence of Golz et al., does not predict for an entire genus of antibodies directed to the specified epitope of the instant application—as the protein sequence itself and/or the predicted nucleotide sequence do not forecast antibodies directed to the epitope of the instant application.
Accordingly, the state of the art illustrates that antibody design and development requires antigen characterization (i.e. frequency of epitope mutation, glycosylation and/or other modifications that can modify antibody binding) along with additional antibody engineering factors, as summarized by Sela-Culang et al. to minimize off-target effects with therapeutic antibody development. Thus, the state of the art supports that the skilled artisan requires guidance on the critical structures of the antibody per se and thereby does not provide adequate written description support for which structural features of the antibody would predictably retain its functional activity.
Maintained Rejection: Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 39-46 and 50-68 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4 of U.S. Patent No. 11,726,094 B2, “Methods For Determining DPP3 and Therapeutic Methods”. Although the claims at issue are not identical, they are not patentably distinct from each other because they are both drawn to substantially the same methods for treating the same patient populations using substantially the same structural elements.
For example, instant claims are drawn to methods for treating a disease or condition in a subject selected from the group consisting of heart failure, chronic heart failure, acute heart failure, myocardial infarction, infection that is microbial, infection that is viral, sepsis, septic shock, and cardiogenic shock comprising administering to a subject in need thereof an effective amount of an inhibitor, wherein said inhibitor is provided by a process comprising one or more steps to make the inhibitor (i.e. the inhibitor to administer is claimed as a product-by-process; see MPEP 2113).
Similarly, patented claims are drawn to methods for treating a disease or condition in a subject accompanied by or related to necrotic processes, wherein said disease is selected from the group consisting of heart failure, chronic heart failure, acute heart failure, myocardial infarction, infection that is microbial, infection that is viral, and sepsis, comprising administering to a subject in need thereof an effective amount of an inhibitor, wherein said inhibitor is provided by a process comprising: immunizing a mammal with peptides comprising SEQ ID No. 2, infecting or fusing a human B cell with a myeloma or hybridoma cell to produce a trioma cell, testing the immunoglobulins produced by the trioma cell for binding to DPP3, and selecting the immunoglobulins which bind to DPP3.
With regards to all functional properties recited in either claim set; it is noted that these limitations do not add structural components to the inhibitor per se and therefore have been interpreted as functional properties thereof; see MPEP 2112.01. Accordingly, the antibody binding to Seq ID No.2 of US Patent 11,726,094B2 will naturally inhibit DPP3 by at least 50% and/or 60%.
With regards to all of the process steps for providing the inhibitor in instant claims 39-46 and 49-68; it is noted that product-by-process claim limitations are not limited to the manipulation of the recited steps, but only the structure implied by those steps. MPEP 2113 states that “[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process”; see In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). By extension, the use of the product (i.e. an antibody against DPP3), is not limited by how the antibody was generated, absent convincing evidence to the contrary for structure implied by the process steps per se.
Therefore, because the already patented claims teach the only positively recited step required by each of the instantly claimed therapeutic methods (i.e. administer an antibody inhibitor to a subject in need thereof); the instant and patented claims are not patentably distinct.
Conclusion
No claims are allowed.
Correspondence Information Any inquiry concerning this communication or earlier communications from the examiner should be directed to ENUSHA KARUNASENA whose telephone number is (571)272-3972. The examiner can normally be reached Monday-Friday 7:30am-5pm.
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/ENUSHA KARUNASENA/Examiner, Art Unit 1653
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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