DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-9 and 11-13 are pending in the instant application.
Applicant's election with traverse of the invention of group I, drawn to antibodies that bind Mac-1, and the antibody species of 28E07 (VH of SEQ ID NO:109, VL of SEQ ID NO:110, CDRs of SEQ ID NOs: 483-488) in the reply filed on March 11, 2026 is acknowledged. The traversal is on the ground(s) that there is no search burden in simultaneously examining the inventions of groups I and II. This is not found persuasive because the restriction requirement of January 12, 2026 sets forth why the instant claimed inventions lack unity of invention, and search burden is not a consideration in a finding of lack of unity. Applicant is reminded of the possibility of rejoinder as set forth in section 7 of said restriction requirement.
The requirement is still deemed proper and is therefore made FINAL.
Claim 13 is withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on March 11, 2026.
Claims 1-9, 11, and 12 are under examination as they read upon the elected anti-Mac-1 antibody species of 28E07 (VH of SEQ ID NO:109, VL of SEQ ID NO:110). The elected species appears to be free of the prior art and as such the search was extended beyond 28E07. The search of the prior art was stopped upon finding art that read upon the generic claimed invention.
Information Disclosure Statement
The IDS forms received 6/29/2023, 7/30/2025, and 1/28/2026 are acknowledged and the references cited therein have been considered.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency - This application contains sequence disclosures in accordance with the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 CFR 1.821 - 1.825.
The sequence disclosures are located on pages 39-57.
More specifically, the sequence listing received 6/29/2023 contains only 380 sequences. Tables VI, VII, and instant claim 3 clearly indicate that there are at least 560 sequences disclosed in the specification. As can be seen on pages 39-57 the specification discloses a lot of biological sequences accompanied by a SEQ ID number yet such SEQ ID numbers are NOT present in the sequence listing. It should be appreciated that no meaningful search of such biological sequences can occur if said sequences are not present in a searchable electronic form. Appropriate correction is required to properly account for all disclosed sequences.
Required response – Applicant must provide:
A "Sequence Listing" part of the disclosure, as described above in item 1); as well as
An amendment specifically directing entry of the "Sequence Listing" part of the disclosure into the application in accordance with 1.825(b)(2);
A statement that the "Sequence Listing" includes no new matter in accordance with 1.825(b)(5); and
A statement that indicates support for the amendment in the application, as filed, as required by 37 CFR 1.825(b)(4).
If the "Sequence Listing" part of the disclosure is submitted according to item 1) a) or b) above, Applicant must also provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required incorporation-by-reference paragraph, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter;
If the "Sequence Listing" part of the disclosure is submitted according to item 1) b), c), or d) above, Applicant must also provide:
A replacement CRF in accordance with 1.825(b)(6); and
Statement according to item 2) a) or b) above.
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 1-3 and 6 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.
Applicant has broadly claimed antibodies that bind Macrophage-1 antigen (Mac-1), a receptor formed by the association of CD11b and CD18, which is also known in the art as complement receptor 3 (CR3, see particularly paragraphs [0001-0002] of the instant specification). CD11b is also known as integrin alpha M (ITGAM) while CD18 is integrin beta 2 (ITGB2, ibid.). In addition to binding Mac-1, such antibodies are further recited as having the functional properties of “modulating” cytokine secretion (claim 1) including wherein Th2 cytokine secretion is enhanced relative to Th1 cytokine secretion (claim 2). The broadest claims recite not specific or particular structure responsible for giving rise to such functional properties while dependent claims 3 and 6 recite biological sequences at the level of CDRs (claim 3) and full length VH and VL sequences (claim 6). The working examples disclose the recovery of 79 clones from screening murine and human phage display antibody libraries (paragraph [0034]) followed by sequencing (Table I) and testing such antibodies in vitro (paragraphs [0035-0037] and in an in vivo mouse cancer model (paragraphs [0038-0040]). No working examples concerning production of antibody variants, such as via CDR mutagenesis, appear to be disclosed.
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, 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 genus. See MPEP 2163. In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.” The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts 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 for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014). Such cases have indicated 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 provide information as to what an antibody binding that antigen necessarily looks like (i.e. the primary amino acid structure of the antibody). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of an antibody (such as its ability to bind Mac-1) does not provide evidence of possession of the antibody itself. Further, courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “A sufficient description of a genus . . . requires the disclosure of either 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.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69.
It should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al., and Winkler et al., see entire documents). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
Artisans are well aware that knowledge of a given antigen (for instance human Mac-1) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). Further, it should be noted that degenerate binding of the same structural motif by antibodies does not require the existence of sequence homology or identity at any of their CDRs or other chemical similarities at the antigen-binding sites; side chain mobility of epitope residues can confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur (Lescar et al., see entire document, in particular Abstract and Discussion). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen, no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen. Indeed, Kanyavuz et al. teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 × 1014).
As discussed above, applicant screened human and mouse antibody libraries and identified 79 lead clones that bind Mac-1, all of which are markedly district from one another in sequence as can be readily be seen by inspection of Table 1 spanning pages 11-35, most particularly the underlined CDR sequences. Based upon the knowledge in the art such as that of Edwards et al., Goel et al., and Lloyd et al. such a result is hardly surprising as a vast number of distinct antibody sequences can bind the same exact antigen. Given that the number of potential antibody structures (i.e. sequences) which can bind to the same antigen is literally astronomical the 79 disparate clones recovered by applicant as binding Mac-1 do not reasonably appear to be representative of such breadth. As such there is inadequate written description in the specification as filed to support the genus antibodies that are recited simply as having the functional properties of binding Mac-1 and altering cytokine expression.
Other dependent claims do recite specific antibody structures, such as claim 3 which recites CDR sequences by SEQ ID number, and claim 6 which recites VH and VL sequences by SEQ ID number. However, such claims still do not correlate structure with function. With regard to claim 3, even though as discussed above the art generally recognizes that six specific CDRs in combination collectively give rise to the function of antigen binding and the claim does require six fully defined sequences, as presently written the claims allow for random reassortment of CDR sequences isolated from independent clones. While it is often reasonable to allow for mixing and matching of CDRs from a clonal family (i.e. a collection of sequences derived by mutation from a single common ancestor, such as a naïve BCR that undergoes somatic hypermutation as part of an immune response to increase antigen binding affinity, or the mutations introduced to the Joe9 lead antibody clone in AbbVie that were considered to be a single “species” even though a large number of variants were made and tested) as can be readily seen by visual inspection of the sequences isolated from the 79 recovered clones in Table 1 for example no such single ancestry is present. Given that six CDRs are generally accepted as needed for binding, randomly choosing such CDRs from unrelated clones is not expected to yield an antibody that binds anything at all even if all of the starting clones were specific for Mac-1. This is because the epitopes bound, as well as the way the epitopes are bound, are likely to be completely different among the clones even though they all bind the same antigen, and the specification explicitly discloses that the recovered anti-Mac-1 antibodies do not all bind the same epitope (see most particularly paragraph [0037] as well as tables II-IV). The same logic applies to claim 6 in that it allows random reassortment of variable domain sequences among unrelated clones, and such assortment reasonably will pair three heavy chain CDRs with three light chain CDRs isolated form structurally dissimilar antibodies such that no antigen binding is reasonably expected.
Therefore, in view of the breadth of the claims artisans would reasonably conclude that while applicant was in possession of the 79 anti-Mac-1 clones recovered as part of the working examples, applicant was not in possession of the full breadth of Mac-1 binders that “modulate” cytokine expression as presently recited at the time the instant application was filed. Amendment of the claims to minimally require that the anti-Mac-1 antibodies comprise six fully defined CDRs known to collectively be capable of binding IGFBP5 when present as a set of six sequences is one possible approach to obviating the issues discussed above.
Claims 3 and 6 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 claims contain 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.
Applicant has claimed antibodies that bind to Mac-1 and modulate cytokine expression, which such antibodies being require to comprise specific recited CDR sequences (claim 3) or VH and VL sequences (claim 6). Given that the claimed antibodies are required to comprise defined biological sequences, the claimed antibodies cannot reasonably be made via library screening (as applicant did in the working example) or via standard hybridoma technology as neither reasonably allows artisans control over the sequence of the recovered antibody. Thus artisans reasonably would need to use the tools of molecular biology and recombinant antibody production, such as that disclosed by Kipriyanov (see entire document). Notably, such techniques typically require six fully defined CDR sequences as a staring point. While it is true that claim 3 does require six fully defined CDR sequences, the way in which the CDRs are selected is a random assortment of sequences from among the 79 unrelated lead clones recovered by applicant via library screening in the working example.
It is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al., and Winkler et al., see entire documents). Thus, allowing artisans to randomly choose CDR sequences, say CDR-H1 from antibody A while CDR-H2 is from antibody G, etc. is likely to yield antibodies that bind nothing at all as the CDRs come from unrelated clones binding different epitopes of Mac-1 which is significantly more extensive changes than just a single residue as taught by Rudikoff et al. and Winkler et al. Indeed, the specification explicitly discloses that the 79 recovered anti-Mac-1 antibodies do not all bind the same epitope (see most particularly paragraph [0037] as well as tables II-IV) and thus combining parts from things known to bind different things is expected to yield a product that binds nothing at all. Claim 6 is similar in that it allows for random pairing of VH and VL from unrelated clones which since all six CDRs are not known to be from eth same source is reasonably expected to yield an antibody incapable of binding the Mac-1 antigen, let alone alter cytokine release profiles. Note that such claims are distinct from say claim 4 which requires specific combinations of CDRs to be used in combination, and the specification discloses such combinations where originally present in the clones recovered as part of the working example. Additionally, the specification does not appear to disclose any mutagenesis data, such as a working example of combinatorial antibody assembly.
Therefore, in view of the breadth of the claims, the teachings of the art, and the guidance and direction of the instant specification artisans would be unable to make and use the full extent of what has been presently claimed as most of the encompassed species are reasonably expected to not maintain the function of antigen binding and identifying which combinations maintain the recited functional activities requires additional unpredictable basic science trial and error research and experimentation.
Claims 3-8 are rejected on the basis that they contain an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush groupings of claims 3-8 are improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: First, the fact that applicant requires so many unique SEQ ID numbers to fully capture the diversity of structures encompassed by the claims clearly indicates that the instant claimed antibodies lack a “single” structural similarity. Second, the specification discloses that while applicant identified many anti-MAC-1 antibodies, such antibodies differ from one another with regard to the precise structure/epitope bound (such as but not limited to bent versus extended/open conformations and crossreactivity with murine and human Mac-1 antigen) and the functional consequences arising therefrom (such as but not limited to secretion of distinct cytokine profiles and agonist versus antagonist activity) as can be seen by inspection of, for example, paragraphs [0035-0038] and Figure 5.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 102
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.
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.
Claims 1, 2 and 9-11 are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Lu et al. (WO 2019/177669).
Lu et al. disclose antibodies that bind CD11b and increase the release of inflammatory cytokines (see entire document, particularly the title, abstract, claims, and paragraph [0034]). It should be noted that CD11b is also known in the art as integrin alpha M and that when it is present in a complex in conjunction with CD18/integrin beta 2 , a receptor known as Mac-1 (macrophage-1 antigen) or CR3 (complement receptor 3) is formed (see most particularly paragraphs [0002], [0003], and [0030]). Thus anti-CD11b antibodies necessarily bind Mac-1. Such antibodies are disclosed as being present in pharmaceutical compositions that are to be administered to treat cancer (see particularly paragraphs [0007-0013] and the in vivo murine cancer treatment working examples). Therefore the prior art anticipates that which is presently claimed.
No claims are allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Michael Szperka whose telephone number is (571)272-2934. The examiner can normally be reached Monday-Friday 8:30-5:00.
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Michael Szperka
Primary Examiner
Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641
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