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. Applicant’s amendments to the claims dated 4/18/23 are acknowledged. Claims 1-7, 9 and 31-40 are pending. Claims 8 and 10-30 are cancelled. Claims 1, and 31-32 are amended. Claims 34-40 are new. Prosecution on the merits commences for claims 1-7, 9, and 31-40. PRIORITY Th e instant application , filed 4/18/2023, is a DIV ISIONAL of US P atent No. 11 , 649 , 435 , filed 02/28/2018 which is a 371 of PCT/US2016/048638 , filed 08/25/2016 , which claims priority to US Provisional Application No 62/211,295 , filed 08/28/2015 . Thus, the earliest possible priority for the instant application is 08/28/2015. Drawings The original drawings of 4/18/2023 and replacement drawings of 10/16/2023 are objected to because they are not in according with 35 USC 1.84. The drawings of 4/1 8 /202 3 are objected to because they are not in accordance with the requirements of 35 USC 1.84 (I) and (p), which requires all drawings must be legible for reproduction: 35 USC 1.84 (I): Every line, number, and letter must be durable, clean, black (except for color drawings), sufficiently dense and dark, and uniformly thick and well-defined. The weight of all lines and letters must be heavy enough to permit adequate reproduction. 35 USC 1.84 (p)(1) and (3): Reference characters (numerals are preferred), sheet numbers, and view numbers must be plain and legible; and Numbers, letters, and reference characters must measure at least .32 cm. (1/8 inch) in height. FIGs 1,2, 19B-20, 21B and 21C are not legible. Some of the text is too small to be sufficiently reproducible, and is not legible. Applicant should review EACH drawing of record and ensure the text conform to the requirements of 35 USC 1.84 (p)(1) and (3). The replacement drawings of 10/16/23 are objected to because they are not in accordance with the requirements of 35 USC 1.84 (g), which requires minimal top, bottom, right side and left side margins: Each sheet must include a top margin of at least 2.5 cm. (1 inch), a left side margin of at least 2.5 cm. (1 inch), a right side margin of at least 1.5 cm. (5/8 inch), and a bottom margin of at least 1.0 cm. (3/8 inch), thereby leaving a sight no greater than 17.0 cm. by 26.2 cm. on 21.0 cm. by 29.7 cm. (DIN size A4) drawing sheets, and a sight no greater than 17.6 cm. by 24.4 cm. (6 15/16 by 9 5/8 inches) on 21.6 cm. by 27.9 cm. (8 1/2 by 11 inch) drawing sheets. 9. See, at least, FIGs 5a, 5b, 11c, 12c, 13c, 14a, 14b, 15a, 15d, 16a, 16c, 17a, 17c, 17i, 18a, 18e, 19a, 19e, 19i, 23, 24. Applicant should review EACH drawing of record and ensure the margins conform to the requirements of 35 USC 1.84 (g). Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. CLAIMS Independent claims 1 and 32 are directed to a metabolically enhanced T cell (claim 1) or population thereof (claim 32) comprising a chimeric intracellular signaling molecule, wherein the chimeric intracellular signaling molecule comprises, at least, ( i ) an intracellular domain of a co-stimulatory molecule, and (ii) a myristoy l ation signal ; or (iii) a hinge and a transmembrane domain; and wherein the chimeric intracellular signaling molecule substantially lacks an extracellular ligand binding domain. The term "chimeric intracellular signaling molecule" refers to recombinant receptor comprising one or more intracellular domains of one or more co-stimulatory molecules. The chimeric intracellular signaling molecule substantially lacks an extracellular ligand-binding domain, such as an non-antigen binding domain, or substantially lacks an extracellular domain. In some embodiments, the chimeric intracellular signaling molecule comprises additional domains, such as a transmembrane domain, a detectable tag, and a spacer domain. Paragraph [0068] of the published specification. The specification does not define “hinge” A "co-stimulatory molecule" refers to the cognate binding partner on a T cell that specifically b inds with a co-stimulatory ligand, thereby mediating a co-stimulatory response by the T cell, such as, but not limited to, proliferation. Paragraph [0071] of the published specification. As used herein, the term "substantially lacks an extracellular ligand-binding domain" refers to a molecule that is essentially free of a binding domain that specifically binds to a molecule. In one embodiment, the chimeric intracellular signaling molecule lacks any functional ligand binding domain in the extracellular domain, such as lacking an antigen binding domain. In another embodiment, the chimeric intracellular signaling molecule includes an extracellular domain but lacks the capacity to specifically bind to a ligand, such as an antigen. Paragraph [0118] of the published specification. Thus, a “chimeric intracellular signaling molecule” that “lacks an extracellular ligand-binding domain” is a chimeric receptor that comprises a transmembrane domain or a myristolation signal, which anchors the chimeric receptor within the cell membrane ; wherein t he chimeric receptor is able to signal within the cell, but is unable to bind an extracellular ligand, either because the ligand binding domain is mutated or deleted. See also FIGs. 10-12 of the published specification. A non-limiting diagram comparing a “a chimeric intracellular signaling molecule” to a “chimeric intracellular signaling molecule ” that “ substantially lack s an extracellular ligand-binding domain” is provided below: 561975 99060 0 0 The instant specification does not define "metabolically enhanced" T cells. Paragraph [0138] of the published specification discloses expression of the chimeric intracellular molecule metabolically enhances the T cell. Paragraph [01 60 ] of the published specification discloses expression of a Chimeric Antigen receptor metabolically enhances the T cell. Paragraph [022 7 ] of the published specification discloses stimulation of a T cell expressing a chimeric intracellular signaling molecule metabolically enhances the T cell. Thus, for the purposes of prosecution, based on the teachings of the specification, a T cell expressing a chimeric intracellular molecule lacking an extracellular ligand binding domain reads on a metabolically enhanced T cell. Claim Objections Claim s 1, 4, 32, and 33 are objected to because of the following informalities: Claim 1 repeats “ITGA4” in section ( i ). Claim s 1 and 32 recite “CD8alpha” in section ( i ) but recite “CD8-alpha” in section (ii). Applicant should use consistent formatting for the same claim terms throughout the claim set. Claim s 1 and 32 recite “PAG/ Cpb ” in section ( i ) but recite “PAG” in section (ii). Applicant should use consistent formatting for the same claim terms throughout the claim set. Additional examples include formatting differences between claim s 1 and 32. Claim 1 recites, “wherein the intracellular domain is selected from the intracellular domain of a T cell receptor (TCR), a CD3 zeta, a CD3 gamma, a CD3 delta, a CD3 epsilon, a CD86, a common FcRgamma ” whereas C laim 32 recites, “wherein the intracellular domain is selected from the intracellular domain of a T cell receptor (TCR), CD3 zeta, CD3 gamma, CD3 delta, CD3 epsilon, CD86, FcRgamma .” Because it appears that claim 32 is a population of the T cell of claim 1, the structural features shared by the two claims should be recited identically. Applicant is required to review the claims and amend as necessary. Claim 4 is missing a comma after “of claim 1” in line 1. Claim 33 is missing a comma after “of claim 32” in line 1. Appropriate correction is required. Claim Rejections - 35 USC § 112(b) 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 appl icant regards as his invention. Claims 1-7, 9, and 31-40 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. Claims 1 and 32 are indefinite for the use of parentheticals at section (iii) for reciting “CD160 (BY55).” It is unclear whether the limitations recited within the parentheticals are required or optional, or if they represent an acronym for the adjacent term. Claims 2-7, 9, 31 and 33-40 are included in the rejection because they depend from a rejected claim. 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 1-3, 9, 31-32 and 34-35 are rejected under 35 U.S.C. 102 (a)(1) and 102(a)(2) as being anticipated by WO20 0 4/127261 to Wu . 1181100 1966595 0 0 With regard to claims 1 and 32, WU discloses T cells comprising heterodimeric chimeric antigen receptors (CARs), wherein a CAR comprises, at least, a first polypeptide comprising an extracellular ligand-binding domain and a transmembrane domain, and a second polypeptide comprising a hinge/transmembrane domain and an intracellular co-stimulatory domain, and the two polypeptides form a heterodimer via an intracellular heterodimerization domain (paragraphs [00 60 ] -[0062] , [0066] , [0082] , [00206]-[00208], [00216] ). See, FIG. 17 of WU: W u discloses transmembrane/hinge domains can be present on both the first and second polypeptides, and are selected from CD8 (paragraphs [0045], [0074], [0083]-[0084], [0087]-[0093]. The intracellular signaling domains the second peptide are selected from 4-1BB, CD28, ICOS, OX-40, CD27, CD30, GITR, DAP10, CD3 delta, CD3 epsilon, CD3 gamma, CD3 zeta, CD79 (paragraphs [0098]-[0101], [00104]-[00112], [00162]-[0163]). Wu discloses the chimeric receptor transmits signal from the ligand-binding domain of the first polypeptide to the second polypeptide when the chimeric receptor heterodimerizes (paragraph [0060], [0066]-[0075]). Thus, the second polypeptide of the chimeric receptor domain of Wu necessarily comprises 1) the intracellular signaling domains of the co-stimulatory proteins to be selected from the group consisting of 4-1BB, CD28, ICOS, OX-40, CD27, CD30, GITR, DAP10, CD3 delta, CD3 epsilon, CD3 gamma, CD3 zeta, CD79, and 2) substantially lacks an extracellular ligand-binding domain. Thus, WU anticipates claim s 1 and 32 . With regard to claims 2-3, because Wu discloses the chimeric receptor is expressed on a T cell, Wu anticipates the claims. With regard to claim 9, Wu discloses the T-cells comprising the CARs are generated ex vivo and administered to a subject in need as a treatment , as an intravenous injection (paragraph [00215]-[00220], [00226]-[00227],[00267]-[00268] , and [00306]) which reads on a pharmaceutical composition comprising the cells and a pharmaceutically acceptable carrier , absent evidence to the contrary. With regard to claim 31, Wu discloses the T-cells comprising the CARs are generated ex vivo and administered to a subject in need as a treatment, as an intravenous injection (paragraph [00215]-[00220], [00226]-[00227],[00267]-[00268], and [00306]) which reads on a composition comprising the cells, absent evidence to the contrary. With regard to claim 34, Wu discloses the CARs comprise detectable tags (paragraphs [00184]-00190]). With regard to claim 3 5 , Wu discloses the hinge and transmembrane domain are from CD8 alpha (SEQ ID NO: 29, 30 , 56, 143, 144] (paragraphs [0090], [0093]). Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness . This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claim s 4- 6 , 33, and 37 are rejected under 35 U.S.C. 103 as being unpatentable over WO20 0 4/127261 to Wu, as applied to claims 1-3, 9, 31-32 and 34-35 above, further in view of US2013/0315884 to Galetto , of record. Claims 4- 6 , 33 and 37 are directed to embodiments wherein the cells further comprise a bispecific antibody. Wu is applied as in the 102 rejection above, the content of which is incorporated herein in its entirety. Wu discloses T cells comprising heterodimeric chimeric antigen receptors (CARs), wherein a CAR comprises, at least, a first polypeptide comprising an extracellular ligand-binding domain and a transmembrane domain, and a second polypeptide comprising a hinge/transmembrane domain and an intracellular co-stimulatory domain, and the two polypeptides form a heterodimer via an intracellular heterodimerization domain (paragraphs [0060]-[0062], [0066], [0082], [00206]-[00208], [00216]). Wu discloses the ligand—binding domain can be an antigen-binding domain from an antibody, and the antigen binding domain can have a variety of antigen-binding specificities , including cancer cell antigens/epitopes (paragraphs [0077]-[0079]). However, Wu does not disclose that the antigen-binding domain comprises a bispecific antibody as required by claims 4 and 33. Galetto discloses T cells expressing multi-chain chimeric antigen receptors which form dimeric, trimeric and tetrameric CARS, wherein at least one chain does not have an extracellular ligand binding domain , and upon ligand binding, the dimers transmit signal through the chain that does not have an extracellular ligand binding domain ( paragraph s [0127]-[0128], [0136]-[01 46 ]; FIGs 3-4 ). Galetto further discloses a chain of the multi-chain CAR comprises a bispecific antibody , or the cell encodes and expresses a bispecific antibody (paragraphs [0133], [0151], [0162], [0214]) and wherein the bispecific antibodies comprise two distinct antigen binging domains , which function to direct the T cells to target antigens as well as activate the T cells (paragraphs [0162], [0246]). It would have been obvious to combine the T cells expressing multi-chain CARs of Wu, wherein at least one chain comprises an antigen-biding domain from an antibody, further with the disclosure of Galetto . A skilled artisan would have been motivated to include a bispecific antibody in the T cells of Wu because Wu discloses the multi-chain CARs can have a variety of antigen-binding specifi cities, and Galetto teaches bispecific antibodies in T-cells expressing multi-chain antibodies allow for targeting two different antigen binding domains, allowing to redirect and activate the T cells. A skilled artisan would have had a reasonable expectation of success in practicing the claimed invention as including bispecific antibodies in T cells expressing multi-chain CARs was known at the time of the invention. With regard to claims 5-7 and 37, Wu does not disclose the use of bispecific antibodies. However, Galetto discloses the bispecific antibodies comprise two distinct antigen binging domains , and they function to direct the T cells to target antigens as well as activate the T cells (paragraphs [0162], [0246]). Claims 7, 37-38 are rejected under 35 U.S.C. 103 as being unpatentable over WO20 0 4/127261 to Wu and US2013/0315884 to Galetto , of record, as applied to claims 1-6, 9, 31-33, 34-35 and 37 above, and further in view of Müller and Kontermann . Bispecific Antibodies for Cancer Immunotherapy. Biodrugs , 2010. 24(2): 89-98, of record. The disclosures of Wu and Galetto are applied as in the 102 and 103 rejections above, the content of which is incorporated herein in its entirety. Wu and Galetto combine to render obvious T cells comprising a chimeric receptor and a bispecific antibody, as required by claims 1, 4-5, and 32-33. Galetto discloses the bispecific antibodies can be produced in any variety of ways (paragraph [0246]). However, neither Wu nor Galetto disclose wherein the bispecific antibody is a first and second single-chain antibody as required by claim 28; or wherein the bispecific antibody comprises a first whole immunoglobulin and a second whole immunoglobulin comprising IgG, IgA or IgD , as required by claims 37 and 38. Müller and Kontermann disclose bispecific antibodies utilize multiple formats, having evolved over time with technology and clinical requirements (Abstract, page 91, first column). Müller and Kontermann discloses known formats include wherein the bispecific antibodies comprise a first and second single chain variable fragment molecule, or wherein the bispecific antibody comprises an antigen binding domain comprising a first whole immunoglobulins and a second whole IgG molecule (FIG 1; page 90 , 95 ). Müller and Kontermann disclose the use of two ScFV in an antigen binding domain allows two binding sites for a single antigen or a binding site for two distinct antigens, which can result in bivalent, trivalent or more formats in small and compact molecules (page 90, second column last paragraph bridging page 91, first column). Müller and Kontermann disclose use of whole immunoglobulins such as IgG increases the half-life of the bispecific antibodies (page 95, Half-Life Extension Strategies section). It would have been obvious to combination the disclosure s of Wu and Galetto on T cell s expressing multi-chain CARs comprising a bispecific antibody, further with the disclosure of Müller and Kontermann . A skilled artisan would have been motivated to use known bispecific antibody structures known in the art which are known for use in cancer therapies (MPEP2143(I)(A); MPEP2144.07). A skilled artisan would have had a reasonable expectation of success in practicing the claimed invention as multiple formats of bispecific antibodies used in cancer therapies comprising T cells was known in the art at the time of the invention. Claim 36 is rejected under 35 U.S.C. 103 as being unpatentable over WO20 0 4/127261 to Wu and US2013/0315884 to Galetto , of record, as applied to claims 1-6, 9, 31-33, 34-35 and 37 above, and further in view of Sharon et al. Recombinant Polyclonal Antibodies for Cancer Therapy. Journal Cellular Biochemistry, 2005. 96:305-313, of record, and WO2011/057124 to Lum (publication dated May 12, 2011), of record. The disclosures of Wu and Galetto are applied as in the 102 and 103 rejections above, the content of which is incorporated herein in its entirety. Wu and Galetto combine to render obvious T cells comprising a chimeric receptor lacking an extracellular ligand-binding domain and a bispecific antibody, as required by claims 1, 4-5, and 32-33. Galetto discloses the bispecific antibodies can be produced in any variety of ways (paragraph [0246]). However, neither Wu nor Galetto disclose wherein the bispecific antibody is chemically heteroconjugated to a polyclonal antibody specific for a tumor-associated antigen (TAA), and the metabolically enhanced T cell specifically binds the TAA polyclonal antibody , as required by claim 36. Sharon discloses anticancer treatments using monoclonal antibodies (directed to a single target antigen) eventually result in escape variants which render the therapy ineffective (Abstract). Sharon discloses the use of polyclonal antibodies, which target multiple epitopes/antigens on a cancer cell could minimize the generation of escape variants and be more efficient than monoclonal antibodies (Abstract). Sharon discloses the generation of a polyclonal library of a cancer would provide multiple antibodies against different tumor-associated epitopes/antigens which would allow for the polyclonal library to be effective on cancers using lower density tumor-associated antigens, as more polyclonal antibodies are used - compared to a single monoclonal antibody directed to a single tumor antigen (page 308-309; Fig 2). Sharon generates a library of polyclonal antibodies directed to a colorectal cancer cell line, and shows the polyclonal antibody library bound with higher density than a known corresponding anti-colorectal cancer antibody CO17-1A, and was more effective at inhibiting a human colorectal cell line in culture (page 310, second column). Lum discloses generating polyclonal bispecific antibodies, wherein the bispecific antibody is generated from the fusion of a T cell antibody binding portion (first antigen binding portion) to a polyclonal antibody directed to a second target antigen (paragraph [0007], [0042]-[0043], [0061]). Lum discloses the polyclonal antibody directed to the second target antigen is directed to different epitopes on an antigen or to two different antigens (paragraph [0011]). Lum discloses the polyclonal bispecific antibodies are produced by heteroconjugating a polyclonal antibody directed to the second antigen to the T cell antibody binding portion (paragraphs [0031], [0095]-[0100]). Lum discloses the polyclonal antibodies are armed on T cells (paragraph [0014]). Lum discloses the concentration of polyclonal bispecific antibodies needed to arm cells is reduced compared to traditional bispecific antibodies, thus reducing the amount of antibody necessary to achieve a therapeutic effect, and reduce the possibility of an immune response generated against the bispecific antibodies by a patient (paragraph [0023]). It would have been obvious to combine the disclosure s of Wu and Galetto on T cel ls expressi ng multi-chain CARs comprising a bispecific that binds a T cell and a tumor cell, further with the disclosures of Sharon and Lum. A skilled artisan would have been motivated to use polyclonal bispecific antibodies, as Sharon identifies the benefits of using polyclonal antibodies as therapeutics for cancer treatments by providing multiple antibodies which bind lower concentrations of individual tumor associated antigens, but result in more overall binding to cancer cells compared to monoclonal antibodies directed a single tumor antigen, and suggests use of polyclonal antibodies would reduce escape variants. Lum further shows that generating polyclonal bispecific antibodies can localize the bispecific polyclonal antibodies to a target site using a significantly reduced amount of antibody necessary to result in a therapeutic effect. The skilled artisan would have been motivated to generate the polyclonal antibodies by chemically conjugating the polyclonal antibodies targeted to a tumor antigen to a T cell binding segment, as Lum discloses polyclonal bispecific antibodies are made using such methods. MPEP 2143 (I)(A). A skilled artisan would have had a reasonable expectation of success in practicing the claimed invention as the benefits of using polyclonal antibodies in cancer therapies, and the generation of polyclonal bispecific antibodies was known in the art at the time of the invention. Claims 39-40 are rejected under 35 U.S.C. 103 as being unpatentable over WO20 0 4/127261 to Wu and US2013/0315884 to Galetto , of record, as applied to claims 1-6, 9, 31-33, 34-35 and 37 above, and further in view of US Patent No. 6,004,554 to Thorpe, of record . The disclosures of Wu and Galetto are applied as in the 102 and 103 rejections above, the content of which is incorporated herein in its entirety. Wu and Galetto combine to render obvious T cells comprising a chimeric receptor lacking an extracellular ligand-binding domain and a bispecific antibody, as required by claims 1, 4-5, and 32-33. Galetto discloses the bispecific antibodies can be produced in any variety of ways (paragraph [0246]). However, neither Wu nor Galetto disclose wherein the T cell expresses and displays two or more bispecific antibodies, as required by instant claim 39. Thorpe discloses T cells displaying two distinct bispecific antibodies, wherein a first bispecific antibody binds to a first T cell cell-surface marker and a first tumor-associated antigen and a second bispecific antibody that binds to a second cell cell-surface marker and a second tumor-associated antigen, to activate or localize the T cells (column 8, line 1- column 9, line 21; Column 9, lines 50-62, column 10, lines 20-40, column 11 lines 18-65; column 16, lines 7-24; Claims 1-5; claims 20-21). Thorpe discloses that using two different bi-specific antibody increases T cell activation (column 51, lines 24-44). It would have been obvious to combine the disclosure s of Wu and Galetto on T cells expressing multi-chain CARs and expressing b ispecific antibodies, further with the disclosure of Thorpe on T cell s expressing and displaying two different bispecific antibodies. A skilled artisan would have been motivated to use two different bispecific antibodies in order to increase T cell activation of the cells, as taught by Thorpe. A skilled artisan would have had a reasonable expectation of practicing the claimed invention as use of two bispecific antibodies to target and activate T cell s were known in the art at the time of the invention. With regard to claim 40 , Galetto discloses the bispecific antibody binds CD3 (paragraph [0162]). Thorpe discloses the two bispecific antibodies bind CD3 (column 51, lines 24-44). This claim is obvious for the same reasons as stated above for claim 39 . Conclusion No claims are allowed. No claims are free of the prior art. 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