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. Claims 2, 6-7, 25-28, 31-33, 57-58, 61-63, 80-81, 84, 88, and 91-92 are pending and under consideration. Information Disclosure Statement The IDSs filed 12/14/2023, 02/20/2024, and 02/20/2025 were fully considered . See attached PTO-892s. However, the listing of references in the specification (pages 84+) is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered. Specification The specification is objected to for the following reasons: The brief description of Figure 7 [00142] appears incorrect. In particular, the description of each panel (A-C) in lines 6-7 are not in line with the graphical representations. Page 75, line 15 recites an amino acid sequence lacking a sequence identifier. Page 76, line 4 also recites an amino acid sequence lacking a sequence identifier . ( See 37 CFR 1.821(c). 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. ) Drawings Similar to items b and c above, Figures 11, 12 , and 13 appear to recite amino acid sequences without respective sequence identifiers. Claim Objections Claims 2, and 57 are objected to for inclusion of parenthetical expressions such as “(from NRC-sdAb021)” since it is not clearly defining the preceding claim terms. Claim 81 is objected to for reciting “where in” which should be rewritten as “wherein”. Claim 92 is objected to for reciting “the use of claim 90” as claim 90 was cancelled. Claim Rejections - 35 USC § 112 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 58, 63, 80-81 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 63 and 81 recite the limitation "the VHH" in claim 2. There is insufficient antecedent basis for this limitation in the claim. Claim 58 is rejected for reciting “(sdAb021/EGFR1)” as this does not appear to be equivalent to SEQ ID NO:34. The submitted sequence listing for SEQ ID NO:34 only states that SEQ ID NO:34 is equivalent to “NRC-sdAb021”. Thus, the terms in parenthesis may be referencing something that is different than SEQ ID NO:34. Claim 80 is rejected for reciting “(sdAb021/EGFR1)” as this does not appear to be equivalent to SEQ ID NO: 63 . The submitted sequence listing for SEQ ID NO: 63 only states that SEQ ID NO: 63 is equivalent to “ EGFR1 used in CAR constructs ”. Thus, the terms in parenthesis may be referencing something that is different than SEQ ID NO: 63 . This also applies to the recitation of “(SdAb027/EGFR7)”, and “(SdAb02 8 /EGFR 10 )” in reference to SEQ ID NO:64 and 65, respectively. Claim Rejections - 35 USC § 102/103 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. 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) 2, 6-7, 25-27, and 84 is/are rejected under 35 U.S.C. 102( a )( 1 ) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Rossotti et al. (Biochem.Jnl., 476(1), January 2019 as further evidenced by ( Editorial Note, Biochem.Jnl, 481 (23), December 2024) . As to claims 2, and 25-27, Rossotti et al. teach (supplementary Table S1 , see reprint below ) isolated single domain antibodies which bind to human epidermal growth factor receptor. Specifically, the claimed single domain antibodies NRC-sdAb021 through NRC-sdAb031033 were identified as anti-EGFR VHHs raised by llama DNA immunization (page 43) . The reference further teaches (page 43) that the V H Hs were humanized by alignment with human IGHV3-30*01 and IGHJ1- 1*01 amino acid sequences. In summary, Rossotti et al. teach (page 44) that t en unique V H Hs falling into three sequence families were identified in the panning against plate-adsorbed EGFRvIII ( NRC-sdAb021 – NRC-sdAb030 ; Supplementary Table S1 below ); all of these V H Hs as well as two others ( NRC-sdAb032 and NRC-sdAb033 ) were identified by panning against streptavidin-captured biotinylated EGFRvIII. The V H Hs had monovalent binding affinities for recombinant human EGFR, ranging from 1 to 40 nM as measured by surface plasmon resonance . Regarding claims 6-7, 28, and 84, w hile the reference does not specifically identify the claimed CDRs or the amino acid sequence s comprising the sdAb s (Claims 6-7), inherently , the amino acid sequences of the exemplified single domain antibodies NRC-sdAb021 – NRC-sdAb030 (and NRC-sdAb032 and NRC-sdAb033 ) comprise any one of SEQ IDs 34-48 or an amino acid sequence that is at least 80% identical to any one of SEQ ID Nos: 34-48. For example, as evidence by the published Editorial Note’s supplementary materials, NRC-sdAb022 is 100% identical to SEQ ID NO:35. Further, nucleic acids encoding the sdABs are inherently taught as the reference teaches that V H H DNA sequences were cloned into the pSJF2H expression vector and monomeric V H Hs tagged C-terminally with c-Myc and 6×His were purified from the periplasm of E. coli TG1 cells by immobilized metal affinity chromatography . There is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference. Schering Corp. v. Geneva Pharm. Inc., 339 F.3d 1373, 1377, 67 USPQ2d 1664, 1668 (Fed. Cir. 2003) . Claim Rejections - 35 USC § 103 Claim (s) 31-33, 57-58, 61-63, 80-81, 88, and 91-92 are also rejected under 35 U.S.C. 103 as being unpatentable over Rossotti et al. (Biochem.Jnl., 476(1), January 2019 as further evidenced by Editorial Note (Biochem.Jnl, 481 (23) December 2024) in combination with the teachings of Muyldermans, S. (Annu. Rev.Biochem 2013 , 82:775–97 ) and Jovcevska et al., BioDrugs, Volume 34, November 2019. Rossotti et al. (& the editorial note) teach as set forth above regarding the claimed single domain antibodies. Additionally, Rossotti et al. teach ( abstract and page 39) that u p-regulation of epidermal growth factor receptor (EGFR) is a hallmark of many solid tumors, and inhibition of EGFR signaling by small molecules and antibodies has clear clinical benefit. (EGFR) is a receptor tyrosine kinase that is overexpressed and constitutively activated in up to 80% of solid cancers. Following the development of small molecule inhibitors, naked antibodies (Abs) against EGFR, exemplified by cetuximab, have shown clinical benefit in treating colorectal and head and neck cancers. However, Rossotti et al. do not specifically teach constructing recombinant polypeptides comprising one or more of the claimed single domain antibodies (Claim 31), or making multivalent antibodies comprising one or more of the claimed single domain antibodies (Claim 31-33, 57-58) or a chimeric antibody receptor (CAR) comprising one of the single domain antibodies (Claims 63, 80-81, 88). They also do not teach treating a cancer in a subject comprising administering multivalent antibodies or engineered cells targeting EGFR (Claims 61-62, 91 -92 ) . Muyldermans teaches (abstract) that the facile identification of antigen-specific VHHs and their beneficial biochemical and economic properties (size, affinity, specificity, stability, production cost) supported by multiple crystal structures have encouraged antibody engineering of these single-domain antibodies for use as a research tool and in biotechnology and medicine. The reference further teaches (2 nd column, page 786) that the strict monomeric behavior of nanobodies (Nb) in combination with its minimal size makes it an ideal building block to develop multidomain constructs . For example, s everal dimeric Nb constructs have been identified such as bivalent, monospecific and biparatopic construct s. Further, bispecific construct s can be generated by formation of a tandem pair of Nbs with each recognizing a different antigen , a process used to tether two independent antigens . Regarding forming recombinant polypeptides , the reference further teaches that the Nb can be cloned to a protein moiety with a natural tendency to dimerize or to multimerize, such as a leucine zipper motif or the pentamerizing motif of verotoxin . Furthermore, the antigen-specific Nb gene has been cloned in frame with the hinge, CH2 and CH3 exons of human, and mouse or pig IgG and subsequently transfected in myeloma cell lines to reconstruct chimeric HCAbs (e.g. a chimeric antibody receptor or CAR). Additionally, Jovcevska et al. teach (page 17, 2 nd column) that nanobodies combine the beneficial properties of small molecules and monoclonal antibodies . Thus, they are an attractive agent for development of novel therapeutic strategies. Their small size makes them useful for targeting antigens residing in tissues that are weakly vascularized and poorly accessible. Nanobodies used in clinical trials are of different formats such as bivalent monospecific, bivalent bispecific, bivalent bispecific albumin-conjugated, trivalent bispecific and bispecific chimeric antigen receptor (CAR) T cell . Notably, (Jovcevska, page 18, 2 nd column) for activating T cells in vitro, the CD3 antigen is targeted . For example, bispecific T-cell engagers ( BiTE ) that are smaller than antibodies (11 nm in length and 55 kDa in size) and are composed of two single-chain variable fragments ( scFv ) with unique antigen specificity connected by a short amino acid linker. What distinguishes BiTE from other scFv is that one receptor usually targets the CD3 subunit of the T-cell receptor, which allows for targeting T cells, while the other receptor targets a specific tumour antigen. In this regard, smaller sized BiTEs can be generated by substituting one or both the scFv with nanobodies. As an alternative, chimeric antigen receptor (CAR) T cells expressing non major histocompatibility complex (MHC) antigen receptors can be used. CAR T cells with nanobodies as the antigen-recognizing agent against MUC1 and EGFR have already been described. One of ordinary skill in the art at the time of filing would consider it prima facie obvious to have modified the teachings of Rossotti et al. (Biochem.Jnl., 476(1), January 2019 ( as further evidenced by Rossotti et al. (Biochem.Jnl, 481 (23) Editorial Note, December 2024) ) to also include recombinant polypeptides, multivalent antibodies, and chimeric antibody receptors. One would have been motivated to do so because Muyldermans teaches (abstract) that the facile identification of antigen-specific VHHs and their beneficial biochemical and economic properties (size, affinity, specificity, stability, production cost) have encouraged antibody engineering of these single-domain antibodies for use as a research tool in biotechnology and medicine. Muyldermans teaches that the strict monomeric behavior of the nanobodies in combination with its minimal size makes it an ideal building block to develop multidomain constructs such as target directed fusion constructs or multivalent antibodies targeting different antigens. These various constructs would also apply to making bispecific nanobodies and CAR T cells for therapeutic purposes. For example, when constructing bispecific nanobodies where the “second antigen binding moiety binds specifically to a cell-surface molecule of a T-cell” (Claim 33) , Jovcevska et al. teach that small bispecific T-cell engagers can be generated using nanobodies where one receptor targets the CD3 subunit of the T-cell receptor , which allows for targeting T cells, while the other receptor targets a specific tumour antigen. Alternatively, Jovcevska et al. teach that chimeric antigen receptor (CAR) T cells expressing non major histocompatibility complex (MHC) antigen receptors can be used. CAR T cells with nanobodies as the antigen-recognizing agent against MUC1 and EGFR have already been described in the literature. Thus, since the target (EGFR) and amino acid structures of the single domain antibodies was known, the construction of well-known constructs such as recombinant polypeptides, CAR T-cells, and multivalent antibodies that incorporate the targeting aspect would have been obvious to one of ordinary skill in the art in view of the teachings of the art. Further, it would have been obvious to treat cancers comprising administering multi-valent antibodies or engineered (CAR) cells that target tumors over- expressing EGFR , as Rossotti et al. teach that u p-regulation of epidermal growth factor receptor (EGFR) is a “ hallmark ” of many solid tumors wherein inhibition of EGFR signaling by small molecules and antibodies has clear clinical benefit. Moreover, Jovcevska et al. taught that CAR T cells with nanobodies as the antigen-recognizing agent against MUC1 and EGFR have already been described. Conclusion No claim is allowed. 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