DETAILED ACTION Examiner acknowledges receipt of the reply filed 9/11/2025, in response to the restriction requirement mailed 7/17/2025. Claims 1-25 are pending . Claims 10-25 are withdrawn from further consideration for the reasons set forth herein. Claims 1 - 9 are being examined on the merits in this office 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. Election/Restrictions Applicant’s election of Group I (claims 1-9) without traverse in the reply filed on 9/11/2025 is acknowledged. Claims 10-25 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 9/11/2025. Applicant’s election of the following species without traverse in the reply filed on 9/11/2025 is acknowledged. zinc finger protein domain - SEQ ID NOs:89, 143, 253, 145, 259, and 176 (F1-F6) transcription repressor domain - KRAB domain SEQ ID NO :2 DNA-binding recognition helix sequence ( SEQ ID NOs:89, 143, 253, 145, 259, and 176 (F1-F6) fusion protein - SEQ ID NO :292 Claims 1-9 read on the elected species. Drawings The drawings are objected to for the following reasons. The figure legend of Fig 1 refers to SEQ ID NO:308. SEQ ID NO:308 is the wrong sequence and does not correlate with the nucleotide sequence of Fig 1. It is further noted that Fig 1 has 2 separate nucleotide sequences. The figure legends of at least Figs 2, 5, 8, 9, 10-12 refer to color- blue, red, orange, etc. The figure legend of Fig 5B refers to SEQ ID NOs:309-311. These appear to be the wrong SEQ ID NOs. For instance, Fig 5B mouse sequence begin s with GTCTC. However, SEQ ID NO:309, per the Sequence listing begins with tctcc . 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. The figure legends of at least Figs 2, 5, 8, 9, 10-12 refer to color- blue, red, orange, etc. Color photographs and color drawings are not accepted in utility applications unless a petition filed under 37 CFR 1.84(a)(2) is granted. Any such petition must be accompanied by the appropriate fee set forth in 37 CFR 1.17(h), one set of color drawings or color photographs, as appropriate, if submitted via the USPTO patent electronic filing system or three sets of color drawings or color photographs, as appropriate, if not submitted via the via USPTO patent electronic filing system, and, unless already present, an amendment to include the following language as the first paragraph of the brief description of the drawings section of the specification: The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. Color photographs will be accepted if the conditions for accepting color drawings and black and white photographs have been satisfied. See 37 CFR 1.84(b)(2). Specification Please note, the specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification. MPEP § 608.01. Claim Objections Claim s 5 and 7-9 are objected to because of the following informalities: Regarding claim 5, the full name of the acronyms KRAB and KOX1 should be written out in the first order of appearance in the claims. Claims 7-9 should be amended to delete reference to Figures, and to list the substituents therein (see MPEP 2173.05(s)). Appropriate correction is required. Sequence Interpretation/Claim Interpretation The Office interprets claims comprising SEQ ID NOs: in the following manner: “comprising an amino acid sequence of SEQ ID NO: 1” requires only a dipeptide or more within SEQ ID NO: 1, “comprising the amino acid sequence of SEQ ID NO: 1” requires the full-length sequence with 100% identity to SEQ ID NO: 1 with or without additional amino acids at any N-/C-terminal ends or additional nucleotides at 5' /3' ends, “consisting of an amino acid sequence of SEQ ID NO: 1” would encompass any sequence of two or more consecutive amino acids (dipeptide or more) fully contained within SEQ ID NO: 1, and “consisting of the amino acid sequence of SEQ ID NO: 1” would be limited to the sequence of the amino acids as specified by SEQ ID NO: 1, and nothing more or less; " an amino acid selected from the group consisting of SEQ ID NOs: 1, 2 and 3” is any sequence of two or more consecutive amino acids (dipeptide or more) fully contained within SEQ ID NO: 1, 2 or 3; and “ the amino acid selected from the group consisting of SEQ ID NOs: 1, 2, and 3” requires the full-length sequence with 100% identity to SEQ ID NOs: 1, 2, or 3 and the same length as SEQ ID NOs: 1, 2, or 3. Please note that instant claim 9 recites “ an amino acid sequence”. Claim Rejections - 35 USC § 112 The following is a quotation of the first paragraph of 35 U.S.C. 112(a): (a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention. The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112: The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention. Claims 1-9 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. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient” (MPEP § 2163). A claimed genus may be satisfied through sufficient description of a representative number of species or disclosure of relevant, identifying characteristics such as functional characteristics coupled with a known or disclosed correlation between function and structure (MPEP § 2163(3)a(II)). The number of species that describe the genus must be adequate to describe the entire genus; if there is substantial variability, a large number of species must be described. The analysis for adequate written description considers (a) actual reduction to practice, (b) disclosure of drawings or structural chemical formulas, (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure, and (d) representative number of samples. In the instant case, the claims are drawn to a fusion protein comprising a zinc finger protein (ZFP) domain and a transcription repressor domain, wherein the ZFP domain binds to a target region of a human microtubule-associated protein tau ( MAPT ) gene. Claim 2 recites wherein the target region is within 1.5kb (1000 nucleotides) of a transcription start site (TSS) in the MAPT gene. Claim 3 recites that the target region is within 1000 bps upstream and are within 500 bps of the TSS. Claim 4 recites wherein the fusion protein represses MAPT gene expression by at least about 40%, 75%, 90%, 95%, or 99% with no or minimal detectable off-target binding or activity. Claim 5 recites wherein the transcription repressor domain comprises a KRAB domain, optionally from a human KOX1 protein. Claim 6 recites wherein the DNA-binding domain is linked to the transcription repressor through a peptide linker. Claims 7-9 recite ZFP domains comprise a DNA-binding recognition helix sequence from Figs 14-17. Claim 9 further recites alternative claim language that the fusion protein comprises between 4-6 zinc fingers, or the recited SEQ ID NO. The issue at question is whether a person of ordinary skilled in the art would be able to determine what structural feature/amino acid sequence is required for the instant claimed fusion protein to have the functional characteristics of binding to a target region of MAPT gene and repressing gene expression . (a) actual reduction to practice and (b) disclosure of drawings or structural chemical formulas : The court explained that “reading a claim in light of the specification, to thereby interpret limitations explicitly recited in the claim, is a quite different thing from ‘reading limitations of the specification into a claim,’ to thereby narrow the scope of the claim by implicitly adding disclosed limitations which have no express basis in the claim.” The court found that applicant was advocating the latter, i.e., the impermissible importation of subject matter from the specification into the claim.). See also In re Morris , 127 F.3d 1048, 1054-55, 44 USPQ2d 1023, 1027-28 (Fed. Cir. 1997). The claims recite the ZFP domain binds to a target region in a human microtubule-associated protein tau ( MAPT ) gene at a high level of generality. The specification discloses the ZFP may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, or more zinc fingers (e.g. paras. [0009], [0040], [0046]-[0051]). The specification discloses that a ZFP comprising 1 zinc finger typically recognizes 3-4 nucleotides (para. [0047]). A ZFP comprising 2 zinc fingers typically recognizes 6-8 nucleotides. A ZFP comprising 3 zinc fingers typically recognizes 9-12 nucleotides. A ZFP comprising 4 zinc fingers typically recognizes 12-15 nucleotides. A ZFP comprising 5 zinc fingers typically recognizes 15-18 nucleotides. A ZFP comprising 6 zinc fingers typically recognizes 18-21 nucleotides. Id . The specification discloses that each zinc finger contains a DNA-binding recognition helix comprising 7 amino acids that determine DNA binding specificity (para. [0046]). Thus, 7 amino acid positions with 20 naturally occurring amino acids combinations equates to 20^7 or 1.3x10^9 structurally undisclosed zinc finger motifs that are to determine DNA binding specificity for one zinc finger protein (ZFP) domain. The following structurally undisclosed combinations are possible for the indicated number of zinc finger protein domains: 2 ZFP domains: (1.3x10^9)^2 = 1x10^18 4 ZFP domains: (1.3x10^9)^4 = 1x10^36 6 ZFP domains: (1.3x10^9)^6 = 1x10^54 8 ZFP domains: (1.3x10^9)^8 = 1x10^72 10 ZFP domains: (1.3x10^9)^10 = 1x10^90 12 ZFP domains: (1.3x10^9)^12 = 1x10^108 13 ZFP domains: (1.3x10^9)^13 = 1x10^117 Thus, for a polypeptide comprising 13 zinc finger protein domains there are 1x10^117 peptide sequence combinations with each zinc finger having 7 amino acids. The number of actual polypeptide sequences encompassed by the instant claim scope further increases when one considers inclusion of natural and nonnatural amino acids. When one considers, the inclusion of peptide linkers and various transcription repressor domains- each with variable sequences, the number of fusion protein sequences that fall within the instant claim scope are infinite . It is noted that the claim term “target region” is not defined in the specification. Thus, the “target region” of a MAPT gene that is bound by the ZFP domain is highly variable. As noted above, 1 zinc finger can recognizes of to 4 nucleotides, with 4 naturally occurring nucleotide combinations equates to: 4^4 = 256 structurally undisclosed 4 nucleotide MAPT target sequences. See above for the corresponding ZFP domains and correlating number of nucleotides that can be recognized. The following indicates possible combinations: 2 ZFP- 4^8 = 1.6x10^7 structurally undisclosed 8 nucleotide MAPT target sequences. 3 ZFP: 4^12 = 1.6x10^7 structurally undisclosed 12 nucleotide MAPT target sequences 4 ZFP: 4^15 = 1x10^9 structurally undisclosed 15 nucleotide MAPT target sequences 5 ZFP: 4^18 = 7x10^10 structurally undisclosed 18 nucleotide MAPT target sequences. 6 ZFP: 4^21 = 4x10^12 structurally undisclosed 21 nucleotide MAPT target sequences. The size of the human genome is about 3.1x10^9 base pairs (en.wikipedia.org/wiki/ Human_genome ; last visited March 18, 2025). 3.1x10^9 /256 = 1.2x10^7 possible off-target sequences for each 4 nucleotide MAPT target sequence that are present elsewhere in the human genome. 3.1x10^9 /6x10^4 = 5x10^4 possible off-target sequences for each 8 nucleotide MAPT target sequence that are present elsewhere in the human genome. 3.1x10^9 /1.6x10^7 = 194 possible off-target sequences for each 12 nucleotide MAPT target sequence that are present elsewhere in the human genome. 3.1x10^9 /1x10^9 = 3 possible off-target sequences for each 15 nucleotide MAPT target sequence that are present elsewhere in the human genome. In the instant case, the instant specification discloses Figure 14 which shows specific ZFPs consisting of a combination of 4-6 specific zinc finger SEQ ID NOs in specific N-terminal to C-terminal order. Figure 15 shows the full-length fusion protein sequences comprising the ZFPs of figure 14. Figure 16 shows specific ZFPs comprising Arg Glu substitutions. Figure 17 shows the full-length fusion protein sequences comprising the ZFPs of figure 16. Taken all these together, other than the specific examples, the instant specification does not describe a general correlation between structure and function for the claimed genus of fusion proteins comprising a zinc finger domain and a transcription repressor domain, wherein the ZFP domain binds to a target region of MAPT gene thereby repressing MAPT gene expression . (c) sufficient relevant identifying characteristics in the way of complete/partial structure or physical and/or chemical properties or functional characteristics when coupled with known or disclosed correlation with structure : As discussed above, in the instant case, based on the disclosure of instant specification, other than the limited examples, a person of ordinary skilled in the art would not be able to determine what structural feature is required for the claimed zinc finger protein domain an d targeting sequence of the MAPT gene, wherein the fusion protein has functional characteristics of binding and repressing expression of the MAPT gene . It is further noted that this is further complicated by the inclusion of transcription repressor domains (of undefined sequence), and peptide linkers (of undefined sequence). There is no requirement as to the amino acid sequence and/or chemical physical properties of the amino acids. The amino acids include natural and non-natural amino acids. Pruett et al ( Molecular Therapy 16(4 ): 707-717 ( 2008) ) is considered relevant art for having taught that although conceptually ZFPs can be made to recognize new target sequences by mixing and matching individual fingers with known recognition sites (syn. modular assembly), this approach has limitations because it does not take into account the potential interactions between fingers in DNA-binding interactions, which are important in determining target sequence affinity and specificity (e.g. pgs 707-708, joining para). One study reporting that ZFNs made by modular-assembly had only a 50% success rate, and they were never able to target a natural site ( pg 708, col. 1). Gupta et al ( Nucleic Acids Research 39(1) : 381-392 ( 2011) ) teaches that many ZFPs display dose-dependent toxicity due to undesired off-target effects (e.g. Abstract). For each ZFP, the number of binding sites within a genome is primarily dictated by the number and quality of the incorporated zinc fingers (e.g. pg 382, col. 1). Gupta et al also taught that the number of functional target sites is also defined by the composition and length of the linker joining the ZFP and nuclease domain, which determines the required spacing between ZFP half-sites for activity (e.g. pg 382, col. 1). Instant claims recite the ZFPs at a high level of generality, including the linker. Handel et al ( Current Gene Therapy 11 : 28-37 ( 2011) ) teaches that a key issue in the successful biotechnological and therapeutic applications of ZFPs is undeniably the specificity of the nucleases, which is closely linked to ZFP activity and ZFP-associated toxicity (e.g. pg 28, col. 2). The prior art has shown that the DNA binding specificity is a major factor governing ZFP activity and that specificity is inversely correlated with ZFP-associated toxicity (syn. off-target effects). ZFP subunits that do not contain a DNA-binding domain with sufficient affinity to the recognition site will either not find the DNA target at all or bind and cleave many similar sequences in the genome and therefore cause toxicity ( pg 29). Determination of the in vivo specificity is quite challenging ( pgs 29-30). While modular assembly strategy is appealing due to its straightforwardness, the price for this simplicity is the relatively low success frequency (below 10%) in terms of generating ZFPs that work in the context of a complex genome , and there is some concern about the specificities of such ZFPs. One reason for the low success rate may be that the zinc fingers in a multi-finger array are not truly modular, as individual zinc fingers in an array show positive and negative cooperativity in DNA binding (e.g. pg 33, col. 2). Irrespective of the platform used to assemble the zinc finger arrays, a burning issue with regard to specificity of ZFPs is the question about the optimal number of zinc finger motifs per ZFP subunit ( e.g . pg 34, col. 1). For modular assembly, an optimal array seems to consist of 3 to 5 zinc finger modules, while a 6- finger ZFP subunit performed worse (e.g. pg 34, col. 1). Also, one should ask ‘what is the optimal affinity of a ZFP subunit?’ Undoubtedly, zinc finger arrays with little affinity will either bind DNA in a non-specific fashion, or not at all . The prior art taught an example whereby the activity of the three-finger ZFP E3 was barely detectable , while the six-finger ZFN E6 was only half as active as the corresponding ZFN E4 and E5 with four and five fingers, respectively (e.g. pg 34, col. 1). High affinity to the target site does not always translate into high specificity . Juarez et al ( Epigenetics 8(2) : 164-176 ( 2013 ) ) teaches that a designer fusion protein comprising a ZFP and a KRAB transcription repressor domain. Juarez et al taught that, while KRAB-containing ZFPs are traditionally described as transcriptional repressors, they found that these proteins can also function as potent transcriptional activators (Abstract), which is opposite of the functional property to be achieved by the instantly claimed invention. Juarez et al taught that the potency of the ZFP was dependent on the cell type , and the genomic microenvironment critically influences the regulatory outcome, be it transcriptional repression or transcriptional activation , of the KRAB-ZFPs (e.g. pg 165, col. 2). Thus, simply appending the enormously vast genus of about 1x10^117 structurally and functionally undisclosed ZFP protein variants to a transcriptional repressor domain, including a KRAB domain, as recited in Claim 5 , is not, in and of itself dispositive to necessarily and predictably yield the functional property of inhibiting expression of the MPAT gene. Furthermore, the present application is attempting to patent what has not yet been invented and the fact that one of skill in the art can test for the effect used to determine the compounds does not necessarily confer sufficient written description. The claimed fusion protein sequence s would entail testing limitless potential fusion proteins, and one of skill in the art could afterwards still be faced with no hits with the desired functionality. In addition, it is well known in the peptide/protein art that even single amino acid changes or differences in the amino acid sequence of a protein can have dramatic effects on the protein’s function. As an example of the unpredictable effects of mutations on protein function, Drumm et al ( Annu. Rev. Pathol . Mech. Dis., 2012, 7, pages 267-282) teach cystic fibrosis is an autosomal recessive disorder caused by mutations in the CFTR (cystic fibrosis transmembrane conductance regulator) gene, for example, page 268, Section “CYSTIC FIBROSIS”. Drumm et al further teach several mutations can cause cystic fibrosis, including two mutations G551D and G551S; and clinical consequences are quite different for these two changes, as the G551D variant has virtually no detectable activity, and consequently a classic, severe phenotype is associated; G551S, however, has reduced but clearly detectable function and is associated with a much milder presentation of CF, for example page 269, left column, the last paragraph. Drumm et al also teach that in the most common cystic fibrosis mutation ΔF508 (the absence of amino acid 508 of the normally 1,480-amino acid protein) gives rise to the cystic fibrosis phenotype, for example, page 268, right column, the 2 nd paragraph. Thus, even the substitution or deletion of a single amino acid can have dramatic and unpredictable effects on the function of the protein. The unpredictability of the effect of amino acid substitution on the function and/or property of peptide/protein is further confirmed and discussed in Yampolsky et al (Genetics, 2005, 170, pages 1459-1472). Yampolsky et al teach even conservative substitution can significantly affect the function of the protein/peptide, for example, page 1465, Table 3. Although the disclosures of Drumm et al and Yampolsky et al are directed to proteins/peptides other than the claimed fusion proteins , they illustrate the inherent unpredictability with respect to the biological activity of a given protein/peptide after even minor changes to the primary amino acid sequence. Therefore, based on the state of art, a person of ordinary skilled in the art would not be able to determine what structural feature is required for the claimed fusion proteins comprising a zinc finger domain and a transcription repressor domain to have the functional ability of targeting a region of a MAPT gene and repressing expression of the MAPT gene . (d) representative number of samples : In the instant case, the genus of instant claimed fusion proteins is limited to sequences disclosed in figures 15 and 17 . Considering the scope of the genus of instant claimed fusion protein sequence s , the instant specification fails to provide sufficient examples to describe the entire genus of fusion proteins comprising a zinc finger protein domain and a transcription repressor domain that bind to a target region of a MAPT gene as claimed. Taken all these together, considering the state of the art and the disclosure in instant specification, it is deemed that the instant specification fails to provide adequate written description for the claimed genus of fusion proteins comprising a zinc finger domain and a transcription repressor domain and having functional ability of targeting MAPT gene and repressing expression of the MAPT gene ; and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention. The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. Claims 4 and 6 - 9 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. Regarding claim 4, the metes and bounds of the term “at least about" are unclear because there are two limitations in this phrase: "at least" and "about". The limitation "about" is broad, but not indefinite. Similarly, the limitation "at least" is broad, but not indefinite. However, "at least about" is indefinite because the metes and bounds of limitation "at least about" can not be determined. “About” encompasses values below 40%, which necessarily fails to meet the "at least" requirement. To overcome this rejection, Examiner suggests amending the claim to recite “ at least about 40%, 75%, …”. Further regarding claim 4, the term “minimal” in the claim is a relative term which renders the claim indefinite. The term “minimal” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. “Minimal” denotes that some off-target binding and/or activity is necessarily present; however, what amount that is considered “minimal”, as opposed to not-minimal, is an arbitrary and subjective determination. Also, the claim is not clear as to what measure, context, or threshold with determine if MAPT is repressed by a given ZFP-TP fusion protein. Claim clarification is required. Claim 6 recites the limitation "the DNA-binding domain". There is insufficient antecedent basis for this limitation in the claim. Claim 6 recites the limitation "the transcription repressor". There is insufficient antecedent basis for this limitation in the claim. To overcome this rejection, the claim should be amended to recite “the transcription repressor domain ”. Claims 7-9 refer to Figures for describing DNA-binding recognition helix sequence s . Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table "is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim. Incorporation by reference is a necessity doctrine, not for applicant’s convenience." Ex parte Fressola , 27 USPQ2d 1608, 1609 (Bd. Pat. App. & Inter. 1993). The DNA-binding recognition helix sequences for claims 7-9 can be accomplished by amino acid sequences with sequence identifiers. Therefore, the claim calling back to Figures is not necessary and must be amended to remove the reference to the figures. Claim 8 recites the limitation " the DNA-binding recognition helix sequences ". There is insufficient antecedent basis for this limitation in the claim. Claim 9 recites the limitation " the DNA-binding recognition helix sequences " twice in the claim. There is insufficient antecedent basis for this limitation in the claim. The metes and bounds of claim 9 are deemed to be indefinite. The claim recites “wherein the ZFP domain of the fusion protein… and/or comprises an amino acid sequence selected from SEQ ID NOs: 89-196, 197-248 and 267-307. SEQ ID NOs: 197-248 (Figure 15) and SEQ ID NOs:267-307 (Figure 17) recite amino acid sequences of full-length fusion proteins that encompass ZFP domains . In contrast, SEQ ID NOs: 89-196 correlate with ZFP domains (see Figures 14 and 16). Thus, there is a lack of correlation between the preamble and the body of the claim which recite s SEQ ID NOs that are ZFP domains and larger/full-length fusion proteins that encompass a ZFP domain within the fusion protein. It is noted that Applicant elected SEQ ID NO:292 as a representative species of full-length fusion protein comprising a ZPF domain and a transcription repressor domain. SEQ ID NO:292 is recited in claim 9 as a ZFP domain which is not accurate for the reasons set forth herein . T o overcome this rejection, Examiner recommends that claim 9 be amended to remove reference to SEQ ID NOs 197-248 and 267-307. The claim should further remove reference to Figures 15 and 17. As note d above, Figs 15 and 17 disclose full- length fusion protein sequences, which are larger sequences that encompass the ZFP domain. 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) 1-9 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Ledeboer et al. (U.S. 2018 / 0153921 - cited in IDS filed 4/22/2024 ). This is the PBPUB of Patent 11504389- cited in the ODP below. Regarding claim 1, Ledeboer et al. teaches genetic modulators comprising a DNA-binding domain that binds to a target site of at least 12 nucleotides in the MAPT gene; and a transcriptional regulatory domain or nuclease domai n. The DNA-binding domain can be a zinc finger protein, and the transcriptional regulator domain can be a repression domain ( e.g , paras. [0018], [0095]-[0097] ; claims 1-3; Examples 1-2, Table 1). Regarding claims 2-3, the target region is within 300 base pairs downstream or within 100 base pairs upstream of a transcription start site (TSS) in the MAPT gene (Fig 1A, Table 1). Regarding claim 4, the fusion protein represses gene expression by about 50%, 75%, 90%, 95% or greater (e.g., paras. [0036]-[0037], Example 3). Regarding claim 5, the transcription repressor domain comprises a KRAB domain, such as KOX (e.g., paras. [0031], [0125], [0185], Example 2). Regarding claim 6, the fusion protein can include a peptide linker between the DNA-binding domain and the transcription repressor (e.g., paras. [0095]-[0098]). Regarding claims 7-9, Table 1 , first row correlates with ZFP ID 52364 of instant Fig 14 [SBS#52364 of Ledeboer et al] and has 4 zinc fingers. The second row correlates with ZFP ID 52389 of instant Fig 14 [SBS#52389 of Ledeboer et al] and has 6 zinc fingers . See also, paras. [0017], Examples 1 and 3. Claim(s) 1-9 is/are rejected under 35 U.S.C. 102(a)(2) as being anticipated by U.S. 2023 / 0270774; earliest effective filing date 12/01/2016 ; hereinafter referred to as “‘774” - cited in IDS filed 4/22/2024). This is the PBPUB of Appl. No. 18/046327 - cited in the ODP below. The applied reference has a common applicant FILLIN "Insert --assignee-- or --applicant-- or --joint inventor--." \d "[ 4 ]" with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed in the reference and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement. Regarding claim 1, ‘ 774 teaches genetic modulators comprising a DNA-binding domain that binds to a target site of at least 12 nucleotides in the MAPT gene; and a transcriptional regulatory domain or nuclease domain (claim 1). The DNA-binding domain can be a zinc finger protein, and the transcriptional regulator domain can be a repression domain (claims 2-3 ; Examples 1-2, Table 1). Regarding claims 2-3, the target region is within 300 base pairs downstream or within 100 base pairs upstream of a transcription start site (TSS) in the MAPT gene (Fig 1A, Table 1). Regarding claim 4, the fusion protein represses gene expression by about 50%, 75%, 90%, 95% or greater (e.g., paras. [0037]-[0038], Example 3). Regarding claim 5, the transcription repressor domain comprises a KRAB domain, such as KOX (e.g., paras. [0032], [0127], [0185], Example 2). Regarding claim 6, the fusion protein can include a peptide linker between the DNA-binding domain and the transcription repressor (e.g., paras. [0095]-[0098]). Regarding claims 7-9, Table 1, first row correlates with ZFP ID 52364 of instant Fig 14 [SBS#52364 of Ledeboer et al] and has 4 zinc fingers. The second row correlates with ZFP ID 52389 of instant Fig 14 [SBS#52389 of Ledeboer et al] and has 6 zinc fingers. See also, paras. [0018], Examples 1 and 3. 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. Claim s 1 - 5 and 7- 9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-31 of U.S. Patent No. 11504389 (hereinafter referred to as “the ‘389 patent”). Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons. Regarding claim 1, claim 1 of the ‘389 protein recites a genetic modulator of a human or mouse microtubule associated protein tau ( MAPT ) gene, the modulator comprising a zinc finger protein (ZFP) DNA-binding domain that binds to a target site of at least 12 nucleotides within the MAPT gene, wherein the ZFP DNA-binding domain comprises four, five or six zinc finger domains, each zinc finger domain comprising a recognition helix region, and wherein the ZFP DNA-binding domain comprises the recognition helix regions ordered as F1 to F4, F1 to F5, or F1 to F6 shown in a single row of the recited table, and a transcription regulatory domain or a nucleus domain [reads on fusion protein]. Claim 2 of the ‘389 patent recites that the transcriptional regulatory domain comprises a repression domain [reads on transcription repressor domain]. Claim 1 of the ‘389 patent discloses a table comprising zinc finger domains: . The first row correlates with ZFP ID 52364 of instant Fig 14. The second row correlates with ZFP ID 52389 of instant Fig 14. See also claim 12 of the ‘389 patent which recites the same nomenclature. Regardi n g claims 2-4, Table 1 of the ‘389 patent discloses the target binding sites/sequences for ZFP numbers 52364 and 52389 [rows 1 and 2 of Table in claim 1 pf the ‘389 patent]. “[The specification] may be used to learn the meaning of terms and interpreting the coverage of a claim ." In re Basell Poliolefine Italia S.P.A., 89 USPQ2d 1030, 1036 (Fed. Cir. 2008). Thus, even though the instant claims recite specificities not explicitly recited by the claims of the reference application, the ‘389 specification indicates the exact same binding specificity and shown in instant Figure 14. M.P.E.P. § 2112.01 recites, “ Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established.” In re Best , 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "Products of identical chemical composition can not have mutually exclusive properties. A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.” See In re Spada , 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Thus, the ‘389 patent teaches fusion proteins of instant claim 1 and their corresponding binding sites in the MAPT gene. Regarding claim 5, claim 29 of the ‘389 patent discloses that the transcriptional regulatory domain comprises a KRAB domain. Regarding claims 7-9, claim 1 of the ‘389 patent discloses a table comprising zinc finger domains: . The first row correlates with ZFP ID 52364 of instant Fig 14. The second row correlates with ZFP ID 52389 of instant Fig 14. See also claim 12 of the ‘389 patent. Regarding claim 9, claim 1 of the ‘389 protein recites that the genetic modulator comprises between 4-6 zinc finger domains. Claim 1 -4 and 7-9 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim s 1-13 and 15-25 of copending Application No. 18046327 (hereinafter referred to as “the ‘327 application”). Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons. The ‘327 application is a child of the ‘389 patent set forth above. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. Regarding claim 1, claim 1 of the ‘327 application recites a genetic modulator of a MAPT gene, the modulator comprising a DNA-binding domain that binds to target site that includes SEQ ID NOs:1 and 2; and a transcriptional regulatory domain or a nucleus domain. Claims 2 and 3 of the ‘327 application recite that the DNA-binding domain is a zinc finger protein, and that the transcriptional regulatory domain comprises a repression domain. Claim 12 recites DNA-binding recognition helix sequences SEQ ID NOs:7-10 (F1-F4, correlates with compound ZFP ID 52364); and SEQ ID NOs:11-16 (F1-F4, correlates with compound ZFP ID 52389). See instant Fig 14 which contains the same sequences, and MAPT gene target sequences. Regarding claims 2 and 3, claim 20 of the ‘327 application recites wherein the target site is within 300 base pairs downstream or within 100 base pairs upstream of a transcription start site (TSS) in the MAPT gene. Regarding claim 4, claim 22 of the ‘327 application recites that MAPT expression is reduced by 20-80% after administration of the genetic modulator. Claim 24 of the ‘327 application recites gene expression is reduced by 40-90%. Regarding claims 7-9, c laim 12 of the ‘327 application recites DNA-binding recognition helix sequences SEQ ID NOs:7-10 (F1-F4, correlates with compound ZFP ID 52364); and SEQ ID NOs:11-16 (F1-F4, correlates with compound ZFP ID 52389). See instant Fig 14 which contains the same sequences, and MAPT gene target sequence. Relevant Art not Relied Upon Instant SEQ ID NO:292 has 84.3% identity with amino acid positions 1-296 of SEQ ID NO:69 of Zhang et al (U.S. 2006 / 0079475). See SCORE. Conclusion No claims are allowed. Claims 1-25 are pending. Claims 10-25 are withdrawn. Claims 1-9 are rejected. 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