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 with traverse of Group I (i.e., claims 1, 20-22, and 28-31 drawn to a protein) in the reply filed on August 25, 2025 is acknowledged. Additionally, Applicant's election with traverse of Species A (i.e., a protein amino acid sequence of SEQ ID NO: 1 with two substitutions, namely, Y117F and Y217F) in the reply filed on August 25, 2025 is acknowledged. The traversal is on the ground s that (1) no analysis of whether Groups I and II have a special technical feature is needed because Groups I is directed to a protein having channel activity and comprising an amino acid residue different than the amino acid residue present in SEQ ID NO: 1, and Group II is directed to a method of using this protein (See Applicant’s Response received on 8/25/25, pg. 6), (2) both Groups I and II require that the protein has 90% or more identity with SEQ ID NO: 1 with one or more substitutions at a position recited that shifts the wavelength shorter than that of SEQ ID NO:1 thereby rendering the protein useful to improve or recover a photosensitivity for color recognition of a retina, and thus, a lack of unity has not been established (See Applicant’s Response received on 8/25/25, pg. 6-7), and (3) the claimed subject matter and species is sufficiently related that a thorough search for any one Group would encompass a search for the subject matter of the remaining claims and species pursuant to MPEP 803 (See Applicant’s Response received on 8/25/25, pg. 7) . This is not found persuasive . In response to Applicant’s first argument, it is unclear why Applicants contend that a special technical feature analysis is not needed. As acknowledged by Applicant, Group I is directed to a protein and Group II is directed to a method of using the protein of Group I. As such, although both Groups share the protein as the shared technical feature, but the two groups are not identical and encompass different subject matter and examination parameters, e.g., 112(a) considerations. Thus, as acknowledged by Applicants, the shared special technical feature would be the protein of Group I. In response to Applicant’s second argument, it is acknowledged that the amended subject matter of claim 1 now encompasses a smaller genus of amino acid sequences. However, at least 90% identity to SEQ ID NO: 1 encompasses up to 36 amino acid modifications including deletions, insertions, additions, and/or substitutions. Only one of the 36 is required, and this required modification is a substitution at one of the recited substitutions at positions, i.e., 53, 83, 117, 137, 146, 147, 150, 151, 169, 177, 198, 217, 218, 245, and 247 ; and the 36 modifications optionally cannot be located at positions 53, 83, 87, 117, 120, 124, 137, 139, 142, 143, 146, 147, 150, 151, 169, 173, 177, 198, 204, 216-218, 231, 238, 245 and 247. But since the latter claim limitation is optional, it is not limiting in nature. Thus, the only required structure is at least one of the recited substitutions. The remaining 35 amino acid modifications are not limited. A s such, the amended claim scope does not result in a protein amino acid sequence with a sufficient core structure or sequence to represent the claimed genus as a whole. Thus, the Examiner maintains that Groups I and II lack unity of invention a priori given the breadth of sequences encompassed. In response to Applicant’s third argument, it is noted that search burden is not a consideration. More specifically, u ndue search burden is not a criteria for election/ restriction purposes under 35 USC § 372. Please refer MPEP 1850 for details. Therefore, whether a search burden exists is not dispositive as to whether Groups I and II lack unity of invention. The requirement is still deemed proper and is therefore made FINAL. However, in light of the Examiner’s search, Species A is hereby removed. Status of Claims Claims 1-27 were originally filed on September 13, 2022. The amendment received on September 13, 2022, amended claims 2-13, 15-25, and 27. The amendment received on August 25, 2025, canceled claims 2-19 and 26-27; amended claims 1 and 22-24; and added new claims 28-31. Claims 1, 20-25, and 28-31 are currently pending and under consideration as claims 23-25 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. Applicant timely traversed the restriction (election) requirement in the reply filed on August 25, 2025. Priority The present application claims status as a 371 (National Stage) of PCT/JP2021/010440 filed March 15, 2021, and claims priority under 119(a)-(d) to Japanese Application No. 2020-044713 filed on March 13, 2020. Receipt is acknowledged of papers submitted under 35 U.S.C. 119(a)-(d) for Japanese Application No. 2020-044713, which papers have been placed of record in the file. Please note that the Japanese application is in a foreign language and therefore cannot be reviewed. Information Disclosure Statement The information disclosure statements (IDSs) submitted on October 27, 2022; January 4, 2023; January 2, 2024; March 13, 2024; February 21, 2025; April 24, 2025; and November 10, 2025, are being considered by the examiner. Regarding the IDS received on 10/27/22, please note that NPL document 3 has been crossed out and not considered because an English language abstract, translation, and/or statement of relevance as required under 37 CFR 1.98 has not been provided. Regarding the IDS received on 1/4/23, please note that a publication year was not provided for NPL document 1 , and the text, in particular, the text of the figure s in the Results section, is not fully legible as required under 37 CFR 1.98. A search for the publication year resulted in a document indicating that a poster with the same title was publicly available September 2019 (See Lectures and oral presentations – Hidaki Kamitori , available online at https://researcher.nitech.ac.jp/html/96_knkyu_prsn_20_en.html , 2 pages (accessed on 11/27/25) at pg. 2). Given the titles are identical, the Examiner is interpreting that the publication date of NPL1 is September 2019 in order to advance prosecution. Although it appears that one mutant disclosed in NPL1 is Gt_CCR4 V83A (See NPL1, Figure 2B), since the remaining mutants disclosed are not legible, the document has been crossed out as it cannot be fully considered except for disclosing Gt_CCR4 V83A (See 102(a)(1) rejection below) . Clarification is respectfully requested. Sequence Interpretation For claim 1, please note that the Examiner is interpreting the scope as open-ended requiring at least 90% identity to SEQ ID NO: 1 with one or more of the recited substitutions and with any N- and/or C-terminal additions. It is noted that at least 90% identity to SEQ ID NO: 1 encompasses up to 36 amino acid modifications where the modifications include insertions, deletions, and substitutions, but at least one of the 36 must be one of the recited substitutions. Furthermore, it is noted that the protein amino acid sequence optionally can be further modified with up to 35 deletions, substitutions or insertions at a position other than one of the recited positions. However, it is noted that the up to 35 amino acid modifications encompassed by the “at least 90% identity to SEQ ID NO: 1” are not limited by the further modifications given the claim language is optional. Thus, the up to 35 amino acid modifications can occur anywhere within SEQ ID NO: 1. For claim 28, please note that the Examiner is interpreting the scope as open-ended requiring at least 95% identity to SEQ ID NO: 1 with one or more of the recited substitutions in claim 1 and with any N- and/or C-terminal additions. It is noted that at least 95% identity to SEQ ID NO: 1 encompasses up to 18 amino acid modifications where the modifications include insertions, deletions, and substitutions, but at least one of the 18 must be one of the recited substitutions in claim 1. For claim 28, please note that the Examiner is interpreting the scope as open-ended requiring at least 90% identity to SEQ ID NO: 1 with one or more of the recited substitutions and with any N- and/or C-terminal additions. For claim 29, please note that the Examiner is interpreting the scope as open-ended requiring at least 90% identity to SEQ ID NO: 1 with one or more of the recited substitutions and with any N- and/or C-terminal additions. For claim 30, please note that the Examiner is interpreting the scope as open-ended requiring at least 90% identity to SEQ ID NO: 1 with one or more of the recited substitutions and with any N- and/or C-terminal additions. For claim 31, please note that the Examiner is interpreting the scope as open-ended requiring at least 90% identity to SEQ ID NO: 1 with one or more of the recited substitutions and with any N- and/or C-terminal additions. 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, 20-22, and 28-31 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. Independent claim 1 includes a protein having an amino acid sequence that has at least 90% identity to SEQ ID NO: 1 and comprises one or more amino acid substitutions selected from L53N, V83A, Y117A, Y117F, Y117N, K137A, L146A, G169S, W177Y, K198A, Y217F, P218A, P218T, A245M, S247M, L146A/C150A, L146A/G169S, L146A/W177Y, L146A/Y217F, L146A/P218G, L146A/P218S, L146A/P218T, T147C/G151A, V83A/L146A/P218T, and T147C/G151A/Y217F relative to the positions of SEQ ID NO: 1 (hereinafter referred to as “the specific substitutions”), and optionally further comprises a deletion, substitution or insertion of one or several amino acid residues at a position(s) other than positions 53, 83, 87, 117, 120, 124, 137, 139, 142-143, 146-147, 150-151, 169, 173, 177, 198, 204, 216-218, 231, 238, 245, and 247 (hereinafter referred to as “the specific positions”) . The interpretation of claim 1 is described above in the “Sequence Interpretation” where a protein amino acid sequence encompasses up to 36 amino acid modifications where at least one of the 36 modifications must be a specific substitution, but the remaining 35 amino acid modifications can be located at any other position of SEQ ID NO: 1, even at one of the specific positions since the claim language requiring the specific positions is optional. In addition to certain manipulations of SEQ ID NO: 1, the protein amino acid sequence must also exhibit the function s of channel activity (See instant claim 1), a first ratio greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity (See instant claim 20), and a second ratio greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 600 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity (See instant claim 21). As such , the scope of the claimed protein amino acid sequence encompasses a vast array of mutant sequences without a common core structure or sequence shared among the species that would be necessary for each species to exhibit the claimed functions. Therefore is insufficient support for the vast array of mutant sequences that can result from the specific substitutions, with or without the specific positions, to suggest that there is a core sequence that provides the common structure and/or function necessary to establish possession of the genus as a whole . The written description requirement may be met by provided a representative number of species of the genus and/or in light of the state of the art. With regard to the state of the art, a cation channelrhodopsin , Gt_CCR4, which is one of 44 types of microbial rhodopsins from a cryptophyte flagellate, Guillardia theta , was identified as having modest homology with a chlorophyte channelrhodopsin such as Cr_ChR2 from C hlamydomonas reinhardtii thereby suggesting that Gt_CCR4 has a distinct molecular mechanism for channel gating and ion permeation (See Shigemura et al., Appl. Sci. 9 :13 pages (August 2019) at abstract ; pg. 10, 1 st paragraph ) . Shigemura et al. found that the photocurrent inactivation by Gt_CCR4 was much smaller than that of Cr_ChR2 (i.e., 15% v 50%, respectively), and the light sensitivity for Gt_CCR4 was higher than that of Cr_ChR2 (i.e., EC50 = 0.13 mW /mm2 v EC50 = 0.80 mW /mm2, respectively) while the channel open life time (photocycle speed) was the in the same range (See Shigemura, abstract). Gt_CCR4 also exhibited high Na+ selectivity but almost no H+ and no Ca2+ thereby suggesting that ion selectivity in Gt_CCR4 is distinct from that of Cr_ChR2 (See Shigemura, abstract). The wild-type Gt_CCR4 also resulted in a unique red-absorbing and stable intermediate in the photocycle indicating a photochromic property (See Shigemura, abstract). Thus, Shigemura et al. demonstrated that the wild-type Gt_CCR4 exhibits a distinct molecular mechanism for channel gating and ion permeation when compared to a homologous known channelrhodopsin , Cr_ChR2. Moreover, Shigemura et al. developed about 100 mutant Gt_CCR4 amino acid sequences to determine whether photocurrent could be improved (See Shigemura et al., “Study of cation channelrhodopsin Gt_CCR4 from cryptophyte for optogenetics,” Nagoya Institute of Technology, 1 page (September 2019) at col. 2, 1 st paragraph) (cited in the IDS received on 1/4/23) (note: the reference is being referenced/discussed to the extend possible given that the document is not fully legible ). In particular, Shigemura et al. compared a single substitution of V83A to the Gt_CCR4 wild-type amino acid sequence, which appears to exhibit improved photocurrent (See Shigemura, Fig. 2B). Shigemura et al. concluded that mutants that removed amino acid side chain charge or reduce side chain volume are good, and it is better to mutate amino acids in the permeation pathway or an amino acid near the retina (See Shigemura, col. 2, conclusion section). However, a mutant Gt_CCR4 amino acid sequence (note: V83A is the only mutant that is readily apparent from Shigemura) containing a single substitution is not sufficient to constitute a representative number of species within the claimed genus to demonstrate possession of the claimed genus. Similarly, the prior art demonstrates that the wild-type Gt_CCR4 amino acid sequence exhibits distinct properties when compared to a homologous known channelrhodopsin , and thus, the manipulations known of Cr_ChR2 would not be expected to correlate to manipulations of Gt_CCR4. Thus, the claims are directed to protein amino acid sequences with certain function s but no correlated structure /core sequence associated with th ose function s . Without such structure, the specification does not convey possession of the breadth of the claimed genus. Alternat iv ely, the written description requirement may be met by provided a representative number of species of the genus. In this, the specification provides several examples of specific mutant Gt_CCR4 amino acid sequences as depicted in Tables 1-2 and 4-7. The specification also teaches the amino acid positions of each region of the wild-type Gt_CCR4 protein where positions 1 to 41, 92 to 115, 147 to 165, and 222 to 237 represent the extracellular region; positions 51 to 82, 125 to 138, 174 to 213, and 250 to 367 represent the cytoplasmic region; and positions 42 to 50, 83 to 91, 116 to 124, 139 to 146, 166 to 173, 214 to 221, and 238 to 249 represent the gate region (See instant, [0074]-[0076]). The specification describes substitutions at positions within each region including the specific substitutions claimed (See instant Tables 1-2 and 4-7). However, it is noted that the discussed mutations represent single mutations, i.e., Gt_CCR4 amino acid sequences containing one substitution at an identified position, except for two examples of sequences containing specific tri-mutations, i.e., V83A/L146A/P218A and T147C/G151A/Y217F, and 1 1 examples of sequences containing specific double mutations, e.g., L146A/C150A, L146A/G169S, and T147C/G151A , where the L146A is one of the two substitutions in the double mutants in 9 species (See instant, Tables 1 and 4 -5 ). At most the species described in the specification a re representative of protein amino acid sequences containing a single substitution and a double mutant containing at least the single mutation of L146A. There are no examples of any protein amino acid sequences containing deletions or insertions as optionally recited in claim 1. Furthermore, Figure 4 depicts the channel activity ratios for a number of protein amino acid sequences containing single mutations, 10 double mutations, and 2 triple mutations. As depicted in Figure 4, the channel activity ratios vary greatly depending on the substitution type and position substituted. For example S247 when substituted to Ala resulted in a first ratio of 0.57 and a second ratio of 0.24, but when substituted to Met the first ratio was 0.27 and the second ratio was 0.19 (See instant Figure 4). Similarly, channel activity diminished significantly for the W177Y, A245M , S247A , and V83A/L146A/P218T substitutions (See instant, Figure 3) thereby demonstrating that even single substitutions can impart a significant impact on channel activity. Plus, it is noted that combining more than one mutation can greatly affect the channel activity. For example the single mutations of V83A, L146A, and P218T either significantly improved channel activity (i.e., V83A) or remained relative the same when considering statistical significance (i.e., L146A or P218T), but when the three mutations were combined in the same sequence, the channel activity was reduced relative to the wild-type Gt_CCR4 (See instant, Figure 3). As such, the instant specification demonstrates that even the single mutations may not be expected to exhibit similar channel activity and/or first/second ratios when combined, let alone when combined with identified deletions, insertions or substitutions. Thus, the species described in the specification do not constitute a representative number of species exhibiting the claimed functions such that an ordinary skilled artisan can extrapolate to extend to the scope of the claimed genus. Therefore, th e specification is not sufficient for the skilled artisan to envisage other substitutions at other residue sites which preserve function nor to envisage which combination of substitutions other than those claimed with an expectation that function will be preserved. Vas-Cath Inc. v. Mahurkar , 19USPQ2d 1111, clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, what is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116). As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of polypeptides which preserve the required function, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel , 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd. , 18 USPQ2d 1016. One cannot describe what one has not conceived. See Fiddes v. Baird , 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence. Therefore, claims 1, 20-22, and 28-31 do not meet the written description requirement. Claim Rejections - 35 USC § 112 The following is a quotation of 35 U.S.C. 112(d): (d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph: Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers. Claim 20 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 20 is directed to where the protein has a first ratio that is greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity . However, claim 20 is dependent upon claim 1, which recites that the protein has an amino acid sequence comprising one or more substitutions selected from a Markush of specific substitutions. As discussed in the “Sequence Interpretation” section supra , the protein must have one of these substitutions. Although not all substitutions recited are required in one amino acid sequence , the scope of claim 1 encompasses multiple embodiments , i.e., different species each having one of the recited substitutions . A dependent claim should further limit each embodiment when the dependent claim recites only functional language and does not further limit the structure of the protein because " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. As demonstrated in instant Figure 4, the following substitutions do not exhibit a first ratio greater than or equal to 0.4: K137A, K198A, P218A, P218T, A245M, S247M, and V83A/L146A/P218T (See instant Figure 4). Thus, the scope of claim 20 does not further limit the scope of claim 1 when the protein amino acid sequence contains each of the these substitutions. Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. Please note that the Examiner is interpreting that claim 20 is only applicable for protein amino acid sequences of claim 1 that excludes substitutions: K137A, K198A, P218A, P218T, A245M, S247M, and /or V83A/L146A/P218T, in order to advance prosecution. Claim 21 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 21 is directed to where the protein has a second ratio that is greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 600 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity. However, claim 21 is dependent upon claim 1, which recites that the protein has an amino acid sequence comprising one or more substitutions selected from a Markush of specific substitutions. As discussed in the “Sequence Interpretation” section supra , the protein must have one of these substitutions. Although not all substitutions recited are required in one amino acid sequence, the scope of claim 1 encompasses multiple embodiments, i.e., different species each having one of the recited substitutions. A dependent claim should further limit each embodiment when the dependent claim recites only functional language and does not further limit the structure of the protein because " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. As demonstrated in instant Figure 4, the following substitutions do exhibit a second ratio greater than or equal to 0.4: L146A, P218T, L146A/C150A, L146A/G169S, L146A/W177Y, L146A/P218G, L146A/P218T, T147C/G151A, and V83A/L146A/P218T (See instant Figure 4). Thus, the scope of claim 20 does not further limit the scope of claim 1 when the protein amino acid sequence contains a recited substitution in claim 1 other than the above-identified, e.g., L53N and V83A . Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements. Please note that the Examiner is interpreting that claim 2 1 is only applicable for protein amino acid sequences of claim 1 that contains the substitutions: L146A, P218T, L146A/C150A, L146A/G169S, L146A/W177Y, L146A/P218G, L146A/P218T, T147C/G151A, or V83A/L146A/P218T , in order to advance prosecution. 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. Claim s 1, 20, 22, and 28 are rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Shigemura et al., “Study of Cation Channelrhodopsin Gt_CCR4 from Cryptophyte for Optogenetics,” Nagoya Institute of Technology, 1 pages (September 2019) , alone or as evidenced by, GenBank Accession No. ARQ20888 , 1 page (2017) . Please note that the Examiner is interpreting that the publication date of Shigemura is September 2019 as discussed in the “Information Disclosure Statement” section supra . Applicant cannot rely upon the certified copy of the foreign priority application to overcome this rejection because a translation of said application has not been made of record in accordance with 37 CFR 1.55. When an English language translation of a non-English language foreign application is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216. For claims 1, 22, and 28, Shigemura et al. discloses a mutant light-gated cation channelrhodopsin derived from Guillardia theta where the mutant amino acid sequence contains a V83A substitution (See Shigemura, col. 1, 4 th paragraph; col. 2, Figure 2B). Although Shigemura et al. does not expressly disclose the full Gt_CCR4 V83A amino acid sequence , the GenBank reference discloses the wild-type Gt_CCR4 amino acid sequence (See GenBank reference). When comparing instant SEQ ID NO: 1 with a V83A substitution with the wild-type Gt_CCR4 amino acid sequence, there are 3 amino acid modifications, i.e., V83A, M237, and S290. As such, Shigemura’s Gt_CCR4 V83A amino acid sequence is at least 99% identical to instant SEQ ID NO: 1. Therefore, Shigemura’s Gt_CCR4 V83A amino acid sequence constitutes a protein as recited in instant claims 1, 22, and 28. Regarding the protein having a channel activity, Shigemura et al. discloses in Figure 2B that the Gt_CCR4 V83A amino acid sequence exhibits channel activity (See Shigemura, col. 2, Figure 2B). Additionally and/or alternatively, even though Shigemura et al. expressly discloses that the Gt_CCR4 V83A amino acid sequence exhibits a channel activity, it is unnecessary for Shigemura et al. to disclose this property. Since Shigemura et al. discloses a protein amino acid sequence having a V83A substitution and is at least 90% identical to instant SEQ ID NO: 1 thereby constituting a known protein sequence, the functional property (i.e., having a channel activity) of the claimed protein sequence and the known protein sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc. , 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., a channel activity) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best , 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Additionally, " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. Therefore, the Shigemura et al. disclosure satisfies the claim limitation with respect to where the protein has a channel activity as recited in instant claim 1. For claim 20, although Shigemura et al. does not expressly disclose that the Gt_CCR4 V83A amino acid sequence exhibits a first ratio greater than or equal to 0.4the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity, it is unnecessary for Shigemura et al. to disclose this property. Since Shigemura et al. discloses a protein amino acid sequence having a V83A substitution and is at least 90% identical to instant SEQ ID NO: 1 thereby constituting a known protein sequence, the functional property (i.e., a first ratio greater than or equal to 0.4the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) of the claimed protein sequence and the known protein sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc. , 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., a first ratio greater than or equal to 0.4the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best , 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Additionally, " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. Therefore, the Shigemura et al. disclosure satisfies the claim limitation as recited in instant claim 20. Accordingly, the Shigemura disclosure anticipates instant claims 1, 20, 22, and 28. Double Patenting The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg , 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman , 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi , 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum , 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel , 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington , 418 F.2d 528, 163 USPQ 644 (CCPA 1969). A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b). The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13. The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA/25, or PTO/AIA/26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer . Claims 1, 20-22, and 28 are rejected on the ground of nonstatutory double patenting a s being unpatentable over claims 1-6 of U.S. Patent No. 12,030,917 B2 . Although the claims at issue are not identical, they are not patentably distinct from each other because ‘917 claims a protein composed of the amino acid sequence of SEQ ID NO: 1 with one or more mutations and having channel activity where the one or more mutations can be L53N, V83A, K137A, L146A, and L198A, and optionally further comprises a deletion, substitution, or insertion of one or two amino acid residues and the amino acid sequence of the protein has 90% or more identity with the amino acid sequence of SEQ ID NO: 1 (See ‘917, claim 1). As such, when comparing ‘917’s SEQ ID NO: 1 having one or more of the above-identified mutations with instant SEQ ID NO: 1 having one or more of the same mutations, there is 100% identity. ‘917 also claims functional properties of the protein (See ‘917, claim 2), a drug composition comprising the protein (See ‘917, claim 3), and methods of using the protein (See ‘917, claims 4-6). Thus, the ‘917 claimed invention anticipates instant claims 1, 22 and 28. Although ‘917 does not expressly claim that the protein exhibits a first ratio greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity, it is unnecessary for ‘917 to claim this property. Since ‘917 claims a protein amino acid sequence having a L53N, V83A, K137A, L146A, and/or L198A substitution and is at least 90% identical to instant SEQ ID NO: 1 thereby constituting a known protein sequence, the functional property (i.e., a first ratio greater than or equal to 0.4the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) of the claimed protein sequence and the known protein sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc. , 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., a first ratio greater than or equal to 0.4 where the first ratio is a value corresponding to a channel activity at 440 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best , 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Additionally, " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. Therefore, the ‘917 claimed invention satisfies the claim limitation as recited in instant claim 20. Similarly, although ‘917 does not expressly claim that the protein exhibits a second ratio greater than or equal to 0.4 where the second ratio is a value corresponding to a channel activity at 600 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity, it is unnecessary for ‘917 to claim this property. Since ‘917 claims a protein amino acid sequence having a L53N, V83A, K137A, L146A, and/or L198A substitution and is at least 90% identical to instant SEQ ID NO: 1 thereby constituting a known protein sequence, the functional property (i.e., a second ratio greater than or equal to 0.4 where the second ratio is a value corresponding to a channel activity at 600 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) of the claimed protein sequence and the known protein sequence are inherently the same. The discovery of a previously unappreciated property of a prior art composition, or a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer. Atlas Powder Co. v. Ireco Inc. , 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus, the claiming of a new functional property (i.e., a second ratio greater than or equal to 0.4 where the second ratio is a value corresponding to a channel activity at 600 nm relative to the value corresponding to the channel activity at the wavelength ( λmax ) at which the protein exhibits its maximum channel activity) which is inherently present in the prior art does not necessarily make the claim patentable. In re Best , 562 F.2d 1252, 1254, 195 USPQ 430, 4333 (CCPA 1977). Additionally, " [p] roducts of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. See MPEP 2112.01. Thus, the ‘917 claimed invention satisfies the claim limitation as recited in instant claim 21. Therefore, the ‘917 claimed invention is not patentably distinct from the instantly claimed invention. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT THEA D' AMBROSIO whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)270-1216 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 11:00 to 8:00 pm . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Lianko Garyu can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 571-270-7367 . The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /THEA D' AMBROSIO/ Primary Examiner, Art Unit 1654