CTNF 18/263,085 CTNF 101352 DETAILED ACTION 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Claim(s) 1-17 and 21-26 are pending. Preliminary Amendments Applicant’s preliminary amendment filed on 07/26/2022 is acknowledged. The claims were amended to (1) cancel claims 18-20; (2) amend claims 3-14, 16-17, and 25; and (3) add claim 26. Election/Restrictions 08-25-01 AIA Applicant’s election without traverse of Group I in the reply filed on 05/20/2026 is acknowledged. 08-06 AIA Claim 26 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention of Group II , there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 05/20/2026 . 08-25-01 AIA Applicant’s election without traverse of the species of vector genome sequence, SEQ ID NO: 21 , in the reply filed on 05/20/2026 is acknowledged. 08-06 AIA Claim (s) 9 and 11 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species , there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 05/20/2026 . Claim(s) 1-8, 10, 12-17, and 21-25 are under consideration . Priority Acknowledgement is made that this application is a 371 of PCT/US2022/014742 filed 02/01/2022 and claims priority based on provisional application(s) filed as 63/144,103 on 02/01/2021 and 63/286,939 on 12/07/2021 All claims are given the priority date of 02/01/2021 . Information Disclosure Statement Receipt of the information disclosure statement(s) on 01/12/2024, 06/25/2025, and 05/20/2026 are acknowledged. The signed and initialed PTO-1449 form(s) has/have been mailed with this action. Drawings The drawings are objected to under 37 CFR 1.83(a) because they fail to show: cholesterol storage in the brain in FIGs 2A-C ; 06-22-01 cholesterol storage in the brain in FIG 4A ; as described in the specification. Any structural detail that is essential for a proper understanding of the disclosed invention should be shown in the drawing. MPEP § 608.02(d). 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. Specification The use of the term(s): GenBank (line 5 and 15, page 26); PubMed (line 15, page 26); Solutol (line 6, page 33); Labrasol (line 6, page 33); Tween (line 7, page 33); Pluronic (line 29, page 33); which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term. Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. 07-29 AIA The disclosure is objected to because of the following informalities: Page 56, <222> “(1940)..(19456)” should be amended to recite the proper length of the provided Kozak sequence, “1945” . Appropriate correction is required. Claim Objections PNG media_image1.png 234 672 media_image1.png Greyscale Claim 3 is objected to because of the following informalities: SEQ ID NO: 2 and 23 are identical in length and sequence (see alignment below). It would be remedial to amend the claim to only recite one of the sequences because both in the claim is redundant. 07-29-01 AIA Claim 24 is objected to because of the following informalities: (1) a missing comma after “claim 23”, (2) the use of “where” instead of “wherein” which is used as the previous claim(s) language, and (3) “vector gene” should be “vector genome”, and (4) “comprises” is used twice throughout the body of the claim which is redundant. The claim should be amended to recite, “The plasmid according to claim 23 , which comprises a vector genome for packaging into an rAAV, where in the vector gene genome comprises the engineered nucleic acid sequence, regulatory sequences, and comprises a 5' inverted terminal repeat sequence (ITR) and a 3' ITR, at the extreme 5' end and the extreme 3' end, respectively, of the vector genome.” Appropriate correction is required. 07-30-03-h AIA Claim Interpretation SMPD1 is also referred to ASM (instant specification page 5, lines 29-31). Claim Rejections - 35 USC § 112b 07-30-02 AIA 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. 07-34-01 Claim 4 is 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. SEQ ID NO: 2 only contains 629 amino acids, therefore the identity of amino acids 630-631 is unknown. As well as, the parenthesis, i.e., “amino acids 47 to 631 of SEQ ID NO: 2 (or SEQ ID NO: 31)” make it unclear whether “(or SEQ ID NO: 31)” is a limitation or merely an example of a sequence that may be present. It would be remedial to amend claim 4 to replace “amino acids 47-631 of SEQ ID NO: 2 (or SEQ ID NO: 31)” with the phrase “SEQ ID NO: 31.” Claim Rejections - 35 USC § 103 07-20-aia AIA 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. 07-23-aia AIA The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. 07-21-aia AIA Claim (s) 1-4, 14-17, and 21-25 are rejected under 35 U.S.C. 103 as being unpatentable over Passini et al (US 2009/0117156 A1, published 05/07/2009; see PTO 892 02/24/2026) in view of Schuchman et al (US 6,541,218 B1, published 04/01/2003; see PTO 892 02/24/2026) in further view of Wang et al (Adeno-associated virus vector as a platform for gene therapy delivery, Nature Reviews Drug Discovery, Vol 18, pages 358-378, published February 1 st , 2019) . Passini et al teaches, “As noted above, the transgene encoding the polypeptide or protein is administered to the mammal to ultimately deliver the polypeptide or protein using any appropriate gene transfer methods, examples of which are described supra and in U.S. Pat. No. 6,066,626. In one aspect, the transgene encodes ASM (synonym for SMPD1). The genomic and functional cDNA sequences of human ASM have been published in for example, U.S. Pat. Nos. 5,773,278 and 6,541,218).”, (paragraph [0055]). Regarding claim(s) 1, 4, and 21-24 , Passini et al discloses, “The full-length human ASM cDNA was cloned into a plasmid containing ITRs from AAV serotype 2 and 8. . . AAV2-hASM contained serotype 2-inverted terminal repeats (ITRS) and the human acid sphingomyelinase (hASM) cDNA under the control of the CMV enhancer and chicken beta-actin promoter . Both recombinant vectors were produced by triple plasmid co-transfection of human 293 cells and column-purified. The final titers of the AAV8-hASM and AAV2-hASM preparations were 5.0. x 10 12 genome copies (gc) per ml, as determined by TaqMan PCR of the bovine growth hormone polyadenylation signal sequence which each vector contains . Hybrid vectors can be produced by triple transfection using a series of helper plasmids containing serotype specific capsid coding domains in addition to the AAV serotype replication genes.”, (para [0108]-[0109]). Regarding claim(s) 14-17, Passini et al teaches injecting AAV2-hASM into the central nervous system of mice with 2.0e11 genome copies per brain (see figure 1). Moreover, Passini et al teaches, “A combination injection protocol of AAVhASM that targets both the brain and viscera was evaluated in addressing the functional abnormalities and disease sequelae of the ASMKO mouse. In the combination group (n=11), ASMKO mice at 4 weeks of age received 3.0 x 10 11 genome copies (gc) of AAV8-hASM via tail vein injection . Two weeks later, at 6 weeks of age, the same mice were injected with AAV2-hASM into the motor cortex, striatum, midbrain, and cerebellum of the left hemisphere, and into the hypothalamus, hippocampus, medulla, and cerebellum of the right hemisphere. . .”, (see para [0127]). Wherein “genome copies” reads on a population of rAAV. Wherein “tail vein injection” reads on intravenous injection. Regarding claim 25 , Passini et al teaches, “Both recombinant vectors were produced by triple plasmid co-transfection of human 293 cells and column-purified . The final titers of the AAV8-hASM and AAV2-hASM preparations were 5.0. x 10 12 genome copies (gc) per ml, as determined by TaqMan PCR of the bovine growth hormone polyadenylation signal sequence which each vector contains. Hybrid vectors can be produced by triple transfection using a series of helper plasmids containing serotype specific capsid coding domains in addition to the AAV serotype replication genes .”, (para [0108]-[0109]). Passini et al refers to the genomic and functional cDNA sequences of human ASM that have been published in US 6,541,218, however, Passini et al does not explicitly recite the sequence of ASM. Schuchman et al, referred to as US 6,541,218 in Passini et al, teaches the protein and genomic sequences of ASM. Regarding claim(s) 1-3, 15 and 21 , Schuchman et al discloses both the nucleic acid sequence and amino acid sequence for ASM in FIG. 3A-C. In FIG. 3A-C of Schuchman et al, the nucleic acid sequence is labeled as SEQ ID NO: 1, and the amino acid sequence is labeled as SEQ ID NO: 2 (Page 24, col 3, lines 9 and 10). SEQ ID NO: 2 of Schuchman et al is at least 99% identical to the translated sequence of the instant SEQ ID NO: 22. Wherein alanine is the wild-type amino acid present at position 36 (claim(s) 2 and 15). Passini et al and Schuchman et al do not teach codon optimization of human ASM or a exogenous leader sequence. Regarding claim(s) 1-3 and 21 , Wang et al teaches, “. . . For gene expression in human cells, even wild-type human-derived gene sequences are not necessarily optimized to yield robust protein expression. This is in part because a natural sequence may not fully utilize the most preferred codon for an amino acid residue. In addition, elements of the transgene sequence itself, such as GC content, cryptic splice sites, transcription termination signals, motifs that affect RNA stability and nucleic acid secondary structures, can impact on expression. Therefore, codon optimization is widely used in rAAV gene therapy aiming to enhance gene expression . . .” (see page 365, col 1, line 11-21). Regarding claim 4 , “At the translational level, inclusion of a Kozak sequence can further increase protein expression. . .” (see page 365, col 1, line 21-22). Wherein Kozak sequence reads on an exogenous leader sequence. It would have been obvious to try one of ordinary skill in the art before the effective filing date of the claimed invention to modify the AAV2-hASM as taught by Passini et al in view of Schuchman et al through codon-optimized as taught by Wang et al. SEQ ID NO: 2 of Schuchman et al is at least 99% identical to the translated sequence of SEQ ID NO: 22. Wang et al teaches that even wild-type human-derived gene sequences are not necessarily optimized to yield robust protein expression, and that codon optimization is widely used in rAAV gene therapy. Given that these sequences (SEQ ID NO: 2 of Schuchman et al and the translation of instant SEQ ID NO: 22) are at least 99% identical, there are finite positions within the coding sequence to optimize and still yield a protein sequence that is at least 99% identical. One of skill in the art could have codon optimized SEQ ID NO: 1 of Schuchman et al, which is the genomic sequence of SEQ ID NO: 2, to predictably yield instant SEQ ID NO: 22. One would have been motivated to do so to enhance gene expression of an rAAV, as taught by Wang et al. Further, it would have been obvious to try one of ordinary skill in the art before the effective filing date of the claimed invention to modify the codon-optimized AAV2-hASM as taught by the combination Passini et al and Schuchman et al in view of Wang et al, by adding a kozak sequence as an exogenous leader sequence, as taught by Wang et al. One would have been motivated to add the kozak sequence because at the translational level, a kozak sequence can further increase protein expression, as taught by Wang et al. Accordingly, claim(s) 1-4, 14-17, and 21-25 are unpatentable over Passini et al in view of Schuchman et al in further view of Wang et al . 07-21-aia AIA Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Passini et al (US 2009/0117156 A1, published 05/07/2009; see PTO 892 02/24/2026) in view of Schuchman et al (US 6,541,218 B1, published 04/01/2003; see PTO 892 02/24/2026) in view of Wang et al (Adeno-associated virus vector as a platform for gene therapy delivery, Nature Reviews Drug Discovery, Vol 18, pages 358-378, published February 1 st , 2019) as applied to claim(s) 1-4, 14-17, and 21-25 above, and further in view Ambrosi et al (Adeno-Associated Virus Mediated Gene Delivery: Implications for Scalable in vitro and in vivo Cardiac Optogenetic Models, Front Physiol, volume 10, issue 168, pages 1-13, published 03/05/2019) . Despite Passini et al and Wang et al teaching CMV enhancer and the chicken beta actin promoter, which are components of CB7, Passini et al, Schuchman et al, and Wang et al, do not teach CB7 promoter. Regarding claim 5, Ambrosi et al teaches, “CMV, CAG, and CB7 are all strong ubiquitous promoters that are commonly used. CAG/CB7 are considered identical and interchangeable by the UPenn Core and there is no literature to differentiate between the performance of the two. CAG/CB7 is a synthetic promoter, a derivative of CMV with added transcribed sequence from chicken beta-actin gene and enhancer elements (Miyazakietal.,1989). In most cases, CAG/CB7 is considered a stronger version of CMV.”, (see page 10, column 2, para 3 to page 11, column 1, para 1). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the CMV enhancer and chicken beta globin promoter as taught by the combination of Passini et al, Shuchman et al, and Wang et al with CB7 promoter, as taught by Ambrosi et al. One could have substituted the CMV enhancer and chicken beta promoter for CB7 and yield the predictable results of maintaining expression because Ambrosi et al teaches CB7 is a derivative of CMV with chicken beta actin and enhance elements. Accordingly, claim 5 is unpatentable over Passini et al in view of Schuchman et al in view of Wang et al and in further view of Ambrosi et al . 07-22-aia AIA Claim (s) 6-8 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Passini et al (US 2009/0117156 A1, published 05/07/2009; see PTO 892 02/24/2026) in view of Schuchman et al (US 6,541,218 B1, published 04/01/2003; see PTO 892 02/24/2026) in view of Wang et al (Adeno-associated virus vector as a platform for gene therapy delivery, Nature Reviews Drug Discovery, Vol 18, pages 358-378, published February 1 st , 2019) in further view of Ambrosi et al (Adeno-Associated Virus Mediated Gene Delivery: Implications for Scalable in vitro and in vivo Cardiac Optogenetic Models, Front Physiol, volume 10, issue 168, pages 1- 13, published 03/05/2019) as applied to claim 5 above, and further in view of Balazs et al (US 8,865,881 B2, published 10-21-2014) . It is acknowledged that claim(s) 6-8 and 10 do not depend from claim 5, however, the limitation of claim 5, which is dependent upon claim 1, is applicable to claim 6, 7, and 8, and within the scope of claim 1. Claim 7 limits the promoter to a “CB7 hybrid promoter”, and the instant specification defines CB7 hybrid promoter to also be called CB7 (page 13, lines 27-28). Claim 8 limits the vector genome sequence to SEQ ID NO: 21, which includes the CB7 promoter. Passini et al, Shuchman et al, Wang et al, and Ambrosi et al do not teach regulatory sequences such as SV40 late, rabbit beta globin, or a UbC promoter. Regarding claim 6 , Balazs et al teaches using SV40 late poly A and rabbit beta globin (RBG) and Bovine Growth Hormone (BGH) interchangeably in AAVs without effecting luciferase expression (see Fig. 1D; Col 3, lines 19-25; and Col 36, lines 63-67). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the bovine growth hormone polyadenylation signal sequence as taught by the combination of Passini et al, Shuchman et al, Wang et al, and Ambrosi et al with a rabbit beta globin or SV40 polyadenylation sequence, as taught by Balazs et al. One could have substituted the BGH for SV40 or RBG and yield the predictable results of maintaining expression because Balazs et al teaches that these regulatory sequences are interchangeable. Passini et al, Shuchman et al, Ambrosi et al, and Balazs et al do not teach the addition of an intron into the AAV. Regarding claim 7 and 8 , Wang et al does teach an incorporation of an intron into an AAV, more specifically, “In many cases, rAAV gene therapy platforms utilize a strong and ubiquitous promoter to achieve high transgene expression. Such promoters include the cytomegalovirus (CMV) promoter and the chicken β-actin promoter fused with the CMV enhancer. Other regulatory elements can also enhance gene expression, such as an intron and the woodchuck hepatitis post-transcriptional regulatory element (WPRE). . .”, (see page 365, col 1, line 2-9). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the AAV2-hASM as taught by the combination of Passini et al, Schuchman et al, Wang et al, Ambrosi et al, and Balazs et al, to add an intron, as taught by Wang et al. One could add an intron into the AAV2-hASM to yield the predictable results of enhancing gene expression, as taught by Wang et al. Passini et al, Schuchman et al, Wang et al, and Ambrosi et al do not teach a UbC promoter. Regarding claim 10 , Balazs et al teaches that CMV, CAG, and UbC promoters provide comparable robust muscle expression (see Fig. 1A; col 2, lines 65-67; and, col 36, lines 37-47). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the CB7 as taught by the combination of Passini et al, Schuchman et al, Wang et al, Ambrosi et al, and Balazs et al with UbC as taught by Balazs et al. One could have substituted CB7 promoter for UbC and yield the predictable results of maintaining expression because Ambrosi et al teaches that the CAG/CB7 are identical and interchangeable, and Balazs teaches utilizing CMV, CAG, and UbC and that these promoters provide comparable and robust muscle expression. Accordingly, claim(s) 6-8 and 10 are rejected as being unpatentable over Passini et al in view of Schuchman et al in view of Wang et al in view of Ambrosi et al, and in further view of Balazs . 07-22-aia AIA Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Passini et al (US 2009/0117156 A1, published 05/07/2009; see PTO 892 02/24/2026) in view of Schuchman et al (US 6,541,218 B1, published 04/01/2003; see PTO 892 02/24/2026) in further view of Wang et al (Adeno-associated virus vector as a platform for gene therapy delivery, Nature Reviews Drug Discovery, Vol 18, pages 358-378, published February 1 st , 2019) as applied to claim (s) 1-4, 14-17, and 21-25 above, and further in view of Zhou et al (Deletion of the B-B’ and C-C’ regions of inverted terminal repeats reduces rAAV productivity but increases transgene expression, Scientific Reports, volume 7, pages 1-13, published 07/17/2017) . Passini et al, Schuchman et al in, and Wang et al do not teach the full length sequence of AAV2 ITR. Regarding claim 12 , Zhou et al teaches the full-length wt ITR of AAV2 in figure 1a, and a truncated version of AAV2 ITR in figure 1b. Zhou et al teaches that these mutations were made to examine the effects of the ITR truncation on packaging and expression of the rAAV. Zhou et al further teaches, “The results revealed that deletions in the two ITRs did not affect rAAV encapsulation but decreased productivity. . . rAAV plasmids with deletions of RBE’ and adjacent sequences have been shown to exhibit lower rates of replication than wt AAV constructs, consistent with the reduced replication of rAAVbiΔBC observed in our study (Fig. 3a,b). Our results suggest that deletion of the B-B’ and C-C’ regions impairs the genome replication of rAAV and ultimately reduces productivity.”, (see page 9, paragraph 2). Thus, it would been obvious to try one of ordinary skill in the art before the effective filing date of the claimed invention to have the AAV2 ITR(s) of the AAV2-hASM as taught by the combination of Passini et al, Schuchman et al, and Wang et al, be full-length AA2 ITRs as taught by Zhou et al. One of skill would have the full-length AAV2 ITR in the rAAV to yield the predictable results of maintaining genome replication and productivity. Accordingly, claim 12 is unpatentable over Passini et al in view of Schuchman et al in view of Wang et al, in further view of Zhou et al . 07-22-aia AIA Claim 13 is rejected under 35 U.S.C. 103 as being unpatentable over Passini et al (US 2009/0117156 A1, published 05/07/2009; see PTO 892 02/24/2026) in view of Schuchman et al (US 6,541,218 B1, published 04/01/2003; see PTO 892 02/24/2026) in further view of Wang et al (Adeno-associated virus vector as a platform for gene therapy delivery, Nature Reviews Drug Discovery, Vol 18, pages 358-378, published February 1 st , 2019) as applied to claim (s) 1-4, 14-17, and 21-25 above, and further in view of Wilson et al (US 2020/0056159 A1, published 02/20/2020, effective filing date of 01/05/2018; IDS filed 01/24/2024 citation number 19) . The applied reference of Wilson et al has a common inventor 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). Passini et al, Schuchman et al, and Wang et al do not teach an AAVhu68 capsid. Regarding claim 13 , Wilson et al teaches, “Provided herein are nucleic acid sequences and amino acids of a novel isolated adeno-associated virus (AAV), which is termed herein AAVhu68, which is within clade F. AAVhu68 (previously termed herein AAV3G2) varies from another Clade F virus AAV9 (SEQ ID NO: 5) by two encoded amino acids at positions 67 and 157 of vp1, SEQ ID NO: 2. In contrast, the other Clade F AAV (AAV9, hu31, hu31) have an Ala at position 67 and an Ala at position 157. Provided are novel AAVhu68 capsids and/or engineered AAV capsids having valine (Val or V) at position 157 based on the numbering of SEQ ID NO: 2 and optionally, a glutamic acid (Glu or E) at position 67. . . These AAV capsids described herein are useful for generating recombinant AAV (rAAV) vectors that are provide good yield and/or packaging efficiency, and providing rAAV vectors useful in transducing a number of different cell and tissue types. Such cells and tissue types may include, without limitation, lung, heart, muscle, liver, pancreas, kidney, brain, hippocampus, motor cortex, cerebellum, nasal epithelial cells, cardiac muscle cells or cardiomyocytes, hepatocytes, pulmonary endothelial cells, myocytes, pulmonary epithelial cells, islet cells, acinar cells, renal cells, and motor neurons.”, (see para [0046]). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the AAV2 Capsid of the rAAV as taught by the combination of Passini et al, Schuchman et al, and Wang et al, with the AAVhu68 capsid as taught by Wilson et al. One could have substituted the AAVhu68 capsid for the AAV2 capsid to yield the predictable results of providing good yield and/or packaging efficiency, and usefulness for transducing a number of different cell and tissue types (e.g., lung, heart, muscle, liver, pancreas, kidney, brain, hippocampus, motor cortex, cerebellum, etc.), as taught by Wilson et al. Accordingly, claim 13 is rejected as being unpatentable over Passini et al in view of Schuchman et al in view of Wang et al in further view of Wilson et al. This rejection under 35 U.S.C. 103 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); 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 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. See generally MPEP § 717.02. Conclusion No claims allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to LEXUS M TATGE whose telephone number is (571)272-0061. The examiner can normally be reached Monday-Friday: 8:30am to 5:30pm. 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, Jennifer Dunston can be reached at (571) 272-2916. 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. /L.M.T./Examiner, Art Unit 1637 /Jennifer Dunston/Supervisory Patent Examiner, Art Unit 1637 Application/Control Number: 18/263,085 Page 2 Art Unit: 1637 Application/Control Number: 18/263,085 Page 3 Art Unit: 1637 Application/Control Number: 18/263,085 Page 4 Art Unit: 1637 Application/Control Number: 18/263,085 Page 5 Art Unit: 1637 Application/Control Number: 18/263,085 Page 6 Art Unit: 1637 Application/Control Number: 18/263,085 Page 7 Art Unit: 1637 Application/Control Number: 18/263,085 Page 8 Art Unit: 1637 Application/Control Number: 18/263,085 Page 9 Art Unit: 1637 Application/Control Number: 18/263,085 Page 10 Art Unit: 1637 Application/Control Number: 18/263,085 Page 11 Art Unit: 1637 Application/Control Number: 18/263,085 Page 12 Art Unit: 1637 Application/Control Number: 18/263,085 Page 13 Art Unit: 1637 Application/Control Number: 18/263,085 Page 14 Art Unit: 1637 Application/Control Number: 18/263,085 Page 15 Art Unit: 1637 Application/Control Number: 18/263,085 Page 16 Art Unit: 1637 Application/Control Number: 18/263,085 Page 17 Art Unit: 1637 Application/Control Number: 18/263,085 Page 18 Art Unit: 1637 Application/Control Number: 18/263,085 Page 19 Art Unit: 1637
Prosecution Insights