DETAILED ACTION The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Claims 1-13 are pending. This application claims priority to CN 202211032991.2 filed 8/26/2022. The certified priority document is present in the file. However, it is not in English. Hence, a pplicant cannot rely upon the foreign priority papers to overcome any art rejection s in this case because a translation of said papers has not been made of record in accordance with 37 CFR 1.55. See MPEP § 201.15. Hence, the effective filing date for purposes of examination is 10/25/2023. Claim Objections Clai m 1 is objected to becaus e of the following informalities: grammatically in claim 1, lines 11 should recite that –the expression levels from the first expression cassette--. The expression is not of the cassette but from the cassette promoter and of the coding sequence . Claim 3 provides a choice of the first, the second and/or the third promoter. The formatting is more accurately provided if amended as --at least one of the first, second and third promoter--. This allows all three promoters to be equally considered without ambiguity. Furthermore, there are a number of abbreviations in claim 3 that are provided without the full spelling. Although claims are allowed abbreviations, if an abbreviation is not spelled out upon first use in a claim, MPEP §2429 guides Applicant s to only use abbreviations that are specifically defined in "WIPO Standard ST.25 (1998)" or that are well known and would be clear to someone who had not read the invention description. Appropriate correction is required. Claim Rejections - 35 USC § 112, second paragraph 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 2, 3, 5-8 and 10-13 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claims 2, 3, 5, 7, 8, 10 and 13 are vague and indefinite in that the metes and bounds of the term “ preferably ” and “more preferably” are unclear. It is unclear if the components are necessary for the invention or simply a consideration. Claim 6 recites the limitation "the immunoglobin " in claim 1. There is insufficient antecedent basis for this limitation in the claim. There are multiple references to “ Ig chain coding sequences ” which then is several references to “an immunoglobulin” chain. However, there is no single reference to ‘an immunoglobulin” . Claim 11 recites the limitation "the host cell " in claim 8 . There is insufficient antecedent basis for this limitation in the claim. It appears this claim should depen d from claim 9. Claim 13 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. Claim 13 recites “use of the expression vector as defined in claim 1 for an increasing expression level of an immunoglobulin”. While the claim is clearly drawn to a method and hence does not fail to comply with 35 USC 101 , neither it nor claim 1 provide actual steps for using the expression vector. Hence, the claim to a process without setting forth any steps involved in the process renders the claim indefinite. Claim Rejections - 35 USC § 112, first paragraph The following is a quotation of the first paragraph of 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 1-13 are rejected under 35 U.S.C. 112, 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(s), at the time the application was filed, had possession of the claimed invention. The written description requirement for genus claims may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant identifying characteristics, i.e. structure or other physical and/or chemical properties, by functional characteristics coupled with known or disclosed correlations between function and structure, or by a combination of such characteristics sufficient to show that the applicant was in possession of the claimed genus. The instant invention is directed an expression vector which is described in terms of functional properties. The vector must be able to express the first and/or second expression cassette contained within as a lever that is not less than that of the third expression cassette. As well, the transcriptional regulatory elements ascribed to each of the first and second cassette must have a capability of initiating transcription no less tha n that of the third transcriptional regulatory element (claim 1 and claim 2 for the latter property). Claims 7 and 8 further limit the functional properties to specif y the activity of each promoter in terms of ratios of levels. Finally, claim 13 recites ‘use” of the expression vector for increasing an expression level of a ratio of a heavy and/or a light to J chain to great than one. At issue with the vector claims is the description of the structure of the vector to mediate the function. A review of the disclosure will follow but it appears that it is the nature of the transcriptional regulatory elements that creates this effect. This extends to the use of the vector claim as recited in claim 13. This claim requires an increase of the ratio of expression of heavy and/or light to J of greater than 1. As a method claim, it lacks Claim 3 recites a list of promoters from which each of the regulatory elements are selected. It is noted that the first, second and third rely on the same pool of promoters except in a preferably section of the claim. However, overlap still exists for the three transcriptional regulatory elements. One of the promoters is an artificial promoter. For this large breadth of promoters, the disclosure does not provide examples. Claim 4 requires that the transcriptional regulatory element is located upstream of the coding regions. However, the disclosure is limited thus to this configuration and hence the description beyond this arrangement is limited. As a second set of issues is the immunoglobulin claimed in claim 11 and 12. However, it is noted that the expression vector does not necessarily lead to an immunoglobulin. The vector has Ig heavy, light and J chain coding “regions” which complicates the extension to the immunoglobulin encoded thereof. Turning to the disclosure, the specification is directed to design of an expression vector encoding at least three elements- a heavy chain, a light chain and a J chain. Example 1 is directed towards construction of IgM or immunoglobulin M using t he vector s shown in Figure s 1 and 2. Figure 1A comprises a mCMV promoter prior to each of the chain coding sequences. However, the LC and HC also comprise an EF-1 a intron. I n figure 1B the same arrangement also has an EF-1 a intron prio r to the JC coding sequence. Figure 2A and 2B represent a two-vector system with HC and LC in one vector and JC in another . In each case, the transcriptional regulatory element is upstream of the coding sequence. Example 2 and 3 demonstrates express ion CD20-IgM from these vectors. The method requires use of CHO cells transfected in vitro with the vectors . Expression on one vector led to higher viable cell densities, restoration of cell viability rates and Ig expression levels respectively in Figure 3-5. Figure 6 shows that the expression of IgM is highest with the single vector. As to effects recited, the teachings are [0123] The results of the high-performance liquid chromatography shown in table 2 are consistent with the PAGE results as shown in FIGS. 6 and 7. It may be achieved that the light and heavy chains are expressed at a higher level of expression than that of J chain by adjusting the relative transcription-initiating capabilities of the promoters for the light, heavy and J chains, when HC, LC, and JC of anti-CD20 are simultaneously expressed in a single expression vector CD20 p3MGT-IgM-1 or CD20 p3MGT-IgM-2. The results wer e found with an additional IgM immunoglobulin. [ 0128] In this Example, the expression vectors of anti-Her2 IgM antibody were constructed. For the single vector expression system, a vector p3MGT-IgM-1 (FIG. 1A) was used. In brief, the mCMV promoter (SEQ ID NO:1) and intron A of EF-1α (SEQ ID NO:5) were operatively linked upstream of the heavy chain (HC, SEQ ID NO: 9) and light chain (LC, SEQ ID NO: 10) coding regions of anti-Her2 IgM. The mCMV promoter (SEQ ID NO:1) was operatively linked upstream of J chain (JC, SEQ ID NO: 11) coding region. The constructed vector was named as Her2 p3MGT-IgM-1. But, the experimental result were limited . Figure 6 and 7 demonstrate that the single vector produced a band representing the full IgM comprising HC, LC and JC. Figure 10 shows the same with antiHer2 IgM. [0144] From FIG. 10, it can be seen that the expression level of IgM is significantly higher in the case that HC, LC, and JC of anti-Her2 are simultaneously expressed in Her2 p3MGT-IgM-1 plasmid, than that in the cells co-transfected with Her2 p2MGT-HC-JC and Her2 pMGT -JC in a ratio of either 5:1 or 4:1. These results do not reflect the totality of the recited claims for two reasons . First, the constructs only show limited promoters wherein when on the same vector mCMV drives HC and LC plus or minus an intron and with JC with mCMV or SV40 promoter . These vectors lead to a “balanced expression ” of HC and LC but that is greater than that of JC to produce IgM (figures 8C and D). Secondly, t hese results do no t demonstrate “ transcription initiating capability”. The parts of transcription initiation are explained by Dudnyk et al (see page 1, col 1), This problem is especially challenging because the transcription initiation process in-volves many factors, and a single base pair may have multiple functions (1–3, 7). Hence, a systematic approach that simultaneously dissects multiple types of sequence patterns, such as TF binding motifs, and their effects on transcription initiation is critical for solving this problem. Applicants results in which protein levels are measured does not provide the kind of information necessary to demonstrate transcription initiation capability. Thirdly, the only arrangement in the disc l o s ure and the only one that makes sense given the results is on in which the transcriptional regulatory element that is operatively associated with the Ig chains is upstream of the coding sequences. If applicants were contemplating 3’ regulatory sequences or otherwise, there is no disclosure of these embodiments that will regulate expression to that required of the claims. Fourth, claims 7 and 8 requires rations of expression that cannot be predicted. For example claim 7 requires expression of HC and LC to be between 4-20 and JC to be between 1-4. Hence, this is on average 4 to 1 levels which are shown in Figure 8 C and D to be possible with the constructs provided. However, this is not the only range wherein it can even be 1:1 or 20:1. However, there are no constructs that show these ratios. Continuing onto claim 8 and 13 , the ration of HC to LC is limited by being in a range of 0.1 to 10 which is not found in the results. The results show about an6:7 and 7.5:14. Hence, it is not clear how to achieve these results that are recited outside of those that are shown with the two constructs provided. As to claims 11-13, the method of making an immunoglobulin requires use of a host cell wherein the host cells for which the only provided for vectors can use are mammalian cells such as those recited in claim 10. Into this the expression vector so provided for in Figure 1 are transfected and the cell cultured and the Ig harvested. However, only an IgM is demonstrated to be so formed from the methods and constructs of the claims . Only IgA and IgM require use of J chain. But, the constraints of the method are determined in terms of IgM formation. Hence, the methods of using as claims in claim 13 and the product by process for making the immunoglobulin in claim 12 are described only in terms of the method of transforming a CHO cells with sequences to produce IgM wherein the ratios as claimed are not attainable except those shown in the disclosure. An adequate written description of the invention defined by the claims requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it; what is required is the knowledge in the prior art and/or a description as to the availability of a representative number of species of claimed nucleic acid sequences. While one of skill in the art can readily envision numerable species of nucleic acid sequences that are obtained by the instant method, the fact remains that the actual nucleic acid sequences which encode a protein with a particular activity cannot be envisioned any better when the possible choices are narrowed from all possible sequences to all possible sequences with an arbitrary structural relationship with a known functional sequence. “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” Ex parte Kubin , 83 USPQ2d 1410, 1417 (Bd. Pat. App. & Int. 2007) citing University of Rochester , 358 F.3d at 927, 69 USPQ2d at 1895. Vas-Cath Inc. v. Mahurkar , 19USPQ2d 1111, clearly states that “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, whatever 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). Rather, the specification is directed to a promoter that is produced by operable linkage of more than one cis-acting element. The court and the Board have repeatedly held (Amgen Inc. v. Chugai Pharmaceutical Co. Ltd.,18 USPQ2d 1016 (CA FC, 1991); Fiers v. Revel, 25 USPQ2d 1601 (CA FC 1993); Fiddes v. Baird, 30 USPQ2d 1481 (BPAI 1993) and Regents of the Univ. Calif. v. Eli Lilly & Co., 43 USPQ2d 1398 (CA FC, 1997)) that an adequate written description of a nucleic acid and methods of using requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it and using it, irrespective of the complexity or simplicity of the method; what is required is a description of the nucleic acid itself. Claiming all DNA’s and effects without defining what means will do so is not in compliance with the description requirement. Rather, it is an attempt to preempt the future before it has arrived. In this case, applicants claim a genus of promoter that are not described in the specification. Claim Rejections - 35 USC § 102 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis ( i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. 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. Claims 1-4 , 6-9 and 11 -13 are rejected under 35 U.S.C. 102(a)( 1 ) as being anticipated by Tchoudakova et al (mAbs, 2009, pages 163-171) as evidenced by Carrara et al ( Antibodies 2021 , pages 1-12) . Tchoudakova et al teach production of IgM from a vector comprising heavy, light and J chain coding sequences that are operably linked to the CMV promoter. Claim 1 is drawn to an expression cassette so arranged but requires that the expression of HC and/or LC is at least the same as that of JC. Given that each of the promoters are the same and as evidenced by Carrara et al would be stoichiometrically the same (see figure 3A). Claim 2 refers to the transcription initiating capability wherein this event would lead to transcription and hence the co-expression indicates that the two are at least equal. As recited in claim 3 and 4, the promoter is CMV and is upstream of the gene. As recited in claim 6, the immunoglobulin produced from the vector is IgM. The ratio of expression using the same promoter CMV has been shown to express different genes in equal measure and hence the level of light and heavy and J would be expected to be 1:1:12 which meets the limitations of Claims 7 and 8. The vector of Tchoudakova et al is PER.C6 (see title) which is used to produce an IgM which was isolated (see bridging ¶, page 168-169). The levels of H:L :J would appear as set forth above to meet the limitations of claim 13. Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. 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. Claims 1-13 are rejected under 35 U.S.C. 103 as being unpatentable over Yamaguchi et al ( Scientific Reports, 2023, pages 1-9 ) in view of Tchoudakova et al (mAbs, 2009, pages 163-171) as evidenced by Carrara et al ( Antibodies 2021 , pages 1-12) and in view of Wang et al ( European J Pharm Sci, 2018, pages 539-545 ). Yamaguchi et al teach use of a three CMV promoter system to express heavy and light chain with an additional gene. The vector is used in CHO cells to produce. One would have for the production of IgM inserted J chain into the third position as taught by Tchoudakova as set forth above . Tchoudakova teaches similar construction for expression of the J linked IgM. As set forth above, the ratio using the same promoter should be 1:1:1. CHO cells are used to produce the Ig (see Figure 3) wherein using the added J chain of Tchoudakova would lead to IgM as recited in claim 6 as well as claims 11-13 . Inclusion of intron A in the CMV construct was shown by Xia et al to improve expression in CHO cells (see page 116, col 1). This meets the limitation of claim s 5, 9, and 10. Based on such teachings, it would have prima facie been obvious to one of ordinary skill in the art at the time the invention was made to incorporate use the overlapping formats of Tchoudakova and Yamaguchi et al which both use 3 copies of CMV to express 3 proteins wherein use of the CHO system of Yamaguchi et al has the benefit, “ Chinese Hamster Ovary (CHO) cells remain the most popular host cell lines for the production of many therapeutic proteins because of their ability to produce recombinant proteins with human-like posttranslational modifications such as glycosylation or phosphorylation, and also to grow at high cell densities in serum-free suspension culture ” (see page 1 , col 1) and the system can be further improved by inclusion of introns as demonstrated by Xia et al . Such a modification would have resulted in the claims of 1-13 . As noted above: 1) Yamaguchi et al teach use of CHO cells for protein production in suspension wherein Yamaguchi uses a 3 promoter system 2) Tchoudakova teaches that such a system can express IgM and 3) Xia et al teach inclusion of introns improves protein production . Thus, a person of ordinary skill in the art, absent evidence to the contrary, would have reasonably expected that the expanded method would allow improved expression systems . Conclusion No claims allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT MARIA MARVICH whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-0774 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT 8 am - 5 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 Maria Leavitt can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT 571-272-1085 . 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. /MARIA MARVICH/ Primary Examiner, Art Unit 1634