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 .
DETAILED ACTION
1. Applicant’s election of Group I (claims 11-16) without traverse in the reply filed on 4/30/26 is acknowledged.
2. Regarding the species election, Applicants elect the following species without traverse.
Among the species of the fully defined sequence of type III human collagen, the part of amino acid sequences of a type III human collagen is elected. Specifically, the amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen is elected, without traverse. (specific sequence by SEQ ID NO: X – is required and none is elected).
Among the species of the fully defined sequence of type I human collagen, the part of amino acid sequences of a type I human collagen is elected, without traverse. Specifically, amino acid sequences at positions 80 to 1,119 of an a2 chain of the type I human collagen. (specific sequence by SEQ ID NO: X – is required and none is elected).
Among the species of secretion tag, mannosidase (SEQ ID No: 11) is elected, without traverse.
Among the species of histidine tag, histidine tag itself is elected, without traverse.
Among the species of fusion tag, green fluorescent protein (GFP) is elected, without traverse.
Among the species of protease cleavage site sequence, the tobacco etch virus cleavage sequence (SEQ ID NO: 19) is elected, without traverse,.
Among the species of the fully defined sequence of gene, the DNA sequence of SEQ ID NO: 24 is elected, without traverse.
Among the species of the cells, the human embryonic kidney cell Expi293F is elected, without traverse.
Among the species of the skin diseases, the skin burns is elected, without traverse.
3. Claims withdrawn:
Claims 17-30 including non-elected species are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention.
4. Priority
Receipt is acknowledged of papers (foreign priority filed 8/9/23) submitted under 35 U.S.C. 119(a)-(d), which papers have been placed of record in the file.
5. A certified translation of every foreign benefit application or Patent Cooperation Treaty (PCT) application not filed in English is required. 35 U.S.C. 119(b)(3) and 372(b)(3) and 37 CFR 1.55(a)(4). If no certified translation is in the official record for the application, the examiner must require the applicant to file a certified translation. The applicant should provide the required translation if applicant wants the application to be accorded benefit of the non-English language application. Any showing of priority that relies on a non-English language application is prima facie insufficient if no certified translation of the application is on file. 37 CFR 41.154(b) and 41.202(e).
6. Drawings
The drawings filed on 11/16/23 are acknowledged.
7. IDS filed 2/28/24 is acknowledged. A signed copy of the IDS is provided with this Office Action.
8. Specification
The specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant's cooperation is requested in correcting any errors of which applicant may become aware in the specification.
9. 35 U.S.C. § 112, first paragraph (Written Description)
Claims 11-16 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.
The claimed invention is directed to the following genus claims.
11. A recombinant collagen, comprising all or a part of amino acid sequences of a type III human collagen and all or a part of amino acid sequences of a type I human collagen.
12. The recombinant collagen according to claim 11, wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen; and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen.
13. The recombinant collagen according to claim 11, further comprising a secretion tag, a histidine tag, a fusion tag, and a protease cleavage site sequence.
14. The recombinant collagen according to claim 13, wherein the secretion tag is selected from the group consisting of trypsin, human interleukin 2, serum albumin, disulfide-bond formation protein A, pectate lyase B, outer membrane protein A, maltose-binding protein, murein lipoprotein, trimethylamine N-oxide reductase, mannosidase, human insulin, and a hybrid secretion tag: the fusion tag is selected from the group consisting of maltose-binding protein (MBP), cysteine protease, glutathione S-transferase, apolipoprotein A1, thioredoxin, green fluorescent protein, and a hybrid fusion tag; and the protease cleavage site sequence is selected from the group consisting of a tobacco etch virus cleavage sequence, a thrombin cleavage sequence, an enterokinase cleavage sequence, a factor Xa cleavage sequence, a rhinovirus 3C cleavage sequence, and a hybridase cleavage site sequence.
15. The recombinant collagen according to claim 13, wherein the recombinant collagen comprises an amino acid sequence shown in SEQ ID NO: 1.
16. The recombinant collagen according to claim 14, wherein the recombinant collagen comprises an amino acid sequence shown in SEQ ID NO: 1.
The claims are described by functional limitations only (see for example claims 11-14) and are devoid of a reference structure for the claimed recombinant collagen comprising all or a part of amino acid sequences of a type III human collagen and all or a part of amino acid sequences of a type I human collagen (note that claims 15 & 16 does not rectify this deficiency) because of the reference to “an amino acid sequence shown in SEQ ID NO: 1), which may be the fragment of SEQ ID NO: 1 (1043 amino acids in length), wherein the fragment could be of any length. The claimed invention encompasses a genus of type III human collagen or type I human collagen of any length with no corresponding SEQ ID NO:? to relate to, and therefore not adequately described.
The claims further remain undescribed for introducing language “wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen; and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen”. No description is evident from the instant specification – that wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221, as no or which part of amino acid sequences of the type III human collagen/type I human collagen comprises additional amino acid sequences. Further as per the instant specification SEQ ID NO: 1 (1043 aa in length) appears to be the amino acid sequence of type III human collagen.
The MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed by him. The courts have stated:
"To fulfill the written description requirement, a patent specification must describe aninvention and do so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997); In re Gostelli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) ("[T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what isclaimed."). Thus, an applicant complies with the written description requirement "bydescribing the invention, with all its claimed limitations, not that which makes it obvious,"and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d at 1966."Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
Further, for a broad generic claim, the specification must provide adequate written description to identify the genus of the claim. In Regents" of the University of California v. Eli Lilly & Co. the court stated:
"A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) ("In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus ...") Regents" of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The MPEP further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the sequence, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence." MPEP § 2163. The MPEP does state that for a generic claim the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. MPEP § 2163. If the genus has a substantial variance, the disclosure must describe a sufficient variety of species to reflect the variation within that genus. See MPEP § 2163. Although the MPEP does not define what constitute a sufficient number of representative species, the courts have indicated what do not constitute a representative number of species to adequately describe a broad generic. In Gostelli, the courts determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus. In re Gostelli, 872, F.2d at 1012, 10 USPQ2d at 1618. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the Application. These include "level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient." MPEP § 2163. While all of the factors have been considered, a sufficient amount for a prima facie case is discussed below.
Further, to provide evidence of possession of a claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include: a) the scope of the invention; b) actual reduction to practice; c) disclosure of drawings or structural chemical formulas; d) relevant identifying characteristics including complete structure, partial structure, physical and/or chemical properties, and structure/function correlation; e) method of making the claimed compounds; f) level of skill and knowledge in the art; and g) predictability in the art.
Moreover, Vas-Cath Inc. v. Mahurkar, 935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Fed. Cir.1991), 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). The skilled artisan cannot envision the detailed chemical structure of the encompassed genus of polypeptides, 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).
Therefore, for all these reasons the specification lacks adequate written description, and one of skill in the art cannot reasonably conclude that the applicant had possession of the claimed invention at the time the instant application was filed.
10. Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 11, 13, 15 & 16 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a natural phenomenon) without significantly more. An analysis with respect to the claims as a whole reveals that they do not include additional elements that are sufficient to amount to significantly more than the judicial exception. See Alice Corp. Pty. Ltd. v. CLS Bank Int’l, 134 S. Ct. 2347, 110 U.S.P.Q.2d 1976 (2014); Ass’n for Molecular Pathology v. Myriad Genetics, Inc., 133 S. Ct. 2107, 2116, 106 U.S.P.Q.2d 1972 (2013); Mayo Collaborative Svcs. v. Prometheus Laboratories, Inc., 132 S. Ct. 1289, 101 U.S.P.Q.2d 1961 (2012). See also 2014 Interim Guidance on Patent Subject Matter Eligibility, available at http://www.gpo.gov/fdsys/pkg/FR-2014-12-16/pdf/2014-29414.pdf (“2014 Interim Guidance”), and the Office’s examples to be considered in conjunction with the 2014 Interim Guidance in examination of nature-based products, available online at http://www.uspto.gov/patents/law/exam/mdc_examples_nature-based_products.pdf (“Nature-Based Products Examples”) and updated guidance of 2015 https://www.uspto.gov/sites/default/files/documents/ieg-july-2015-update.pdf.
The relevant distinction is the one “between patents that claim the ‘buildin[g] block[s]’ of human ingenuity and those that integrate the building blocks into something more, thereby ‘transform[ing]’ them into a patent-eligible invention. The former ‘would risk disproportionately tying up the use of the underlying’ ideas and are therefore ineligible for patent protection. The latter pose no comparable risk of pre-emption, and therefore remain eligible for the monopoly granted under our patent laws.” See Alice Corp., 110 U.S.P.Q.2d at 1981 (quoting Mayo, 101 U.S.P.Q.2d at 1972, 1965-66).
Analysis of subject-matter eligibility under 35 U.S.C. § 101 requires consideration of three issues: (1) whether the claim is directed to one of the four categories recited in §101; (2A) whether the claim recites or involves a judicial exception (i.e., a law of nature, natural phenomenon, or natural product); and (2B) whether the claim as a whole recites something that amounts to significantly more than the judicial exception.
Question 1: Yes; the claims are directed to a composition of matter.
Question 2A: Yes; the claims are drawn to a product that does not differ from those that exist in nature, e.g. a natural product (all or part) of Type I or II human collagen.
The only requirement in the claims is, for example, is the term ‘recombinant’ which does not distinguishes from ‘naturally occurring’ as no mention of “genetically modified host cell” comprising a DNA encoding Type I or II human collagen is evident.
Recombinant collagen is produced by inserting human or optimized collagen genes into host organisms such as bacteria, yeast, mammalian cells, or plants, which then express the protein during growth. This process ensures that the collagen is structurally identical to natural human collagen, eliminating risks of immune reactions, viral contamination, or batch variability associated with animal-derived sources.
Question 2B: No; while the claims state “recombinant”, there is nothing in the claims which differentiates, for example, naturally occurring Type I or II human collagen from a modified host cell as no specific genetic modification is evident. There is nothing in terms of structure and/or function in the limitations which gives rise a significant or marked difference because as noted above.
11. 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 12, 15 & 16 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 pre-AIA the applicant regards as the invention.
Claim 12 recite –The recombinant collagen according to claim 11, wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen; and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen.
The claim (a) amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 is unclear regarding which of the amino acid sequences are being referred to at the positions indicated as no reference sequence(s) are present in the claim and further are these amino acid sequences inserted at the positions 847 to 849 or at positions 154 to 1,221 – which makes the claim further unclear and indefinite.
Similarly – claim 12 – recites “and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen” - is unclear regarding which of the amino acid sequences are being referred to at the positions indicated as no reference sequence(s) are present in the claim.
Further as per the instant specification SEQ ID NO: 1 (1043 aa in length) appears to be the amino acid sequence of type III human collagen. In this regard it is not clear where and how - amino acid sequences are inserted at positions 154 to 1,221.
Claims 15 & 16 – refer to ‘an amino acid sequence of SEQ ID NO: 1’. The claims are indefinite because ‘an amino acid sequence of SEQ ID NO: 1’ could be interpreted as a fragment of SEQ ID NO: 1 of any length.
12. 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.
Claim(s) 11, 15 & 16 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by CN110003324-A (See AC BGO73979). Claims 11, 15 & 16 are broadly drawn to recombinant collagen, comprising all or a part of amino acid sequences of a type III human collagen and all or a part of amino acid sequences of a type I human collagen, or wherein the recombinant collagen comprises an amino acid sequence shown in SEQ ID NO: 1. As noted above in various rejections the phrases “and all or a part” or “an amino acid sequence of SEQ ID NO: 1” is interpreted to read on the recombinant human collagen of CN110003324-A. See the sequence alignment of Applicants’ SEQ ID NO: 1 and CN110003324-A (See AC BGO73979) – presented below.
RESULT 2
BGO73979
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID BGO73979 standard; protein; 1056 AA.
XX
AC BGO73979;
XX
DT 19-SEP-2019 (first entry)
XX
DE Human type I collagen alpha 2 chain (FLAG/His tag), SEQ ID 1.
XX
KW COL1A2 protein; Collagen I alpha 2; cosmetics; dermatological;
KW recombinant protein.
XX
OS Homo sapiens.
OS Synthetic.
XX
CC PN CN110003324-A.
XX
CC PD 12-JUL-2019.
XX
CC PF 20-MAY-2019; 2019CN-10420372.
XX
PR 19-MAR-2019; 2019CN-10206499.
XX
CC PA (JIAN-) JIANGSU YUEZHI BIOLOGICAL PHARM CO LTD.
XX
CC PI Liang L, Chang Y;
XX
DR WPI; 2019-632192/68.
DR N-PSDB; BGO73987.
XX
CC PT New recombinant human collagen useful in external skin-care products and
CC PT lead-in skin-care products, and for preparing collagen gel dressing, raw
CC PT protein dressing and collagen-based skin mucosal protectant dressing.
XX
CC PS Claim 1; SEQ ID NO 1; 24pp; Chinese.
XX
CC The present invention relates to a novel recombinant human collagen
CC having an amino acid sequence of SEQ ID NO: 1 (see BGO73979). The
CC recombinant collage comprises an amino-terminal affinity purification tag
CC (FLAG tag), a human type I collagen alpha 2 chain mature peptide and a
CC carboxy-terminal affinity purification tag (6His tag). The recombinant
CC human collagen is useful in cosmetics for preparing a skin care product
CC and a collagen gel dressing.
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692
563
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13. Double Patenting Rejection
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 claims at issue 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); and 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 a nonstatutory double patenting ground provided the reference application or patent either is shown to be commonly owned with this 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 §§ 706.02(l)(1) - 706.02(l)(3) 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).
Effective January 1, 1994, a registered attorney or agent of record may sign a terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply with 37 CFR 3.73(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/forms/. The 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 http://www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 11-16 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2 of U.S. Patent No. US 12570723 B2. Although the claims at issue are not identical, they are not patentably distinct from each other because of the following reason(s).
Instant claims 11-16 are drawn to as follows:
11. A recombinant collagen, comprising all or a part of amino acid sequences of a type III human collagen and all or a part of amino acid sequences of a type I human collagen.
12. The recombinant collagen according to claim 11, wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen; and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen.
13. The recombinant collagen according to claim 11, further comprising a secretion tag, a histidine tag, a fusion tag, and a protease cleavage site sequence.
14. The recombinant collagen according to claim 13, wherein the secretion tag is selected from the group consisting of trypsin, human interleukin 2, serum albumin, disulfide-bond formation protein A, pectate lyase B, outer membrane protein A, maltose-binding protein, murein lipoprotein, trimethylamine N-oxide reductase, mannosidase, human insulin, and a hybrid secretion tag: the fusion tag is selected from the group consisting of maltose-binding protein (MBP), cysteine protease, glutathione S-transferase, apolipoprotein A1, thioredoxin, green fluorescent protein, and a hybrid fusion tag; and the protease cleavage site sequence is selected from the group consisting of a tobacco etch virus cleavage sequence, a thrombin cleavage sequence, an enterokinase cleavage sequence, a factor Xa cleavage sequence, a rhinovirus 3C cleavage sequence, and a hybridase cleavage site sequence.
15. The recombinant collagen according to claim 13, wherein the recombinant collagen comprises an amino acid sequence shown in SEQ ID NO: 1.
16. The recombinant collagen according to claim 14, wherein the recombinant collagen comprises an amino acid sequence shown in SEQ ID NO: 1.
The claims are described by functional limitations only (see for example claims 11-14) and are devoid of a reference structure for the claimed recombinant collagen comprising all or a part of amino acid sequences of a type III human collagen and all or a part of amino acid sequences of a type I human collagen (note that claims 15 & 16 does not rectify this deficiency) because of the reference to “an amino acid sequence shown in SEQ ID NO: 1), which may be the fragment of SEQ ID NO: 1 (1043 amino acids in length), wherein the fragment could be of any length. The claimed invention encompasses a genus of type III human collagen or type I human collagen of any length with no corresponding SEQ ID NO:? to relate to, and therefore not adequately described.
The claims further remain undescribed for introducing language “wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221 of the type III human collagen; and the part of amino acid sequences of the type I human collagen comprises amino acid sequences at positions 80 to 1,119 of an α2 chain of the type I human collagen”. No description is evident from the instant specification – that wherein the part of amino acid sequences of the type III human collagen comprises amino acid sequences at positions 847 to 849 or at positions 154 to 1,221, as no or which part of amino acid sequences of the type III human collagen/type I human collagen comprises additional amino acid sequences. Further as per the instant specification SEQ ID NO: 1 (1043 aa in length) appears to be the amino acid sequence of type III human collagen.
Patented claims 1 & 2 are drawn to as follows:
1. A recombinant humanized collagen type III alpha-1 (rhCol III α1) fusion protein consisting of SEQ ID NO: 3 for use in a skin care product, the rhCol III α1 fusion protein being encoded by a fused nucleotide sequence, and wherein the fused nucleotide sequence comprises sequentially a gene sequence for encoding a secretion signal peptide, a gene sequence for encoding a 8× histidine tag, a gene sequence for encoding a green fluorescent protein (GFP), a DNA sequence for encoding a digestion sequence of a tobacco etch virus (TEV) protease, and a gene sequence for encoding rhCol III α1; wherein the rhCol III α1 fusion protein has the amino acid sequence consisting of SEQ ID NO: 3; and wherein the gene sequence for encoding rhCol III α1 has the sequence consisting of SEQ ID NO: 1.
2. A product for skin repair, comprising the rhCol III α1 fusion protein according to claim 1 in the product for skin repair.
Given the fact pattern of the instant case as well as the patent the species claims of the patent anticipates the instant genus (or broad) claims and further explained above in various rejections – particularly under 112 1st & 112 2nd , or are an obvious variation thereof.
14. No claim is allowed.
15. Any inquiry concerning this communication or earlier communications from the examiner should be directed to TEKCHAND SAIDHA whose telephone number is (571)272-0940. The examiner can normally be reached on M-F 8.00-5.30. 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, Robert B Mondesi can be reached on 408 918 7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940
Prosecution Insights