DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. 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 cited rejections 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.
3. Response to Election/Restriction filed on 6/1/2026 is acknowledged.
4. Claim filed on 6/1/2026 is acknowledged.
5. Claims 1-25 have been cancelled.
6. Claims 26-45 are pending in this application.
7. Claims 43-45 are withdrawn from consideration pursuant to 37 CFR 1.142(b), as being drawn to non-elected inventions, there being no allowable generic or linking claim. Claim 39 is withdrawn from consideration as being drawn to non-elected species.
8. Claims 26-38 and 40-42 are under examination.
Election/Restrictions
9. Applicant’s election of Group 1 (claims 26-42) and election of a recombinant human type 21 alpha 1 collagen polypeptide consisting of SEQ ID NO: 76 as species of recombinant human type 21 alpha 1 collagen polypeptide; E.coli. as species of host; a fusion protein consisting of a recombinant human type 21 alpha 1 collagen polypeptide of SEQ ID NO: 76 conjugated to the secretion tag dsbA as species of fusion protein; and a composition comprising a recombinant human type 21 alpha 1 collagen polypeptide of SEQ ID NO: 76 and a topical carrier as species of composition in the reply filed on 6/1/2026 is acknowledged. Since the elected species of fusion protein is a subgenus, not a species; the Examiner telephoned Applicant’s representative, Rikki A. Hullinger, for further species election. Applicant’s representative stated on the phone a fusion protein consisting of SEQ ID NO: 74 as the elected species of fusion protein on 6/5/2026. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). The requirement is made FINAL in this office action.
Group 1 is drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; a fusion protein comprising such recombinant polypeptide and a secretion tag; and a composition comprising from about 0.005% to about 30% w/w of such recombinant polypeptide. A search was conducted on the elected species; a recombinant human type 21 alpha 1 collagen polypeptide consisting of SEQ ID NO: 76 as the elected species of recombinant human type 21 alpha 1 collagen polypeptide, a fusion protein consisting of SEQ ID NO: 74 as the elected species of fusion protein, and a composition comprising a recombinant human type 21 alpha 1 collagen polypeptide of SEQ ID NO: 76 and a topical carrier as the elected species of composition appear to be free of prior art. However, prior art was found for E.coli. as the elected species of host. A search was extended to the genus in claims 26, 36 and 40; and prior art was found. Claim 39 is withdrawn from consideration as being drawn to non-elected species. Claims 26-38 and 40-42 are examined on the merits in this office action.
Effective Filing Date of Instant Claims 27, 28, 34 and 35
10. In view of the rejection set forth in Section 18 below, the effective filing date of instant claims 27, 28, 34 and 35 is the filing date of instant application, which is 6/21/2024.
Claim Interpretation
11. With regards to the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claims 26-28, in view of the disclosure of instant specification and in the broadest reasonable interpretation, the Examiner is interpretating the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claims 26-28 can have additional truncations of the full length human type 21 alpha 1 collagen polypeptide. Therefore, any peptide/protein comprising a dipeptide sequence of the full length human type 21 alpha 1 collagen and comprising no more than one GPP triplet sequence meets the limitations of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claims 26-28. Such interpretation applies to all rejections set forth below.
Specification
12. Please note: The specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification (see MPEP § 608.01).
Objections
13. Claims 34 and 35 are objected to for the following minor informality: Applicant is suggested to amend claims 34 and 35 as “…wherein the recombinant polypeptide comprises the amino acid sequence that is at least…% identical to the amino acid sequence of SEQ ID NO: 76”.
14. Claims 37 and 38 are objected to for the following minor informality: Applicant is suggested to amend claims 37 and 38 as “…wherein the secretion tag is…”.
Furthermore, claim 37 contains various acronyms, such as “DsbA” and many others. An acronym in the first instance of claims should be expanded upon/spelled out with the acronym indicated in parentheses, for example, thiol:disulfide interchange protein (DsbA). The abbreviations can be used thereafter.
15. Claim 40 is objected to for the following minor informality: Applicant is suggested to amend claim 40 as “A composition comprising from about 0.005% w/w to about 30% w/w of the recombinant polypeptide of claim 26”.
16. Claim 42 is objected to for the following minor informality: Applicant is suggested to amend claim 42 as “…wherein the composition further comprises…”.
Rejections
Claim Rejections - 35 U.S.C. § 112 paragraph (a)
Written Description
17. The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
18. Applicant is required to cancel the new matter in the reply to this Office Action.
Claims 27, 28, 34 and 35 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 claims contain 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, at the time the application was filed, had possession of the claimed invention.
The MPEP states that “The introduction of claim changes which involve narrowing the claims by introducing elements or limitations which are not supported by the as-filed disclosure is a violation of the written description requirement of 35 U.S.C. 112, first paragraph. See, e.g., Fujikawa v. Wattanasin, 93 F.3d 1559, 1571, 39 USPQ2d 1895, 1905 (Fed. Cir. 1996) (a “laundry list” disclosure of every possible moiety does not constitute a written description of every species in a genus because it would not “reasonably lead” those skilled in the art to any particular species); In re Ruschig, 379 F.2d 990, 995, 154 USPQ 118, 123 (CCPA 1967) (“If n-propylamine had been used in making the compound instead of n-butylamine, the compound of claim 13 would have resulted. Appellants submit to us, as they did to the board, an imaginary specific example patterned on specific example 6 by which the above butyl compound is made so that we can see what a simple change would have resulted in a specific supporting disclosure being present in the present specification. The trouble is that there is no such disclosure, easy though it is to imagine it.”) (emphasis in original). In Ex parte Ohshiro, 14 USPQ2d 1750 (Bd. Pat. App. & Inter. 1989), the Board affirmed the rejection under 35 U.S.C. 112, first paragraph, of claims to an internal combustion engine which recited “at least one of said piston and said cylinder (head) having a recessed channel.” The Board held that the application which disclosed a cylinder head with a recessed channel and a piston without a recessed channel did not specifically disclose the “species” of a channeled piston.” (see MPEP § 2163).
In the instant case, claim 27 recites “The recombinant polypeptide of claim 26, wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen”; claim 28 recites “The recombinant polypeptide of claim 26, wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen”; claim 34 recites “The recombinant polypeptide of claim 26, wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76”; and claim 35 recited “The recombinant polypeptide of claim 26, wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76”.
With regards to the recited limitations “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76” and “wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76”, such limitations have never been explicitly disclosed and/or discussed in the instant specification. The detailed explanations are as followings:
Lack of Ipsis Verbis Support
The specification is void of any literal support for the limitations “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76” and “wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76” recited in instant claims 27, 28, 34 and 35. Therefore, the instant specification fails to provide literal support to such limitation.
Lack of Implicit or Inherent Support
“While there is not in haec verba requirement, newly added claim limitations must be supported in the specification through express, implicit, or inherent disclosure.” See MPEP § 2163. Thus support can be furnished implicitly or inherently for a specifically claimed limitation.
In the instant case, the instant specification discloses peptide of SEQ ID NO: 76 as example of instant claimed recombinant human type 21 alpha 1 collagen polypeptide; and peptide of SEQ ID NO: 74 as an example of a fusion protein consisting of instant SEQ ID NO: 76 conjugated to a DsbA tag. However, the peptide of instant SEQ ID NO: 76 consists of amino acids 50-236 of the isoform CRA_e of human type 21 alpha 1 collagen, amino acids 82-268 of human type 21 alpha 1 collagen, or amino acids 556-742 of the isoform b precursor of human type 21 alpha 1 collagen. Furthermore, the instant specification fails to disclose any percentage of sequence identity. Therefore, it is determined that the instant specification fails to provide any implicit or inherent support to the limitations “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76” and “wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76” recited in instant claims 27, 28, 34 and 35.
Taken all these together, the instant specification fails to provide any types of support to the limitations “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen”, “wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76” and “wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76” recited in instant claims 27, 28, 34 and 35.
Claim Rejections - 35 U.S.C. § 101
19. 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.
20. Claims 26-32, 34, 35 and 40-42 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon without significantly more. Claims 26-32, 34, 35 and 40-42 recite a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; and a composition comprising from about 0.005% to about 30% w/w of such recombinant polypeptide. This judicial exception is not integrated into a practical application because claims 26-32, 34, 35 and 40-42 are directed to fragment of naturally occurring protein and a composition comprising multiple natural products.
As disclosed in instant claims and instant specification, the instant claimed recombinant human type 21 alpha 1 collagen polypeptide is truncated human type 21 alpha 1 collagen. In the broadest reasonable interpretation, water is a topical carrier recited in instant claim 42; and a composition comprising instant claimed polypeptide and water is a composition formulated for topical application. And as evidenced by the Water document (from http://www.biology-online.org/dictionary/Water, 2014, enclosed pages 1-3), water is a natural product.
The instant claims 26-32, 34, 35 and 40-42 do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the recombinant human type 21 alpha 1 collagen polypeptide and a composition comprising such recombinant polypeptide in instant claims 26-32, 34, 35 and 40-42 do not recite features or steps demonstrating a marked difference from what exists in nature; and the recombinant human type 21 alpha 1 collagen polypeptide and a composition comprising such recombinant polypeptide in instant claims 26-32, 34, 35 and 40-42 do not recite meaningful limitations that add something of significance to the judicial exception. Therefore, the recombinant human type 21 alpha 1 collagen polypeptide and a composition comprising such recombinant polypeptide in instant claims 26-32, 34, 35 and 40-42 are not significantly different than a judicial exception (natural product).
Claim Rejections - 35 U.S.C. § 102(a)(1)
21. 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.
22. Claims 26-33 and 40-42 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hayashida et al (US 2014/0309401 A1).
The instant claims 26-33 and 40-42 are drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; and a composition comprising from about 0.005% to about 30% w/w of such recombinant polypeptide.
Hayashida et al teach peptides with the amino acid sequences Gly-Pro-Ala-Gly, Gly-Pro-Ala-Gly-Pro, Gly-Pro-Ala-Gly-Pro-Arg, Gly-Pro-Ala-Gly-Pro-Ile, Gly-Pro-Leu-Gly-Pro-Val, Gly-Pro-Ile-Gly-Pro-Val, Gly-Pro-Val, Gly-Pro-Gln, Gly-Pro-Glu, Gly-Ala, Gly-Ala-Ile-Gly-Pro-Ala, Gly-Ala-Ile-Gly-Pro-Ser, Gly-Ala-Val-Gly-Pro-Ala, Gly-Ala-Val-Gly-Pro, Leu-Pro, Leu-Pro-Gly, Leu-Pro-Gly-Pro-Ala, and Ala-Pro-Gly, for example, page 3, paragraph [0035]. These peptides in Hayashida et al comprise the amino acid sequence of a human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and no more than one GPP triplet sequence. It meets the limitations of the recombinant polypeptide recited in instant claims 26-28, 32 and 40. Hayashida et al further teach a composition comprising 1 mg of such peptide in 1 ml 50 mM tris-hydrochloric acid buffer (pH 7.5) (the concentration of the peptides equals to about 0.1% w/w), for example, page 5, paragraph [0076]. It meets the limitations of the composition recited in instant claim 40. And in the broadest reasonable interpretation, such composition in Hayashida et al is a composition formulated for topical application and comprising a topical carrier. It meets the limitations of instant claims 41 and 42.
Claims 29-31 are product by process claims for obtaining the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. And the MPEP states the following: "[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)…" (see MPEP § 2113 I). Therefore, the peptides in Hayashida et al meet the limitations of instant claims 29-31; and it reads on E.coli. as the elected species of host.
With regards to the limitation recited in instant claim 33, since the peptides in Hayashida et al meet all the structural limitations of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26, the peptides in Hayashida et al would necessarily have the same properties and/or functionalities of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. Therefore, the peptides in Hayashida et al are monomeric and do not form a stable triple helix structure formed by natural collagen at 37 oC. It meets the limitation of instant claim 33. Furthermore, the MPEP states “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Therefore, the prima facie case can be rebutted by evidence showing that the prior art products do not necessarily possess the characteristics of the claimed product. In re Best, 562 F.2d at 1255, 195 USPQ at 433. See also Titanium Metals Corp. v. Banner, 778 F.2d 775, 227 USPQ 773 (Fed. Cir. 1985) (Claims were directed to a titanium alloy containing 0.2-0.4% Mo and 0.6-0.9% Ni having corrosion resistance. A Russian article disclosed a titanium alloy containing 0.25% Mo and 0.75% Ni but was silent as to corrosion resistance. The Federal Circuit held that the claim was anticipated because the percentages of Mo and Ni were squarely within the claimed ranges. The court went on to say that it was immaterial what properties the alloys had or who discovered the properties because the composition is the same and thus must necessarily exhibit the properties.).” (see MPEP § 2112.01 I). In addition, since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
Since the reference teaches all the limitations of instant claims 26-33 and 40-42; the reference anticipates instant claims 26-33 and 40-42.
23. Claims 27, 28, 34 and 35 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Brightman et al (US 2022/0257492 A1).
The instant claims 27, 28, 34 and 35 are drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 85 amino acids relative to full-length human type 21 alpha 1 collagen, or wherein the recombinant polypeptide comprises an N-terminal truncation that is between 1 and 212 amino acids relative to full-length human type 21 alpha 1 collagen, or wherein the recombinant polypeptide comprises at least 95% amino acid sequence identity to full length SEQ ID NO: 76 or wherein the recombinant polypeptide comprises at least 98% amino acid sequence identity to full length SEQ ID NO: 76.
Brightman et al teach a recombinant polypeptide of SEQ ID NO: 16 (identical to the polypeptide of instant SEQ ID NO: 76), for example, pages 41-42, SEQ ID NO: 16. It meets the limitations of instant claims 27, 28, 34 and 35.
Since the reference teaches all the limitations of instant claims 27, 28, 34 and 35; the reference anticipates instant claims 27, 28, 34 and 35.
24. Claims 26-33 and 36-38 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Hatayama et al (JP 2011097898 A, machine translation used and enclosed pages 1-32), and as evidenced by the Sequence listing of JP 2011097898 A document (2011, enclosed pages 1-22).
The instant claims 26-33 and 36-38 are drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; and a fusion protein comprising such recombinant polypeptide and a secretion tag.
Hatayama et al, throughout the patent, teach a recombinant FcγRI extracellular region consisting of the amino acids 1-277 of SEQ ID NO: 2, wherein the recombinant FcγRI extracellular region is produced in E.coli.; and a fusion protein comprising such recombinant FcγRI extracellular region and a secretion tag such as DsbA, for example, page 2, Overview; page 3, claims 1 and 2; page 6, paragraph [0010] to page 7, paragraph [0019]; page 7, paragraph [0022] to page 8, paragraph [0024]; and page 22, Table 1. And as evidenced by the Sequence listing of JP 2011097898 A document, the recombinant FcγRI extracellular region consisting of the amino acids 1-277 of SEQ ID NO: 2 in Hatayama et al comprises a recombinant human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and having no more than one GPP triplet sequence. It reads on E.coli. as the elected species of host; and meets the limitations of instant claims 26-32. And the fusion proteins comprising such recombinant FcγRI extracellular region in Hatayama et al meet the limitations of instant claims 36-38.
With regards to the limitation recited in instant claim 33, since the recombinant FcγRI extracellular region consisting of the amino acids 1-277 of SEQ ID NO: 2 in Hatayama et al meets all the structural limitations of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26, the recombinant FcγRI extracellular region consisting of the amino acids 1-277 of SEQ ID NO: 2 in Hatayama et al would necessarily have the same properties and/or functionality of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. Therefore, the recombinant FcγRI extracellular region consisting of the amino acids 1-277 of SEQ ID NO: 2 in Hatayama et al is monomeric and does not form a stable triple helix structure formed by natural collagen at 37 oC. It meets the limitation of instant claim 33. Furthermore, the MPEP states “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Therefore, the prima facie case can be rebutted by evidence showing that the prior art products do not necessarily possess the characteristics of the claimed product. In re Best, 562 F.2d at 1255, 195 USPQ at 433. See also Titanium Metals Corp. v. Banner, 778 F.2d 775, 227 USPQ 773 (Fed. Cir. 1985) (Claims were directed to a titanium alloy containing 0.2-0.4% Mo and 0.6-0.9% Ni having corrosion resistance. A Russian article disclosed a titanium alloy containing 0.25% Mo and 0.75% Ni but was silent as to corrosion resistance. The Federal Circuit held that the claim was anticipated because the percentages of Mo and Ni were squarely within the claimed ranges. The court went on to say that it was immaterial what properties the alloys had or who discovered the properties because the composition is the same and thus must necessarily exhibit the properties.).” (see MPEP § 2112.01 I). In addition, since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
Since the reference teaches all the limitations of instant claims 26-33 and 36-38, the reference anticipates instant claims 26-33 and 36-38.
Obviousness Double Patenting
25. 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. A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO internet Web site contains terminal disclaimer forms which may be used. Please visit http://www.uspto.gov/forms/. The filing date of the application will determine what form 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.
26. Claims 26-38 and 40-42 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-19 of US patent 11214609 B2.
27. Instant claims 26-38 and 40-42 are drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; a fusion protein comprising such recombinant polypeptide and a secretion tag; and a composition comprising from about 0.005% to about 30% w/w of such recombinant polypeptide.
28. Claims 1-19 of US patent 11214609 B2 are drawn to a recombinant polypeptide produced in a microbial host cell, the recombinant polypeptide comprising the amino acid sequence of full-length human type 21 alpha 1 collagen having a truncation of at least 530 amino acids, wherein the recombinant polypeptide comprises the amino acid
sequence according to SEQ ID NO: 76, and wherein the recombinant polypeptide is monomeric and does not form a stable triple helix structure of natural collagen; a composition comprising from 0.005% w/w to 30% w/w of such recombinant polypeptide; and a method of treating the skin of a subject, the method comprising administering to the skin of a subject a composition of claim 11, thereby treating the skin of the subject.
The peptide of SEQ ID NO: 76 recited in claims of US patent 11214609 B2 is identical to the recombinant polypeptide of instant SEQ ID NO: 76.
29. For the same/similar reasoning/rational as the rejection set forth in Sections 26-28 above, instant claims 26-36 and 40-42 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 49-56, 58-62 and 64-75 of co-pending Application No. 17/491228 (issue fee paid on 7/14/2026).
The non-naturally occurring polypeptide of SEQ ID NO: 16 recited in claim 49 of co-pending Application No. 17/491228 is identical to the recombinant polypeptide of instant SEQ ID NO: 76.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
30. For the same/similar reasoning/rational as the rejection set forth in Sections 26-28 above, instant claims 26-35 and 40-42 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1, 11, 13, 32, 34, 38, 40, 48 and 57-59 of co-pending Application No. 18/191556.
The non-naturally occurring polypeptide of SEQ ID NO: 16 recited in claims 11 and 13 of co-pending Application No. 18/191556 is identical to the recombinant polypeptide of instant SEQ ID NO: 76.
Furthermore, claims 29-31 are product by process claims for obtaining the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. And the MPEP states the following: "[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)…" (see MPEP § 2113 I). Therefore, the non-naturally occurring polypeptide of SEQ ID NO: 16 recited in claims 11 and 13 of co-pending Application No. 18/191556 meets the limitations of instant claims 29-31.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
31. For the same/similar reasoning/rational as the rejection set forth in Sections 26-28 and 30 above, instant claims 26-35 and 40-42 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1 and 25-49 of co-pending Application No. 19/579711.
The peptide of SEQ ID NO: 24 recited in claim 25 of co-pending Application No. 19/579711 is identical to the peptide of instant SEQ ID NO: 76. Furthermore, the peptide of any one of SEQ ID NO: 63-66 and many others recited in claim 27 of co-pending Application No. 19/579711 comprises the amino acid sequence of a human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and no more than one GPP triplet sequence.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
32. Claims 26-33 and 40-42 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-22 of US patent 11168126 B2.
33. Instant claims 26-33 and 40-42 are drawn to a recombinant human type 21 alpha 1 collagen polypeptide comprising: an N-terminal and/or a C-terminal truncation; and no more than one glycine-proline-proline triplet sequence; and a composition comprising from about 0.005% to about 30% w/w of such recombinant polypeptide.
34. Claims 1-22 of US patent 11168126 B2 are drawn to a non-naturally occurring polypeptide produced in a microbial host cell, wherein the non-naturally occurring polypeptide consists of the amino acid sequence having at least 80% sequence identity to the amino acid sequence according to SEQ ID NO: 19, or a truncate thereof that is at least 100 amino acids in length, and wherein the non-naturally occurring polypeptide is monomeric and lacks a cross-linked structure of natural elastin; a composition comprising from 0.001 % to 30% w/w of such non-naturally occurring polypeptide; and a method for improving the appearance of skin, the method comprising applying the composition of claim 12 to the skin of a subject, thereby improving the appearance of
the skin.
The peptide of SEQ ID NO: 19 recited in claims of US patent 11168126 B2 comprises the amino acid sequence of a human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and no more than one GPP triplet sequence.
35. For the same/similar reasoning/rational as the rejection set forth in Sections 32-34 above, instant claims 26-33 and 40-42 are rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-29 of US patent 12269865 B.
36. For the same/similar reasoning/rational as the rejection set forth in Sections 32-34 above, instant claims 26-33 and 40-42 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 42 and 49-60 of co-pending Application No. 17/714896 (notice of allowance mailed on 7/2/2026).
The peptide of SEQ ID NO: 2 recited in claims 49-51 of co-pending Application No. 17/714896 comprises the amino acid sequence of a human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and no more than one GPP triplet sequence.
Claims 29-31 are product by process claims for obtaining the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. And the MPEP states the following: "[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)…" (see MPEP § 2113 I). Therefore, the peptide of SEQ ID NO: 2 recited in claims 49-51 of co-pending Application No. 17/714896 meets the limitations of instant claims 29-31.
With regards to the limitation recited in instant claim 33, since the peptide of SEQ ID NO: 2 recited in claims 49-51 of co-pending Application No. 17/714896 meets all the structural limitations of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26, the peptide of SEQ ID NO: 2 recited in claims 49-51 of co-pending Application No. 17/714896 would necessarily have the same properties and/or functionality of the recombinant human type 21 alpha 1 collagen polypeptide recited in instant claim 26. Therefore, the peptide of SEQ ID NO: 2 recited in claims 49-51 of co-pending Application No. 17/714896 is monomeric and does not form a stable triple helix structure formed by natural collagen at 37 oC. It meets the limitation of instant claim 33. Furthermore, the MPEP states “Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). "When the PTO shows a sound basis for believing that the products of the applicant and the prior art are the same, the applicant has the burden of showing that they are not." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). Therefore, the prima facie case can be rebutted by evidence showing that the prior art products do not necessarily possess the characteristics of the claimed product. In re Best, 562 F.2d at 1255, 195 USPQ at 433. See also Titanium Metals Corp. v. Banner, 778 F.2d 775, 227 USPQ 773 (Fed. Cir. 1985) (Claims were directed to a titanium alloy containing 0.2-0.4% Mo and 0.6-0.9% Ni having corrosion resistance. A Russian article disclosed a titanium alloy containing 0.25% Mo and 0.75% Ni but was silent as to corrosion resistance. The Federal Circuit held that the claim was anticipated because the percentages of Mo and Ni were squarely within the claimed ranges. The court went on to say that it was immaterial what properties the alloys had or who discovered the properties because the composition is the same and thus must necessarily exhibit the properties.).” (see MPEP § 2112.01 I). In addition, since the USPTO lacks the experimental facilities to make a further determination, the burden is on the Applicant to prove the otherwise.
This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
37. For the same/similar reasoning/rational as the rejection set forth in Sections 32-34 and 36 above, instant claims 26-33 are provisionally rejected on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claim 56 of co-pending Application No. 18/856728; and claims 24 and 101 of co-pending Application No. 18/856729.
The peptide of SEQ ID NO: 19 recited in claim 56 of co-pending Application No. 18/856728; and the peptide of any one of SEQ ID NO: 63-65 and many others recited in claims 24 and 101 of co-pending Application No. 18/856729 comprise the amino acid sequence of a human type 21 alpha 1 collagen polypeptide comprising an N-terminal and/or a C-terminal truncation and no more than one GPP triplet sequence.
These are all provisional obviousness-type double patenting rejections because the conflicting claims have not in fact been patented.
Conclusion
No claim is allowed.
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/LI N KOMATSU/Primary Examiner, Art Unit 1658
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