DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Election/Restrictions
Applicant’s election without traverse of Group I, claims 1-10, and the species osteogenesis (claim 10) in the reply filed on 01/09/2026 is acknowledged.
Priority
The instant application filed on 03/13/2023 is a 371 of PCT/US2021/049646 filed on 09/09/2021, which claims priority to U.S. Provisional Applications 63/079,187, 63/093,554, and 63/149,068 filed on 09/16/2020, 10/19/2020, and 02/12/2021, respectively. U.S. PRO 63/079,187 finds support for the instantly claimed invention; therefore, the effective filing date of the instant application is 09/16/2020.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 03/13/2023, 07/24/2024, 02/13/2025, 06/18/2025, 07/31/2025, and 12/19/2025 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Claim Objections
Claim 10 is objected to because of the following informalities: claim 10 recites “…and cardio-vascular repair, breast repair, and endothelial repair”; however, the “and” before cardio-vascular repair should be removed. This is an objection, not a rejection, because this appears to be a typographical issue.
Claim Rejections - 35 USC § 112(b), Indefiniteness
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.
Claims 1-10 are rejected under 35 U.S.C. 112(b) 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 1 recites “amplified desired characteristic”; however, the term “amplified” is considered relative terminology and it is unclear what the amplified characteristic is in relation, or compared to in order to be considered amplified. The instant specification does not provide example(s), teaching(s), or definition(s) on how to measure a desired characteristic and what is considered “amplified”. Moreover, it is unclear what the amplified characteristic is compared to in order to determine it is amplified. Therefore, the instant specification lacks a standard for measuring the degree intended and one of ordinary skill in the art would not readily understand how to determine whether or not a characteristic is amplified (see, e.g., MPEP 2173.05(n)).
Claims 1-2 recite methods of deriving peptides containing desired characteristics; however, it is unclear to the Examiner how the added peptides exhibiting desired characteristics in claim 1 are differentiated from the peptides exhibiting desired characteristics derived from the collagen in claim 2. Moreover, it is unclear to the Examiner if these peptides have the same desired characteristics, or different desired characteristics. Furthermore, it is unclear if the peptides added in claim 1 are derived from collagen, or another source.
Claims 1-2 and 4-10 recite “desired characteristic”; however, this is relative terminology which renders the claim indefinite. The term “desired” is not defined by the claim, the specification does not provide a standard for ascertaining the requisite degree, and one of ordinary skill in the art would not be reasonably apprised of the scope of the invention. This claim is indefinite because the metes and bounds of what desired characteristic(s) exhibited by the collagen product and/or the peptides is intended to be included in, or excluded from, the collagen and/or peptides product is unclear. Moreover, what is desired by one skilled artisan might not be desired by another. Therefore, these peptides can be any peptides since what is desired by one skilled artisan may, or may not be, desired by another skilled artisan. Based on this, the metes and bounds of the claimed invention cannot be ascertained. Therefore, for the purposes of applying prior art, the Examiner has interpreted these peptides to be any peptide since the term “desired” is subjective and can encompass any peptide since any peptide can be desirable based on its characteristics.
Claim 3 recites the limitation "the digestion step" There is insufficient antecedent basis for this limitation in the claim. No digestion step was previously recited.
Claim 7 recites “the release profile”. There is insufficient antecedent basis for this limitation in the claim. No release profile was previously recited. Moreover, it is unclear what a “release profile” means, as there is no definition in the instant specification for this term. It is unclear if the release profile simply refers to the peptide’s release from the collagen, or if the release profile refers to how much peptide is released from the collagen and interacts with a cell of interest over time, or if the release profile refers to how much peptide is released from the collagen and exhibits a desired effect. Therefore, this is indefinite because it is unclear what a release profile is in terms of the peptide and the metes and bounds of the claimed invention cannot be readily ascertained since this is not defined in the instant specification (see, e.g., MPEP 2173.02). For the purposes of applying prior art, the Examiner has interpreted “release profile” to be the concentration of peptides needed to exhibit a desired effect.
Claim Rejections - 35 USC § 112(a), Written Description
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1-10 are rejected under 35 U.S.C. 112(a) 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 1-2 and 4-10 recite “peptides exhibiting a desired characteristic”; however, Applicant is broadly and functionally claiming peptides that have a “desired characteristic” and the instant specification does not describe these peptides in enough specificity such that the Applicant has shown possession of the entire genus. The instant specification states “The collagen is then digested and fractioned (120), to break the collagen down into its constituent fragments, or peptides. Such peptides include, for example, P20 and P35” (see, e.g., instant specification, [00179]). Moreover, the instant specification states “Different peptides have different biological properties that imbue them with desired/desirable attributes/characteristics, such as a higher affinity for therapeutic usage in specific medical applications” (see, e.g., instant specification, [00180]). Additionally, the instant specification states “In various embodiments, the collagen fractions or synthesized collagen peptide (e.g., CHP or CMP) can be a single-, double- or triple-stranded peptide” (see, e.g., instant specification, [00184]). Furthermore, the instant specification states “In an embodiment, after digestion and fragmentation of the collagen tissue, each of the collagen fractions/peptides is tested (130) for various biological properties, such as, for example, attributes/characteristics that are useful for wound healing, blood clotting, bone formation/osteogenesis, cosmetic application, scaffolds for organ regeneration, use as antioxidants, antibacterial and/or anti-inflammatory activity, and for the delivery of drugs such as insulin and methylene blue, showing lower water absorbency” (see, e.g., instant specification, [00180]). Moreover, the instant specification states “Of course, it is recognized that more than a single desired characteristic may be engineered into or out of the targeted collagen. For example, in skin wound healing, amplification of the collagen via bio-active peptides could be added for clotting, epithelial growth and faster resorption. A clotting test could identify the peptide that induces this process, an epithelial cell assay could identify the bioactive peptide for cell activity and the peptide that is targeted by the enzyme collagenase could be added to increase the collagen absorption” (see, e.g., instant specification, [00215]). This further shows that Applicant does not have possession of the peptides and is merely describing potential peptides not yet in their possession. Based on this, the Applicant does not describe these peptides by their structure or sequence, and merely functionally describes these peptides by the effects they should exhibit within the body. Furthermore, Applicant has not provided a representative number of species for the claimed genus. To satisfy the written description requirement, the Applicant must have possession of a representative number of species which are adequately described and are representative of the entire genus at the time the invention was filed (see, e.g., MPEP 2163(II)(A)(3)(ii)).
Moreover, each of these claims described the peptide functionally, but does not provide descriptions and/or structures of these peptides; therefore, there is no structure/function correlation. Thus, without a structure associated with the function, one would not know what known and unknown peptides fall within each genus. Additionally, claiming a generic function attempts to claim all known and unknown species with that specific function at the time the invention was filed. For example, the Applicant claims peptides with a desired characteristic; however, the Applicant does not teach any species that fall within the genus. Therefore, a skilled artisan would not know from the guidance of the instant specification what species are capable of exhibiting the desired characteristic in such a manner as to produce the claimed product. Furthermore, the metes and bounds of the claimed invention cannot be ascertained.
Accordingly, claims 1-10 do not meet the written description requirement. Claim 3 is included in this rejection for depending on independent claim 1 and failing to rectify the noted deficiencies.
Claim Rejections - 35 USC § 102, Anticipation
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.
Claims 1-5 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Harrell (US 2012/0189586; Date of Publication: July 26, 2012 – cited in the IDS filed on 03/13/2023).
Harrell’s general disclosure relates to “a composition for use in tissue augmentation of a human. More specifically, the composition comprises collagen extracted from human placenta and a bulking agent” (see, e.g., Harrell, abstract). Furthermore, Harrell discloses “Representative tissues include but are not limited to breast tissue, sphincter tissue, buttocks tissue, fatty tissue, perineal body of the vagina, a cleft lip and corn tissue” (see, e.g., Harrell, [0010]). Moreover, Harrell discloses “the composition further comprising a pharmaceutical excipient, an analgesic, a local anesthetic, an anti-inflammatory agent, or a combination thereof. In another form, the composition further comprises contractile tissue, subcutaneous tissue, dermal tissue, connective tissue, epidermal cells, or stem cells, or a combination thereof. In yet another form, the composition further comprises an anti-microbial agent, a growth factor, a growth-promoting serum factor, or a combination thereof” (see, e.g., Harrell, [0011]).
Regarding claim 1 pertaining to the targeted collagen product, Harrell teaches a method for soft tissue augmentation comprising contacting tissue with a bulking agent and human collagen (see, e.g., Harrell, [0009]). Furthermore, Harrell teaches that the bulking agent can “include but are not limited to autologous globin, elastin, acellular human cadaveric dermis or autologous fibroblasts or a synthetic polymer” (see, e.g., Harrell, [0009]). One of ordinary skill in the art would readily recognize that globulin and elastin can be peptides. Furthermore, in Example 1, Harrell teaches combining human placental collagen with a bulking agent (see, e.g., Harrell, [0114]-[0115]). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 2 pertaining to digesting the collagen, Harrell teaches “the collagen is extracted by proteolytic digestion of a source selected from the group consisting of insoluble amnion, soluble amnion, soluble chorion of the placenta and combinations thereof. The collagen comprises Type I and Type III collagen. In more particular embodiments, the Type III collagen is at least 30% of the weight or volume of the collagen component” (see, e.g., Harrell, [0077]). Furthermore, Harrell teaches “In certain embodiments, the proteolytic digestion is with pepsin” (see, e.g., Harrell, [0079]). Moreover, in Example 10, Harrell teaches digestion of placental tissue by pepsin in an acidic solution (see, e.g., Harrell, [0126]). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 3 pertaining to procuring collagen, Harrell “Representative collagen materials include placental collagen, recombinant human collagen, tissue engineered human-based collagen, porcine collagen, bovine collagen, autologous collagen, collagen fibers, and human tissue collagen matrix. In certain embodiments, collagen in the compositions comprises collagen extracted from human placental tissue” (see, e.g., Harrell, [0035]). Furthermore, Harrell teaches “Human sourced collagen is advantageous over compositions containing non-human sourced collagen, such as bovine collagen, when administered to humans. Allogeneic compositions exhibit a reduced immune response compared to injections of compositions containing material sourced from a different species than the recipient” (see, e.g., Harrell, [0036]). Additionally, in Example 1, Harrell teaches a method of producing a composition comprising human placental collagen (see, e.g., Harrell, [0114]).
Regarding claim 4 pertaining to testing the peptides, Harrell teaches, in Examples 10-11, testing the peptides for desired characteristics, wherein the digested collagen peptides from Example 10 were implanted into the dermis of domestic pigs in Example 1 in order to study tissue implants (see, e.g., Harrell, [0126]-[0127]). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 5 pertaining to isolating the peptides, Harrell teaches collagen peptides can be derived from human placenta and porcine skin (see, e.g., Harrell, Examples 10-11, [0126]-[0127]). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 6 pertaining to adding peptides to a mixture, Harrell teaches isolating collagen peptides from placental tissue, wherein the placental tissue was digested by pepsin in an acidic solution (see, e.g., Harrell, Example 10, [0126]). Moreover, Harrell teaches injecting these digested placental tissue samples, which contain collagen peptides, into pig dermis (see, e.g., Harrell, Example 11, [0127]). One of ordinary skill in the art would readily understand that the pig dermis contains collagen. Therefore, Harrell teaches isolating collagen peptides through digestion of placental tissue with pepsin and further adding these peptides to a mixture (i.e., pig dermis) which further contains collagen. Therefore, this would inherently lead to reconstitution of the collagen into the targeted collagen product (see, e.g., MPEP 2112). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Claims 1, 3, and 6-9 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lee (Prolonged survival of transplanted stem cells after ischaemic injury via the slow release of pro-survival peptides from a collagen matrix; 2018 – cited in the IDS filed on 03/13/2023; herein referred to as “Lee 2018”).
Lee 2018’s general disclosure relates to covalently crosslinking peptide analogues to collagen matrix scaffolds via dendrimers in order to improve the half-life of peptide analogues (see, e.g., Lee 2018, Introduction, pg. 104). Furthermore, Lee discloses the peptide analogues are BMP2, EPO, and FGF2; therefore the “col×D×pep cocktail contained a combination of BMP2, EPO and FGF2 individually crosslinked to dendrimized collagen (for example, col×D×BMP2, col×D× EPO and col×D× FGF2)” (see, e.g., Lee 2018, Introduction, pg. 104), wherein D represents dendrimer.
Regarding claim 1 pertaining to the targeted collagen product, Lee 2018 teaches covalently crosslinking peptide analogues to a collagen matrix scaffold via dendrimers (see, e.g., Lee, 2018, Introduction, pg. 2014). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 3 pertaining to the step of deriving collagen, Lee 2018 teaches that the collagen was derived from rat tail (see, e.g., Lee, 2018, Methods, “Preparation of peptide-crosslinked collagen”, pg. 112). Refer to the Examiner’s interpretation of this claim in the 112(b) rejection above.
Regarding claim 6 and 8-9 pertaining to the adding step, Lee 2018 teaches “peptide analogues could be covalently cross-linked to a collagen matrix scaffold via dendrimers (col×D×pep, in which col represents collagen, × represents crosslinked, D represents dendrimer and pep represents peptide) to provide a controlled delivery system. Specifically, our col×D×pep cocktail contained a combination of BMP2, EPO and FGF2 individually crosslinked to dendrimized collagen (for example, col×D×BMP2, col×D× EPO and col×D× FGF2)” (see, e.g., Lee 2018, Introduction, pg. 104). Furthermore, Lee 2018 teaches “collagen was crosslinked with first-generation polyamidoamine dendrimers, which are rich in amine groups (Fig. 1a). Dendrimer crosslinking was achieved by coupling the amine groups on dendrimers to the carboxyl groups of collagen's ≈ 12% acidic amino acids (for example, aspartic acid and glutamic acid) through the standard peptide coupling method utilizing 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide and N-hydroxysulfosuccinimide (EDC/sulfo-NHS) to obtain col× D. Pro-survival peptides BMP2, FGF2 and EPO were separately crosslinked to the dendrimers on collagen using the same crosslinkers” (see, e.g., Lee 2018, Figure 1 & Results – “Design of the colxDxpep delivery system”). Therefore, Lee 2018 teaches adding peptides to intact collagen, wherein the peptides crosslink with the collagen.
Regarding claim 7 pertaining to the release profile of the peptides, Lee 2018 teaches crosslinking collagen and peptides via dendrimers (see, e.g., Lee 2018, Introduction, pg. 104), wherein the crosslinked peptides demonstrated prolonged release that lasts for “periods longer than 15 day” (see, e.g., Lee 2018, “Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105). Moreover, Lee 2018 teaches “Interestingly, dendrimer crosslinking resulted in different release profiles for different peptides, possibly due to the differential alterations in collagen structure and charges (Fig. 2a–c). The slowest release profile, however, was observed only when peptides were covalently crosslinked (Fig. 2d)” (see, e.g., Lee 2018, “Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105). Additionally, Lee 2018 teaches “Peptides covalently crosslinked are released gradually as collagen degrades and autolysis occurs. The presence of the dendrimer moieties promotes hydrolysis of the amide bonds24,25, fostering peptide release (Supplementary Fig. 9). Of the two cleavable sites (dendrimer–peptide and dendrimer–collagen), the dendrimer–peptide link has greater exposure to solvent, is more accessible for chemical transformations and is thus more prone to autolysis. After autolytic cleavage, the release kinetics depends on the binding affinity of the peptide to dendrimers in col× D, which varies according to the number of hydrogen donor groups in each peptide. The quicker release of peptides from col× D + peptide compared to col + peptide is probably due to the low binding affinity of peptides to the highly positively charged dendrimers present in col× D (Fig. 2a–c)” (see, e.g., Lee 2018, “Gradual release of peptide factors from the colxDxpep delivery system”, pg. 105).
Claims 1, 3, 6, and 8-10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Lee (Assembly of collagen-binding peptide with collagen as a bioactive scaffold for osteogenesis in vitro and in vivo; 2007 – herein referred to as “Lee 2007”).
Lee 2007’s general disclosure relates to “peptide, denoted as collagen-binding motif (CBM, GLRSKSKKFRRPDIQYPDATDEDITSHM) identified from osteopontin (OPN) protein, was able to specifically bind collagen without chemical conjugation, while presenting apatite forming capability in vitro and in vivo” (see, e.g., Lee 2007, abstract). Moreover, Lee discloses “In vivo result further demonstrated that the CBM peptide in complex with material was able to induce bone formation by helping mineralization in the bone defect. Taken together, the CBM peptide herein and its assembly with collagen can be applied as an inducer of biomineralization as well as a bioactive scaffold for bone regeneration” (see, e.g., Lee 2007, abstract).
Regarding claim 1 pertaining to the targeted collagen product, Lee 2007 teaches a “peptide, denoted as collagen-binding motif (CBM, GLRSKSKKFRRPDIQYPDATDEDITSHM) identified from osteopontin (OPN) protein, was able to specifically bind collagen without chemical conjugation, while presenting apatite
forming capability in vitro and in vivo (see, e.g., Lee 2007, abstract). Therefore, Lee teaches a peptide binding to collagen. Moreover, Lee 2007 teaches measuring the binding kinetics of the collagen binding motif of osteopontin by immobilizing collagen onto a matrix and allowing the osteopontin peptides to bind to the collagen (see, e.g., Lee 2007, section 2.4, pg. 4258).
Regarding claim 3 pertaining to the derived collagen, Lee 2007 teaches that the collagen is human type I collagen (see, e.g., Lee 2007, Section 2.1 – Materials, pg. 4258).
Regarding claims 6 and 8-9 pertaining to the adding step, Lee 2007 teaches osteopontin, which has a collagen-binding domain (see, e.g., Lee 2007, abstract), and wherein the binding kinetics of osteopontin and collagen can be measured by immobilizing collagen onto a matrix and allowing osteopontin peptides to bind (see, e.g., Lee 2007, section 2.4, pg. 4258).
Regarding claim 10 pertaining to the peptides exhibiting osteogenesis, the Examiner has interpreted this claim to mean that the peptides that are added to the collagen have the desired characteristic of osteogenesis. Lee 2007 teaches a peptide from osteopontin containing a collagen-binding motif, wherein the peptide can bind to collagen, forming a collagen-peptide complex, and wherein the complex can induce bone formation and help mineralization of a bone defect (i.e., osteogenesis) (see, e.g., Lee 2007, abstract).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1 and 8 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1 of copending Application No. 18/091,782 (reference application; herein referred to as “App’782”). Although the claims at issue are not identical, they are not patentably distinct from each other because App’782 claims: A method for forming a targeted collagen product having an amplified desired characteristic, comprising: adding peptides exhibiting a desired characteristic to collagen to form the targeted collagen product; wherein the adding step includes adding the peptides exhibiting the desired characteristic to a mixture to modify collagen into the targeted collagen product; wherein the adding step is performed so that the modified collagen is crosslinked to the peptide exhibiting the desired characteristic and wherein the crosslinking of the collagen to the peptide exhibiting the desired characteristic occurs by modification of the peptide to facilitate binding to the collagen (see, e.g., App’782, claim 1).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Claims 1-10 are rejected.
No claims are allowed.
Correspondence Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE IANNUZO whose telephone number is (703)756-5559. The examiner can normally be reached Mon - Fri: 8:30-6:00 EST.
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/NATALIE IANNUZO/Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653