DETAILED CORRESPONDENCE
Status of the Application
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on January 16, 2026 has been entered.
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1, 4, 7-20, and 26-28 are pending in the application.
Applicant’s amendment to the claims, filed January 16, 2026, is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s remarks filed January 16, 2026 in response to the final rejection mailed October 17, 2025 have been fully considered.
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Restriction/Election
In response to a requirement for restriction/election mailed August 9, 2022, applicant elected without traverse the invention of Group I, pending claims 1, 3, 4, 7, 11-13, 19, 20, and 26-28, drawn to the technical feature of a synthetic compound, a pharmaceutical or diagnostic composition or formulation, and a device; Species A), a therapeutic agent including a growth factor, a therapeutically active polypeptide, an antibody, a polymer, a small molecule, or a combination thereof; and Species AA), FXIII.
Claims 8-10 and 14-18 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Claim 4 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim.
Claims 1, 7, 11-13, 19, 20, and 26-28 are being examined on the merits to the extent the claim reads on the elected subject matter set forth above.
Claim Objections
The objection to claim 1 is withdrawn in view of the applicant’s amendment to claim 1.
Claim Rejections - 35 USC § 103
The rejection of claims 1, 7, 11-13, 19, and 20 under 35 U.S.C. 103 as being unpatentable over Mûller-Maissen et al. (US 2013/0183279 A1; cited on Form PTO-892 mailed on October 25, 2022; hereafter “Mûller-Maissen”) in view of Sivaramakrishnan et al. (Biochim. Biophys. Acta 1833:3176-3185, 2013; cited on the IDS filed on June 5, 2020; hereafter “Sivaramakrishnan”), and
the rejection of claims 26-28 under 35 U.S.C. 103 as being unpatentable over Mûller-Maissen in view of Sivaramakrishnan as applied to claims 1, 7, 11-13, 19, and 20 above, and further in view of Traoré et al. (J. Agric. Food Chem. 39:1892-1896, 1991; cited on Form PTO-892 mailed January 16, 2024; hereafter “Traoré”)
are withdrawn in view of applicant’s amendment to claim 1 to recite “wherein the at least one therapeutically or diagnostically active molecule is an antibody…” and in favor of the new rejections set forth below.
Claims 1, 7, 11-13, 19, and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Mûller-Maissen in view of Sivaramakrishnan and as evidenced by Salampessy et al. (Journal of Functional Foods 14:716-725, 2015; cited on the attached Form PTO-892; hereafter “Salampessy”) and Sanjabi et al. (Cold Spring Harb Perspect Biol 9:a02226, June 2017, 33 pages; cited on the attached Form PTO-892; hereafter “Sanjabi”).
Regarding the claim 1 limitation “A pharmaceutical or diagnostic composition,” Mûller-Maissen teaches a fibrin formulation comprising fibrinogen, thrombin, and an added bioactive factor (claim 1 of Mûller-Maissen).
Regarding the “synthetic compound” of claim 1, part 1), Mûller-Maissen teaches the added bioactive factor of the fibrin formulation is a fusion protein comprising at least two domains wherein the first domain comprises a growth factor and the second domain comprises a transglutaminase substrate domain (claim 10 of Mûller-Maissen). Mûller-Maissen teaches various growth factors including platelet-derived growth factor (PDGF) A, PDGF B, and transforming growth factor β (TGFβ) (paragraph [0155]).
Regarding PDGF A and PDGF B, Mûller-Maissen teaches the amino acid sequence of PDGF A, which comprises the dipeptide sequence Ala-Val (AV) corresponding to amino acids 26-27 and 29-30 of SEQ ID NO: 2 (paragraph [0170]) and teaches the amino acid sequence of PDGF B, which comprises the dipeptide sequence Ala-Arg (AR) corresponding to amino acids 126-127 of SEQ ID NO: 3 (paragraph [0171]). Evidentiary reference Salampessy is cited to show that the dipeptides AV and AR are ACE inhibitory peptides with molecular weights of 245 and 188, respectively (p. 716, Abstract; p. 720, column 2, middle to bottom) and AV and AR dipeptides of the PDGF A or PDGF B component of the fusion protein of Mûller-Maissen are considered to be therapeutically active small molecules. As such, the fusion protein of Mûller-Maissen comprises at least one anchor domain (i.e., the transglutaminase substrate domain of the fusion protein of Mûller-Maissen) and comprises at least one therapeutically active small molecule (i.e., the ACE inhibitory AV or AR dipeptide of the PDGF A or PDGF B component of the fusion protein of Mûller-Maissen).
Regarding TGFβ, evidentiary reference Sanjabi is cited to show that TGFβ is a cytokine that regulates the immune response (p. 1, Abstract and paragraph bridging pp. 1-2) and TGFβ is considered to be a therapeutically active immune modulating cytokine. As such, the fusion protein of Mûller-Maissen comprises at least one anchor domain (i.e., the transglutaminase substrate domain of the fusion protein of Mûller-Maissen) and comprises at least one therapeutically active immune modulating cytokine (i.e., TGFβ).
Mûller-Maissen teaches the transglutaminase substrate domain is a Factor XIIIa substrate domain (claim 11 of Mûller-Maissen).
Regarding the “heterologous cleavable linker peptide between the at least one anchor domain and the at least one therapeutically or diagnostically active molecule, wherein the cleavable linker peptide is cleaved in a desired environment of use or administration of the pharmaceutical or diagnostic composition” of claim 1, Mûller-Maissen teaches the fusion protein comprises an enzyme degradation site between the first and second domains, e.g., an enzymatic degradation site that is cleaved by an enzyme selected from plasmin and matrix metalloprotease (paragraphs [0039] and [0126]), exemplified by a 21 amino acid “TG-hook” comprising a plasmin degradation site (paragraph [0166]).
Regarding the ACE inhibitory AV or AR dipeptide of the PDGF A or PDGF B component of the fusion protein of Mûller-Maissen as the “therapeutically active molecule” in claim 1, given a broadest reasonable interpretation, the amino acid sequence between the transglutaminase substrate domain and the ACE inhibitory dipeptide of the fusion protein of Mûller-Maissen is considered to be “a heterologous cleavable linker peptide” in claim 1 because it is “heterologous” to the transglutaminase substrate domain, directly links the transglutaminase substrate domain and the ACE inhibitory dipeptide, and has an enzyme degradation site.
Regarding TGFβ of the fusion protein of Mûller-Maissen as the “therapeutically active molecule” in claim 1, given a broadest reasonable interpretation, the TG hook between the transglutaminase substrate domain and TGFβ of the fusion protein of Mûller-Maissen is considered to be “a heterologous cleavable linker peptide” in claim 1 because it is “heterologous” to the transglutaminase substrate domain and TGFβ, directly links the transglutaminase substrate domain and TGFβ, and has an enzyme degradation site.
Regarding the “enzyme having transglutaminase activity” of claim 1, part 2), Mûller-Maissen teaches the fibrinogen of the fibrin formulation is in a fibrinogen precursor solution (paragraph [0097]). Mûller-Maissen teaches that preferably, factor XIII is present in the fibrinogen precursor solution (paragraph [0120]), which is activated to Factor XIIIa by mixing with thrombin (paragraphs [105] and [0108]).
The difference between Mûller-Maissen and claim 1 is that Mûller-Maissen does not teach the transglutaminase substrate domain of the fusion protein (i.e., the “anchor domain” of claim 1) comprises the sequence of instant SEQ ID NO: 1 or a derivative thereof as recited in parts i), ii), and iii) of claim 1.
Sivaramakrishnan teaches the amino acid sequence surrounding K68 (PAK68SA) of IGF-I is in broad agreement with the consensus (P/L)-(S/L/A/R)-K-(OH/L/G/V) substrate motif for transglutaminases (p. 3183, column 1, middle). Sivaramakrishnan teaches that the D domain sequence CAPLKPAKSA of IGF-I is cross-linked by FXIIIa (p. 3176, Abstract; p. 3179, column 2; p. 3180, Figure 4). According to Sivaramakrishnan, the data indisputably demonstrates that IGF-I is a lysine donor substrate to FXIIIa and that K68 is the key lysine donor site in IGF-I to FXIIIa (p. 3183, column 1, middle).
In view of the combined teachings of Mûller-Maissen and Sivaramakrishnan, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify Mûller-Maissen to use the sequence surrounding K68 of IGF-I, e.g., PAKSA or CAPLKPAKSA, as the Factor XIIIa substrate domain of the fusion protein. One would have been motivated and would have expected success to do this because Mûller-Maissen discloses the fusion protein of the fibrin formulation comprises a transglutaminase substrate domain, particularly a Factor XIIIa substrate domain, and Sivaramakrishnan teaches that K68 of IGF-I is within a consensus substrate motif for transglutaminases and is a lysine donor for Factor XIIIa cross-linking.
Regarding claim 7, given that claim 7 does not define to what the composition is being locally administered, the modified fibrin formulation of combined Mûller-Maissen and Sivaramakrishnan is considered to be encompassed by claim 7.
Regarding claim 11, Mûller-Maissen discloses various “devices” comprising the fibrin formulation, including a fibrin foam (paragraph [0135]) and a fibrin matrix (paragraph [0135]).
Regarding claim 12, Mûller-Maissen discloses fibrin matrices have been used as drug delivery devices (paragraph [0107]).
Regarding claim 13, Mûller-Maissen discloses fibrin matrices have been used as a material for cell in-growth matrices (paragraph [0107]) and discloses adding cells to the matrix prior to implantation (paragraph [0162]).
Regarding claims 19 and 20, Mûller-Maissen discloses fibrin is polymerized fibrinogen (paragraph [0108]) and thus, the fibrin matrices used as a material for cell in-growth as noted above for claim 13 are polymer networks.
Therefore, the invention of claims 1, 7, 11-13, 19, and 20 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 26-28 are rejected under 35 U.S.C. 103 as being unpatentable over Mûller-Maissen in view of Sivaramakrishnan and as evidenced by Salampessy and Sanjabi as applied to claims 1, 7, 11-13, 19, and 20 above, and further in view of Traoré et al. (J. Agric. Food Chem. 39:1892-1896, 1991; cited on Form PTO-892 mailed January 16, 2024; hereafter “Traoré”).
The relevant teachings of Mûller-Maissen and Sivaramakrishnan and evidentiary reference Salampessy as applied to claims 1, 7, 11-13, 19, and 20 are set forth above.
Regarding claims 26-28, as noted above for claim 1, Mûller-Maissen teaches that preferably, factor XIII is present in the fibrinogen precursor solution (paragraph [0120]), which is activated to Factor XIIIa by mixing with thrombin (paragraphs [105] and [0108]).
The combination of Mûller-Maissen and Sivaramakrishnan does not teach or suggest the Factor XIII is mammalian or human Factor XIII.
Traoré teaches thrombin activation of human Factor XIII (p. 1892, column 1, bottom) and cross-linking of caseins by thrombin-activated human Factor XIIIa (p. 1894, Table II).
It would have been obvious to one of ordinary skill in the art before the effective filing date to combine Mûller-Maissen, Sivaramakrishnan, and Traoré to use human Factor XIII of Traoré in the fibrin formulation of Mûller-Maissen. One would have been motivated to and would have had a reasonable expectation of success to do this because Mûller-Maissen teaches thrombin-activated Factor XIII in the fibrin formulation as a cross-linking agent and Traoré teaches human Factor XIII is activated by thrombin and teaches thrombin-activated human Factor XIII as a cross-linking agent.
Therefore, the invention of claims 26-28 would have been obvious to one of ordinary skill in the art before the effective filing date.
RESPONSE TO REMARKS: In summary, applicant argues the combination of cited prior art fails to teach or suggest all limitations of the claims because the PDGF component of the fusion protein of Mûller-Maissen is not an antibody, polyethylene glycol, a small molecule, an anti-apoptotic molecule, an anti-inflammatory molecule, an antibiotic, a hormone, an immune modulating cytokine, or a combination thereof.
Applicant’s arguments are not found persuasive. For reasons described above, the ACE inhibitor dipeptide within the PDGF A or PDGF B of the fusion protein of Mûller-Maissen is considered to be a therapeutically active small molecule in claim 1 and the TGFβ of the fusion protein of Mûller-Maissen is considered to be a therapeutically active immune modulating cytokine in claim 1. Contrary to applicant’s position, in view of the rejections set forth above, the combination of cited prior art teaches or suggests all limitations of the claims and it is the examiner’s position that the claimed invention would have been prima facie obvious to one of ordinary skill in the art before the effective filing date.
Claim Rejections – 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.
The provisional rejection of claims 1, 7, 11-13, 19, 20, and 26-28 on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 5-7, 9, 11-13, 20, and 21 of copending Application No. 17/047,851 (reference application) is withdrawn in view of applicant’s amendment to claim 1 to recite “wherein the at least one therapeutically or diagnostically active molecule is an antibody…” and in favor of the new rejections set forth below.
Claims 1, 7, 11-13, 19, and 20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3, 5-7, 11, 12, and 21 of copending Application No. 17/047,851 (reference application) as evidenced by Salampessy. Although the claims at issue are not identical, they are not patentably distinct from each other.
Regarding claim 1 of this application, claim 6 of the reference application recites a pharmaceutical composition or formulation comprising a synthetic compound,
wherein the synthetic compound is suitable for transglutaminase-mediated binding or attachment or incorporation of a therapeutic and/or diagnostic molecule into an extracellular matrix or a synthetic extracellular matrix component, wherein said synthetic compound comprises
(a) at least one anchor domain and
(b) at least one second domain, wherein said second domain possesses therapeutic and/or preventive activity,
wherein said anchor domain is the isolated D domain of Insulin Growth Factor-1 (IGF-I) as depicted in SEQ ID NO: 1,
wherein said isolated D domain does not comprise the growth factor activity of IGF-I,
wherein said anchor domain is capable of binding to an extracellular matrix or a synthetic extracellular matrix component;
wherein said second domain is directly or indirectly linked to the anchor domain, and
wherein said second domain comprises the amino acid sequence as defined in SEQ ID NO: 12;
claim 3 of the reference application recites the synthetic compound according to claim 1, wherein the second domain is selected from the group consisting of a binder of myostatin and a protein; and
claim 5 of the reference application recites the synthetic compound according to claim 1, wherein said compound further comprises a cleavable linker between the anchor domain and the at least one second domain, wherein the linker has an amino acid sequence as depicted in SEQ ID NO: 13.
SEQ ID NO: 12 of the reference application comprises the dipeptide sequence Ala-Arg (AR) corresponding to amino acids 5-6 of SEQ ID NO: 12. Evidentiary reference Salampessy is cited to show that the dipeptide AR is an ACE inhibitory peptide with a molecular weight of 188 (p. 716, Abstract; p. 720, column 2, middle to bottom). In view of the evidence of Salampessy, the AR dipeptide of SEQ ID NO: 12 of the reference application is a therapeutically active small molecule. Given a broadest reasonable interpretation, the amino acid sequence between the anchor domain and the ACE inhibitory dipeptide of SEQ ID NO: 12 of the claims of the reference sequence is considered to be “a heterologous cleavable linker peptide” in claim 1 of this application because it is “heterologous” to the anchor domain, directly links the anchor domain and the ACE inhibitory dipeptide, and has a cleavable linker.
Regarding claim 7 of this application, claim 7 of the reference application recites wherein said composition or formulation is suitable for localized administration.
Regarding claim 11 of this application, claim 11 of the reference application recites a device comprising a synthetic compound as defined in claim 1.
Regarding claim 12 of this application, claim 12 of the reference application recites wherein the device is suitable as a delivery system for immediate and/or sustained release of said compound.
Regarding claim 13 of this application, claim 11 of the reference application recites wherein said device is selected from the group consisting of patches, implants, scaffolds, porous vascular grafts, stents, and/or wound dressings.
Regarding claims 19 and 20 of this application, claim 21 of the reference application recites wherein said device is made of biocompatible fleece, hydrocolloid, polyacrylate, alginate, hydrogel, or foam, and/or an artificially produced tissue, bone-replacement, polymer network, fibrin, collagen, elastin, hyaluronic acid or silk protein.
Therefore, claims 1, 7, 11-13, 19, and 20 of this application are unpatentable over claims 3, 5-7, 11, 12, and 21 of the reference application. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 26-28 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 3, 5-7, 11, 12, and 21 of copending Application No. 17/047,851 (reference application) as evidenced by Salampessy as applied to claims 1, 7, 11-13, 19, and 20 above, and further in view of Sivaramakrishnan and Traoré. Although the claims at issue are not identical, they are not patentably distinct from each other.
The claims of the reference application do not recite the transglutaminase recited in claim 1 is a mammalian transglutaminase as recited in claims 26-28 of this application.
Sivaramakrishnan teaches FXIIIa is a transglutaminase (p. 3176, column 2), teaches the D domain of IGF-I is cross-linked by FXIIIa (p. 3176, Abstract; p. 3179, column 2; p. 3180, Figure 4), and teaches substrate proteins that are cross-linked by transglutaminases have been shown to be present in the extracellular matrix (p. 3177, column 1).
Traoré teaches using human FXIIIa to cross-link proteins (p. 1892, Abstract).
In view of Sivaramakrishnan and Traoré, it would have been obvious to one of ordinary skill in the art for the transglutaminase recited in claim 1 of the reference application to be human FXIIIa. One would have been motivated and expected success for the transglutaminase recited in claim 1 of the reference application to be human FXIIIa because claim 1 of the reference application recites transglutaminase-mediated incorporation of a synthetic compound comprising D domain of IGF-I into an extracellular matrix, Sivaramakrishnan teaches FXIIIa is a transglutaminase, teaches the D domain of IGF-I is cross-linked by FXIIIa, and teaches substrate proteins that are cross-linked by transglutaminases have been shown to be present in the extracellular matrix, and Traoré teaches human FXIIIa can be used to cross-link proteins.
Therefore, claims 26-28 of this application are unpatentable over claims 3, 5-7, 11, 12, and 21 of the reference application. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
RESPONSE TO REMARKS: Applicant argues the reference application has an effective filing date after that of the instant application; the reference application has been allowed; and the reference application includes a Terminal Disclaimer with respect to the instant application. Thus, according to applicant, there is no possibility of improper timewise extension of patent term beyond the current application and the double patenting rejection should be withdrawn.
Applicant’s arguments are not found persuasive. While the doctrine of nonstatutory double patenting seeks to prevent the unjustified extension of patent exclusivity beyond the term of a patent, a double patenting rejection also serves public policy interests by preventing the possibility of multiple suits against an accused infringer by different assignees of patents claiming patentably indistinct variations of the same invention (see MPEP 804 and 804.II.B). Thus, even if there is no improper timewise extension of patent rights, the provisional rejection as set forth above is raised in order to prevent the possibility of multiple suits against an accused infringer by different assignees of patents claiming patentably indistinct variations of the same invention.
Citation of Relevant Prior Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure. JP2003024012A (cited on the attached Form PTO-892) discloses various dipeptides, e.g., Ala-Val, as therapeutics for inhibiting angiotensin I converting enzyme (ACE) (see paragraph [0005] of machine translation of JP2003024012A, obtained from Espacenet on February 2, 2026; cited on the attached Form PTO-892).
Conclusion
Status of the claims:
Claims 1, 4, 7-20, and 26-28 are pending in the application.
Claims 4, 8-10, and 14-18 are withdrawn from consideration.
Claims 1, 7, 11-13, 19, 20, and 26-28 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656