Ex Parte Sarasa BarrioDownload PDFPatent Trial and Appeal BoardMar 21, 201714026374 (P.T.A.B. Mar. 21, 2017) Copy Citation United States Patent and Trademark Office UNITED STATES DEPARTMENT OF COMMERCE United States Patent and Trademark Office Address: COMMISSIONER FOR PATENTS P.O.Box 1450 Alexandria, Virginia 22313-1450 www.uspto.gov APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO. 14/026,374 09/13/2013 MANUEL SARASA BARRIO DRN-104US2 2004 23122 7590 03/23/2017 RATNFRPRFSTTA EXAMINER 2200 Renaissance Blvd BALLARD, KIMBERLY Suite 350 King of Prussia, PA 19406 ART UNIT PAPER NUMBER 1649 NOTIFICATION DATE DELIVERY MODE 03/23/2017 ELECTRONIC Please find below and/or attached an Office communication concerning this application or proceeding. The time period for reply, if any, is set in the attached communication. Notice of the Office communication was sent electronically on above-indicated "Notification Date" to the following e-mail address(es): PCorrespondence @ ratnerprestia.com PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE BEFORE THE PATENT TRIAL AND APPEAL BOARD Ex parte MANUEL SARASA BARRIO Appeal 2015-004503 Application 14/026,374 Technology Center 1649 Before DONALD E. ADAMS, TAWEN CHANG, and TIMOTHY G. MAJORS, Administrative Patent Judges. ADAMS, Administrative Patent Judge. DECISION ON APPEAL1 This appeal under 35 U.S.C. § 134(a) involves claims 1, 2, 5, and 6 (Final Act.2 2). Examiner entered rejections under the written description provision of 35 U.S.C. § 112, first paragraph, 35 U.S.C. § 102(b), and 35 U.S.C. § 103(a).3 We have jurisdiction under 35 U.S.C. § 6(b). We AFFIRM. 1 Appellant identifies the real party in interest as “Araclon Biotech, S.L.” (App. Br. 2). 2 Examiner’s June 6, 2014 Final Office Action. 3 Application 10/555,865 was abandoned July 11, 2016. Therefore, the provisional obviousness-type double patenting rejection over claims 9-11 and 14 of Application 10/555,865 is moot (see Ans. 7). Appeal 2015-004503 Application 14/026,374 STATEMENT OF THE CASE Appellant discloses “a method for treatment and/or prevention of diseases associated with the presence of amyloid deposits, which include Alzheimer’s disease” (Spec. 1: 7—8). Claims 1 and 5 are representative and reproduced below: 1. A method for reducing the accumulation of beta amyloid Ap42 peptide deposits in the brain of a patient suffering from a disease associated with the accumulation of beta amyloid Ap42 peptide deposits in the brain comprising administering to said patient a therapeutically effective amount of SEQ ID NO:[]3 conjugated to keyhole limpet hemocyanin for the production of antibodies that specifically recognize beta amyloid Ap42 peptide and effectively reduce beta amyloid Ap42 peptide deposition in said patient and wherein said antibodies do not bind to beta amyloid Ap40 peptide. (App. Br. 20.) 5. A method for reducing the accumulation of beta amyloid Ap42 peptide deposits in the brain of a patient suffering from a disease associated with the accumulation of beta amyloid Ap42 peptide deposits in the brain comprising administering to said patient an effective amount of an antibody, or an antigen binding fragment thereof that specifically binds to SEQ ID NO:[]3 and selectively inhibits beta amyloid Ap42 peptide deposition in said patient, and wherein said antibody or the fragment does not bind to beta amyloid Ap40 peptide. (Id.) The claims stand rejected as follows: Claims 1, 2, 5, and 6 stand rejected under the written description provision of35U.S.C. § 112, first paragraph. 2 Appeal 2015-004503 Application 14/026,374 Claims 5 and 6 stand rejected under 35 U.S.C. § 102(b) as anticipated by Schenk ’880.4 Claims 5 and 6 stand rejected under 35 U.S.C. § 102(b) as anticipated by Schenk ’686.5 Claims 5 and 6 stand rejected under 35 U.S.C. § 102(b) as anticipated by Chain.6 Claims 1 and 2 stand rejected under 35 U.S.C. § 103(a) as unpatentable over Chain. Written Description: ISSUE Does the preponderance of evidence on this record support Examiner’s finding that Appellant’s Specification fails to provide written descriptive support for the claimed invention? FACTUAL FINDINGS (FF) FF 1. Examiner finds that although Appellant’s Specification generically discloses antibodies “that bind[] to Ap40 and/or Ap42 and a method that reduces the deposition of amyloid in a subject,” Appellant’s Specification fails to disclose “an antibody that specifically binds to SEQ ID NO: 3 (AP33-42) and selectively inhibits/reduces Ap42 peptide deposition in a patient as [] claimed” (Ans. 7, citing Spec. 4—5; see Ans. 17 (Appellant’s “[Specification as filed does not support a subgenus of antibodies that have the properties of both specifically binding Ap42 and not Ap40 and 4 Schenk et al., WO 00/72880 A2, published Dec. 7, 2000. 5 Schenk, US 6,905,686 Bl, issued June 14, 2005. 6 Chain, US 2003/0073655 Al, published Apr. 17, 2003. 3 Appeal 2015-004503 Application 14/026,374 ‘selectively inhibiting’ or effectively reducing A042 peptide deposition in a patient”)). FF 2. Examiner finds: [TJhere is no disclosed support [in Appellant’s Specification], nor evidence of record, to indicate that the disclosed antibodies of [Appellant’s claimed] invention have th[e] very specific and selective functional property of inhibiting or reducing A042 peptide deposition selectively in the absence of reducing Af40 peptide (or other Aft speciesj deposition. (Ans. 17.) ANALYSIS The claims are not separately argued and, therefore, stand or fall together. Appellant’s claim 1 is representative. The method of Appellant’s claim 1 comprises the administration of a therapeutically effective amount of a peptide, specifically the peptide having SEQ ID NO: 3, which is conjugated to keyhole limpet hemocyanin, to a patient (App. Br. 20). As Appellant explains, Appellant’s Specification discloses the use of a peptideF such as a peptide having SEQ ID NO:[]3 (AP33-42),] conjugated to a protein that acts as an immunogen[, such as keyhole limpet hemocyanin,] to produce antibodies able to specifically recognize any of the predominant variants of the beta amyloid peptide A/NO and A//42 in the preparation of a medicament. (App. Br. 17, citing Spec. 4: 21—23, 5: 9-12, and 6: 18—22; see also Reply Br. 8—9; see FF 1). Thus, Appellant concedes that the administration of a peptide-immunogen conjugate, such as a peptide having SEQ ID NO: 3 conjugated to keyhole limpet hemocyanin, to a patient, will result in the production of antibodies that are able to specifically recognize any of the 4 Appeal 2015-004503 Application 14/026,374 predominant variants of the beta amyloid peptide, including Ap40 and A042. Appellant’s claimed invention, however, expressly requires that, notwithstanding the foregoing, the administration of a peptide having SEQ ID NO: 3 conjugated to keyhole limpet hemocyanin will result in the production of antibodies that specifically recognize beta amyloid Af42 peptide and effectively reduce beta amyloid Ap42 peptide deposition in the patient, wherein the antibodies do not bind to beta amyloid Af 40 peptide (App. Br. 20). As Examiner explains, Appellant’s Specification fails to disclose a method that produces antibodies to one epitope (Ap42) of a peptide, such as a peptide having SEQ ID NO: 3, which spans AP33-42 and not another epitope (Ap40) that is present in the same peptide (see FF 1—2). For the foregoing reasons, we are not persuaded by Appellant’s contention that a person of ordinary skill in this art would have readily appreciated that Appellant’s Specification discloses a method, wherein the administration of a peptide comprising a plurality of epitopes, including more than one predominant epitope, will result in the exclusive production of antibodies to only one epitope on the protein, i.e., Ap42 not Ap40 (see App. Br. 17—18; see also id. at 20; Reply Br. 9). We recognize Appellant’s contention that they identified one antibody that was produced in response to immunization with SEQ ID NO: 3, which was given the designation SAR-4 (see App. Br. 18; see also Spec. 9: 1—6). Appellant, however, fails to direct our attention to the specific portion of Appellant’s Specification that supports a finding that this was the only antibody produced by immunizing a patient with a peptide having SEQ ID NO: 3 conjugated to keyhole limpet hemocyanin (see App. 5 Appeal 2015-004503 Application 14/026,374 Br. 18). In addition, Appellant fails to direct our attention to a specific portion of Appellant’s “[Specification [that] clearly conveys to a skilled person that the antibody (SAR-4) generated using SEQ ID NO:[]3 binds to A//42 and does not bind to A//40” (id). Nevertheless, assuming that Appellant established that the one antibody, SAR-4, they identified does bind to Ap42 and not Ap40; Appellant failed to establish that SAR-4 is the only antibody produced by immunizing a patient with a peptide having SEQ ID NO: 3 conjugated to keyhole limpet hemocyanin, or, more specifically, that the immunization of a patient with such a peptide conjugate will not necessarily result in the production of antibodies to both Ap42 and Ap40, as well as any other predominant epitope present in a peptide having SEQ ID NO: 3 (see App. Br. 17; cf. App. Br. 17—18 and 20). Having failed to provide a disclosure of a method of producing antibodies that bind to Ap42 and not Ap40, we agree with Examiner’s finding that: [T]here is no disclosed support [in Appellant’s Specification], nor evidence of record, to indicate that the disclosed antibodies of [Appellant’s claimed] invention have th[e] very specific and selective functional property of inhibiting or reducing Ap42 peptide deposition selectively in the absence of reducing Af40 peptide (or other Aft species) deposition. (FF 2.) CONCLUSION OF LAW The preponderance of evidence on this record supports Examiner’s finding that Appellant’s Specification fails to provide written descriptive support for the claimed invention. 6 Appeal 2015-004503 Application 14/026,374 The rejection of claim 1 under the written description provision of 35 U.S.C. § 112, first paragraph is affirmed. Claims 2, 5, and 6 are not separately argued and fall with claim 1. Anticipation'. ISSUE Does the preponderance of evidence on this record support Examiner’s finding that Schenk ’880, Schenk ’686, or Chain teaches Appellant’s claimed invention? FACTUAL FINDINGS (FF) FF 3. Examiner finds that Schenk ’880 “disclose[s] therapeutic methods for the treatment of a disease associated with amyloid deposits of amyloid- beta (AP) in the brain of a patient, such as Alzheimer’s disease,” wherein the method “comprise[s] administering an effective dosage of an antibody that binds to AP” (Ans. 2). FF 4. Examiner finds that Schenk ’880 discloses “the therapeutic administration of the 2 IF 12 monoclonal antibody (mAb), which is reported to specifically bind the epitope of AP33-42, to transgenic mice that overexpress amyloid precursor protein” (Ans. 2; see id. (Appellant’s peptide having “SEQ ID NO: 3 is AP33-42”)). FF 5. Schenk ’880 discloses that the 21F12 mAb was “not efficacious in vivo” (Schenk ’880 97: 6-9). FF 6. Examiner finds that Schenk ’686 “discloses methods of treating a disease associated with amyloid deposits of Ap in the brain of a patient, such as Alzheimer’s disease (AD), comprising administering an effective amount of an antibody that binds to AP” (Ans. 4). 7 Appeal 2015-004503 Application 14/026,374 FF 7. Examiner finds that Schenk ’686 “discloses the therapeutic administration of the 2 IF 12 monoclonal antibody (mAb), which specifically binds the epitope of AP33-42 [] to transgenic []mice” that overexpress amyloid precursor protein (id.; see id. (Appellant’s “peptide of SEQ ID NO: 3 [is] []Ap3 3-42 []”)). FF 8. Schenk ’686 discloses that the 21F12 mAb was “not efficacious in vivo” (Schenk ’686 63: 33-37). FF 9. Chain relates to methods of treating a subject having Alzheimer's Disease, comprising the step of administering an antibody molecule which is targeted to P amyloid peptide or to fragment thereof. In another embodiment the invention relates to methods of treating a disease or a disorder, characterized by amyloid beta deposition. In another embodiment, the invention relates to an antibody molecule, which is free end-specific for the N-terminus or the C-terminus of an amyloid P peptide, or fragment thereof, and to a pharmaceutical composition thereof. (Chain 12; see id. at Abstract; see also id. 1 87 (“The diminished accumulation of amyloid P peptides will [] delay the progression of the Alzheimer’s Disease or other diseases characterized by amyloid beta deposition, in a subject in need”); id. at 8: claims 14 and 17; see Ans. 3 and 10-11). FF 10. Chain discloses that “[t]he most effective target for end-specific antibodies as therapy for Alzheimer’s Disease is likely to be Api-40, which forms the bulk of circulating amyloid P peptide human CSF, plasma, and urine[], or the more toxic but less abundant Api-42 and Api-43 species that can seed amyloid deposition” (Chain 141; see Ans. 3 and 10). 8 Appeal 2015-004503 Application 14/026,374 FF 11. Chain discloses: Once delivered into the brain the specific antibody molecules will transfer into the extracellular space, interstitial fluid and cerebrospinal fluid. The specific antibody molecules then form a soluble complex with Ap peptide. These soluble specific-Ap peptide-antibody complexes reduce, in one embodiment, the deposition of Ap peptides into amyloid plaques and attenuate Ap peptide-induced neurotoxicity by clearing Ap peptides from the central nervous system through drainage of the extracellular space, interstitial fluid and cerebrospinal fluid into the general blood circulation where they will be eliminated by protease digestion. Accordingly, the accumulation of newly secreted soluble Ap peptides responsible for amyloid deposition and Ap-induced neurotoxicity is inhibited. (Chain 1 57.) FF 12. Chain “relates to an antibody that is ffee-end specific and is targeted to the free C-terminus of N- and/or C-terminus-truncated amyloid P peptide fragment” (Chain 173; see Ans. 3 and 9). FF 13. Chain “relates to a single chain antibody that is ffee-end specific and is targeted to the free C-terminus of the amyloid P-peptide Api-42” (Chain 170; see also id. 178; id. at 19: claim 36; see Ans. 3 and 10). FF 14. Chain discloses the sequence of Ap42; discloses that “Ap41, Ap40 and Ap39 differ from Ap42 by the omission of Ala, Ala-lle and Ala-lle-Val respectively from the C-terminal end,” whereas “Ap43 differs from Ap42 by the presence of a threonine at the C-terminus;” and further discloses that “peptides can be designed for targeting Apx42 species” (Chain || 75—76; see generally Ans. 9—10). FF 15. Chain discloses that an antibody generated against an immunogenic peptide is evaluated for the selectivity of the antibody in its recognition of 9 Appeal 2015-004503 Application 14/026,374 a free N- or C-terminus of an Ap peptide. A competitive inhibition assay, using [an] Enzyme-Linked Immunosorba[n]t Assay (ELISA) or immunoprecipitation with peptides corresponding to different regions of Ap and the region immediately preceding the P-secretase cleavage site in the extracellular domain of the PAPP,[7] can determine the selectivity of the antibody. (Chain 179.) ANALYSIS The rejections over Schenk ’880 or Schenk ’686: Examiner finds that either of Schenk ’880 or Schenk ’686 anticipates the subject matter of Appellant’s claims 5 and 6. We are not persuaded. Appellant’s claim 5 and claim 6, which depends from claim 5, are directed to a method for reducing the accumulation of beta amyloid Ap42 peptide deposits in the brain of a patient suffering from a disease associated with the accumulation of beta amyloid Ap42 peptide deposits in the brains, such as Alzheimer’s disease, wherein the method comprises, inter alia, administering to said patient an effective amount of an antibody, or an antigen-binding fragment thereof that specifically binds to SEQ ID NO:[]3 and selectively inhibits beta amyloid Ap42 peptide deposition in the patient (see App. Br. 20). Examiner finds that Schenk ’880 and Schenk ’686 both disclose mAh 21F12, which binds a peptide having SEQ ID NO: 3 (see FF 4 and 7). Schenk ’880 and Schenk ’686, however, both disclose that the 21F12 mAh was “not efficacious in vivo” (FF 5 and 8). Thus, Examiner failed to establish an evidentiary basis on this record to support a finding that either 7 Chain defines the acronym “PAPP” as “P-amyloid precursor protein” (Chain 13). 10 Appeal 2015-004503 Application 14/026,374 of Schenk ’880 or Schenk ’686 teach a method of reducing the accumulation of beta amyloid Ap42 peptide deposits in the brain of a patient suffering from a disease associated with the accumulation of beta amyloid Ap42 peptide deposits in the brains, which comprises the administration of an antibody that specifically binds to SEQ ID NO: 3 and is efficacious in vivo, such that the antibody will selectively inhibit beta amyloid Ap42 peptide deposition in the patient (see App. Br. 7 (the “2IF 12 (monoclonal antibody specific for AP33-42). . . w[as] not efficacious in vivo”); see also id. at 11— 12; FF 5 and 8). The rejection over Chaim The claims are not separately argued and, therefore, stand or fall together. Appellant’s claim 5 is representative. Examiner finds that Chain teaches the subject matter of Appellant’s claim 5 (Ans. 3^4; FF 9—15). Chain teaches an antibody that specifically targets the C-terminus of the amyloid P-peptide Api-42 and that Ap42’s C-terminus differs from other Ap-peptides (see e.g., FF 12—14). Therefore, we are not persuaded by Appellant’s contention that “Chain does not teach an antibody or an antigen binding fragment thereof that binds to SEQ ID NO:[]3, and that binds to Ap42, but that does not bind to Ap40” (App. Br. 10; Reply Br. 4). See In re Best, 562 F.2d 1252, 1255 (CCPA 1977) (“Where, as here, the claimed and prior art products are identical or substantially identical, or are produced by identical or substantially identical processes, the PTO can require an applicant to prove that the prior art products do not necessarily or inherently possess the characteristics of his claimed product.”). On this record, Appellant failed to establish an evidentiary basis to support a finding that 11 Appeal 2015-004503 Application 14/026,374 Chain’s antibody that specifically targets the C-terminus of the amyloid P- peptide Api-42 does not inherently possess the properties required by Appellant’s claim 5. In addition to teaching an antibody that specifically targets the C- terminus of the amyloid P-peptide Api-42; Chain teaches a method of reducing P amyloid peptide deposits (see, e.g., FF 9-11). Appellant failed to establish an evidentiary basis on this record to support a finding that Chain’s antibody would not reduce the accumulation of Ap42 deposits when used in Chain’s method. See Best, 562 F.2d at 1255. Therefore, we are not persuaded by Appellant’s contention that “Chain does not teach a method for reducing the accumulation of Ap42 deposits” (App. Br. 10; Reply Br. 4). CONCLUSION OF LAW The preponderance of evidence on this record fails to support Examiner’s finding that Schenk ’880 or Schenk ’686 teaches Appellant’s claimed invention. The rejection of claims 5 and 6 under 35 U.S.C. § 102(b) as anticipated by Schenk ’880 is reversed. The rejection of claims 5 and 6 under 35 U.S.C. § 102(b) as anticipated by Schenk ’686 is reversed. The preponderance of evidence on this record supports Examiner’s finding that Chain teaches Appellant’s claimed invention. The rejection of claim 5 under 35 U.S.C. § 102(b) as anticipated by Chain is affirmed. Claim 6 is not separately argued and falls with claim 5. 12 Appeal 2015-004503 Application 14/026,374 Obviousness: ISSUE Does the preponderance of evidence relied upon by Examiner support a conclusion of obviousness? FACTUAL FINDINGS (FF) FF 16. Chain discloses that “[tjhose of skill in the art will appreciate that a cysteine residue can be added to the end of the [] immunogenic peptides opposite from the end corresponding to the free N-terminus or the free C- terminus of Ap peptides to facilitate coupling to a carrier protein,” such as “keyhole limpet hemocyanin (KLH)” (Chain | 80; see Ans. 5). FF 17. Chain discloses that “[f]or the production of antibodies, [] hosts including [] humans [] may be immunized by injection with the relevant epitope or with any fragment or oligopeptide thereof, which has immunogenic properties” and KLH may be used as an adjuvant to increase the immunological response (Chain | 82; see Ans. 5). ANALYSIS Based on Chain, Examiner concludes that, at the time Appellant’s invention was made, it would have been prima facie obvious “to have modified Chain’s disclosed therapeutic method of passive immunization, comprising the administration of anti-Ap42 specific antibodies, by instead actively immunizing a patient by administering an immunogenic conjugate vaccine comprising an Ap peptide conjugated to KLH for the treatment of Alzheimer’s disease, wherein the Ap peptide is AP33-42” (Ans. 5; see id. at 5-6; see FF 9-17). As discussed above, Chain discloses antibodies that specifically target Ap42 and teaches that such antibodies will effectively reduce Ap42 13 Appeal 2015-004503 Application 14/026,374 deposition in a patient (FF 9-15). Therefore, we are not persuaded by Appellant’s contention to the contrary (App. Br. 14). A prior art reference is available for all that it discloses and is not limited to its preferred or exemplified embodiments. See In re Lamberti, 545 F.2d 747, 750 (CCPA 1976). Therefore, we are not persuaded by Appellant’s contention that “Chain does not exemplify antibodies produced using SEQ ID NO:[]3” (App. Br. 14; see also Reply Br. 7). For the same reason, we are not persuaded by Appellant’s contention that Chain fails to “provide a reasonable expectation of success for active immunization with SEQ ID NO:[]3 conjugated to KLH,” because Chain does not exemplify active immunization with SEQ ID NO: 3 conjugated to KLH (see App. Br. 14; Reply Br. 7). Chain discloses the production of antibodies to the C-terminus of A0- peptides, including Ap42; discloses that Ap-peptides differ at their C- terminal end; and that Ap-peptides can be designed for targeting Apx42 species (see e.g., FF 12—14). Therefore, we are not persuaded by Appellant’s contention that Chain fails to make obvious antibodies that bind Ap42 but “do not bind to beta amyloid Ap40 peptide” or the administration of “any peptides for treating a disease characterized by the accumulation of Ap42 deposits in the brain of a patient” (App. Br. 14; see Reply Br. 6—7; cf. FF 9-17). Appellant failed to establish that Chain’s disclosed methodology is the same as that of Schenk ’880. Therefore, we are not persuaded by Appellant’s contentions regarding Schenk ’880 or Schenk ’686 (App. Br. 14—15; see also Reply Br. 7). For the same reasons, we are not persuaded by 14 Appeal 2015-004503 Application 14/026,374 Appellant’s reliance on the Barrio Declaration8 to suggest that, despite Chain’s disclosure, it would have been surprising and unexpected that the administration of a peptide having SEQ ID NO: 3 conjugated with KLH protein would have resulted in the production of antibodies that specifically bind to Ap42 and that such antibodies would effectively reduce A042 amyloid deposition (App. Br. 15; Reply Br. 7—8). In this regard, we are not persuaded by Barrio’s statement that Chain does not disclose “antibodies generated using any specific fragments” (see Barrio Dec. ]f 8; cf FF 12—14). Further, for the reasons set forth above, we are not persuaded by Barrio’s statement that Chain’s use of Ap-peptide-KLH conjugates to make antibodies useful to treat a subject having Alzheimer’s disease or another disease or disorder characterized by amyloid P deposition, comprising the step of administering an antibody molecule which is targeted to P amyloid peptide or to [a] fragment thereof [] cannot be extrapolated to a teaching of [a] method of treating Alzheimer’s disease comprising administering [] Ap[42] peptides or antibodies to specific epitopes of Ap[42] peptide. (Barrio Dec. 17; see also id. 1 5; App. Br. 15—16; Reply Br. 7—8; cf. FF 9— 17.) Notwithstanding Appellant and Barrio’s assertions to the contrary, Chain discloses the immunization of humans with an Ap42 peptide conjugated to KFH for the production of antibodies that specifically target Ap42 for the treatment of amyloid deposits in a human brain (FF 9—17). Therefore, we are not persuaded by Appellant’s contention that Chain fails to make obvious the administration of a peptide, such as “SEQ ID NO:[]3 8 Declaration of Manuel Sarasa Barrio, signed February 4, 2014 (hereinafter “Barrio Declaration” or “Barrio Dec.”). 15 Appeal 2015-004503 Application 14/026,374 conjugated to [KLH] for the production of antibodies that specifically recognize Ap42 and effectively reduce Ap42 deposition, wherein the antibodies do not bind to Ap40” (App. Br. 15; see Reply Br. 7—8). As explained above, Appellant fails to establish an evidentiary basis on this record to support a conclusion that Chain fails to make obvious the subject matter of Appellant’s claim 1 (see FF 9—17; cf. App. Br. 15—20). CONCLUSION OF LAW The preponderance of evidence relied upon by Examiner supports a conclusion of obviousness. The rejection of claim 1 under 35 U.S.C. § 103(a) as unpatentable over Chain is affirmed. Claim 2 is not separately argued and falls with claim 1. TIME PERIOD FOR RESPONSE No time period for taking any subsequent action in connection with this appeal may be extended under 37 C.F.R. § 1.136(a). AFFIRMED 16 Copy with citationCopy as parenthetical citation