Ex Parte Sarasa Barrio

Patent Trial and Appeal Board

Mar 21, 2017

14026374 (P.T.A.B. Mar. 21, 2017)

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.
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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.
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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.
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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
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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.
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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.
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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).
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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).
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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
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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).
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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
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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.
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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
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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
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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.”).
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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
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