Ex Parte Niklason et al

Patent Trial and Appeal Board

Jun 6, 2018

12784235 (P.T.A.B. Jun. 6, 2018)

UNITED STA TES p A TENT AND TRADEMARK OFFICE
APPLICATION NO. FILING DATE
121784,235 05/20/2010
58249 7590 06/08/2018
COOLEYLLP
ATTN: IP Docketing Department
1299 Pennsylvania Avenue, NW
Suite 700
Washington, DC 20004
FIRST NAMED INVENTOR
Laura E. Niklason
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
ATTORNEY DOCKET NO. CONFIRMATION NO.
HMCY-004001US
322168-2081
8393
EXAMINER
ROMEO, DAVIDS
ART UNIT PAPER NUMBER
NOTIFICATION DATE DELIVERY MODE
06/08/2018 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):
zIPPatentDocketingMailbox US @cooley.com
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
BEFORE THE PATENT TRIAL AND APPEAL BOARD
Ex parte LAURA E. NIKLASON, YULING LI, HEATHER PRICHARD,
SHANNON DAHL, and JULIANA BLUM
Appeal2016-007943
Application 12/784,235 1
Technology Center 1600
Before DONALD E. ADAMS, ULRIKE W. JENKS, and DAVID COTTA,
Administrative Patent Judges.
ADAMS, Administrative Patent Judge.
DECISION ON APPEAL
This Appeal under 35 U.S.C. § 134(a) involves claims 1, 4---6, 8, 9, 11,
12, 15-17, 30, 31, 33, 35, 57, 59, 61, 62, and 64---69 (Br. 2). 2 Examiner
entered rejections under the written description provision of 35 U.S.C.
§ 112, first paragraph, 35 U.S.C. § 102(b), 35 U.S.C. § 103(a), and
obviousness-type double patenting. We have jurisdiction under 35 U.S.C.
§ 6(b ).
We AFFIRM.
1 Appellants identify "Humacyte, Inc." as the real party in interest (Br. 2).
2 Pending "claims 10, 13-14, 34, and 36-56 [stand] withdrawn [from
consideration] as directed to non-elected subject matter" (Br. 2).
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Application 12/784,235
STATEMENT OF THE CASE
Appellants' disclosure "relates generally to compositions comprising
elastin" (Spec. i-f 2). Claims 1 and 68 are representative and reproduced
below:
1. An injectable composition consisting of isolated non-human
elastin and a pharmaceutically acceptable carrier wherein the
non-human elastin has a molecular weight greater than 100 kDa
and is substantially insoluble in water,
wherein the isolated non-human elastin comprises an
amino acid concentration selected from the group consisting of
an alanine residue concentration that is at least 200/1000 total
residues, a valine residue concentration that is at least 70/1000
total residues, or both an alanine residue concentration that is at
least 200/1000 total residues and a valine residue concentration
that is at least 70/1000 total residues,
wherein the non-human elastin is isolated from non-
human tissue without the use of a protease by decellularizing
the tissue using a salt solution and exposing the decellularized
tissue to a strong base solution followed by exposure to a
primary alcohol, and
wherein said composition does not induce calcification,
fibrosis or encapsulation in vivo upon administration to a
subject.
(Br. 20.)
68. A composition comprising isolated non-human elastin and
a pharmaceutically acceptable carrier wherein the non-human
elastin is isolated from non-frozen, non-human vascular tissue
that has not been previously frozen, has a molecular weight
greater than 100 kDa and is substantially insoluble in water,
wherein the isolated non-human elastin comprises an
amino acid concentration selected from the group consisting of
an alanine residue concentration that is at least 200/1000 total
residues, a valine residue concentration that is at least 70/1000
total residues, or both an alanine residue concentration that is at
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least 200/1000 total residues and a valine residue concentration
that is at least 70/1000 total residues,
wherein the composition does not comprise isolated
collagen,
wherein the non-human elastin is isolated from the non-
frozen, non-human vascular tissue without the use of a protease
by decellularizing the tissue using a salt solution and exposing
the decellularized tissue to a strong base solution followed by
exposure to a hydrophobic solvent, and
wherein said composition does not induce calcification,
fibrosis or encapsulation in vivo upon administration to a
subject.
(Id. at 26-27.)
The claims stand rejected as follows:
I. Claims 1, 4---6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61,
62, and 64---69 stand rejected under the written description
provision of 35 U.S.C. § 112, first paragraph.
II. Claims 1, 4, 6, 8, 16, 30, 31, 57, 59, 61, 62, and 64--69 stand
rejected under 35 U.S.C. § 102(b) as anticipated by Keating, 3 as
evidenced by Daamen 2001. 4
III. Claims 1, 4---6, 8, 9, 11, 12, 16, 17, 30, 31, 57, 59, 61, 62, and
64---69 stand rejected under 35 U.S.C. § 103(a) as unpatentable
over the combination of Keating, Daamen 2001, and Daamen
2003. 5
3 Keating et al., US 7,125,837 Bl, issued Oct. 24, 2006.
4 W.F. Daamen et al., Comparison of Five Procedures for the Purification of
Insoluble Elastin, 22 Biomaterials 1997-2005 (2001 ).
5 W.F. Daamen et al., Preparation and Evaluation of Molecularly-Defined
Collagen-Elastin-Glycosaminoglycan Scaffolds for Tissue Engineering, 24
Biomaterials 4001--4009 (2003).
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IV. Claims 1, 4---6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61,
62, and 64---69 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Keating, Daamen 2001,
Daamen 2003, Sclafani, 6 Gloyer, 7 and Berg. 8
V. Claims 1, 4---6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61,
62, and 64---69 stand rejected under 35 U.S.C. § 103(a) as
unpatentable over the combination of Keating, Daamen 2001,
Daamen 2003, Sclafani, Gloyer, Berg, and Gregory. 9
VI. Claims 1, 4---6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61,
62, and 64---69 stand rejected under the judicially created
doctrine of obviousness-type double patenting as being
unpatentable over the claims ofNiklason. 10
Rejection I:
ISSUE
Does the preponderance of evidence on this record support
Examiner's finding that Appellants' Specification fails to provide written
descriptive support for the claimed invention?
6 Anthony P. Sclafani, MD, et al., Evaluation of Acellular Dermal Graft in
Sheet (AlloDerm) and Injectable (Micronized AlloDerm) Forms for Soft
Tissue Augmentation, 2 Arch Facial Plast Surg. 130-136 (2000).
7 Gloyer, US 4,832,693, issued May 23, 1989.
8 Berg et al., US 7,192,984 B2, issued Mar. 20, 2007.
9 Gregory, US 6,372,228 Bl, issued Apr. 16, 2002.
10 Niklason et al., US 8,198,245 B2, issued June 12, 2012.
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FACTUAL FINDINGS (FF)
FF 1. Appellants disclose a "process for isolating elastin [that] involves a
salt-based decellularization step, followed by boiling in 0.1 N NaOH and
then extraction in hydrophobic solvents" (Spec. i-f 97).
ANALYSIS
Examiner finds that Appellants' Specification "describe[s] a single,
specific procedure for the isolation from non-frozen aorta of an elastin with
claimed properties," wherein tissue is "[ e ]xposed to 'a salt solution,' 'a
strong base' and 'a hydrophobic solvent,"' which "are highly generalized
generic concepts" and, "[t]hus, [Appellants'] claim[s] [are] directed to a
genus of elastin species produced by a highly generalized generic process"
(Ans. 30). Examiner further finds "that even a slight modification of [the]
elastin purification procedure will yield an elastin composition having
significantly different chemical properties" (id.). Thus, Examiner finds that
"[ o ]ne of skill in the art would reasonably conclude that the disclosure fails
to provide a representative number of elastin species with the claimed
properties and produced by the recited process to describe the genus" (id.).
We are not persuaded.
Appellants' claims require that non-human elastin is isolated from
non-human tissue, which may be non-frozen vascular tissue, without the use
of a protease by decellularizing the tissue using a salt solution and exposing
the decellularized tissue to a strong base solution followed by exposure to a
hydrophobic solvent, such as a primary alcohol (see Br. 20-21 and 27).
Appellants' Specification provides written descriptive support for this
process of isolating elastin (see FF 1). We recognize Examiner's concern
that the foregoing process is a "highly generalized generic concept" that may
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result in the isolation of a genus of elastin species, which may or may not
exhibit the elastin properties required by Appellants' claimed invention (see
Ans. 30). Examiner and Appellants appear to agree that "even a slight
modification of' the foregoing elastin isolation "procedure will yield an
elastin composition having significantly different chemical properties" than
those required by Appellants' claims (see id.; cf App. Br. 10 ("Daamen
2001 discloses 5 different purification procedures, each of which yielded
elastin compositions with distinct chemical properties")). Examiner,
however, failed to establish an evidentiary basis on this record to support a
finding that a process for isolating non-human elastin that falls within the
scope of Appellants' claimed invention will fail to yield a non-human elastin
composition within the scope of Appellants' claims. Thus, we find that
Appellants' Specification provides written descriptive support for
Appellants' claimed invention, despite the breadth of the claim.
CONCLUSION
The preponderance of evidence on this record fails to support
Examiner's finding that Appellants' Specification fails to provide written
descriptive support for the claimed invention. The rejection of claims 1, 4--
6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61, 62, and 64--69 under the
written description provision of 35 U.S.C. § 112, first paragraph is reversed.
Rejection II:
ISSUE
Should the anticipation rejection on this record be summarily affirmed
by the Board?
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ANALYSIS
"If a ground of rejection stated by the examiner is not addressed in the
appellant's brief, appellant has waived any challenge to that ground of
rejection and the Board may summarily sustained it." Manual of Patent
Examining Procedure§ 1205.02. Appellants do not address the anticipation
rejection on this record. Therefore, we summarily affirm the anticipation
rejection on this record.
CONCLUSION
The rejection of claims 1, 4, 6, 8, 16, 30, 31, 57, 59, 61, 62, and 64--69
under 35 U.S.C. § 102(b) as anticipated by Keating, as evidenced by
Daamen 2001, is summarily affirmed.
Rejection V:
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness?
FACTUAL FINDINGS (FF)
We adopt Examiner's findings concerning the scope and content of
the prior art (Ans. 7-14, which incorporate by reference Examiner's findings
at Ans. 3-6), and provide the following findings for emphasis.
FF 2. Keating "relates to compositions and methods for delivery of elastin-
based compositions including elastic fibers, elastin, tropoelastin, or
fragments thereof' (Keating 1: 21-24; see Final Act. 11 3 and 12).
FF 3. Keating discloses that although "the elastin-based composition
includes a soluble elastin polypeptide" in preferred embodiments; "[ e ]lastin-
11 Office Action mailed November 20, 2014.
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based compositions can be employed ... in soluble or insoluble ... form"
(Keating 3: 15-18 and 26-27 (emphasis added)).
FF 4. Keating discloses that injectable compositions are within the scope
of its disclosure, wherein "[ f]or parenteral administration, the active agent
[i.e. elastin composition,] is dissolved (e.g., soluble elastin) or suspended in
a pharmaceutical carrier and administered as either a solution or a
suspension" (Keating 7: 6-10 and 18: 52-55; see Final Act. 5 and 12).
FF 5. Keating discloses that"[ e ]lastin-based compositions can be derived
from ... any vertebrate. However, for most applications, these proteins are
derived from ... mammalian sources, such as, for example, porcine, bovine,
equine, or primate sources. For administration to humans, human elastin
polypeptides (or variants thereof) are preferred" (Keating 13: 65 - 14: 4; see
Final Act. 3--4 and 12).
FF 6. Keating discloses that "elastin can be obtained from natural sources
using conventional techniques" (Keating 15: 38-39; see Final Act. 4 and
12).
FF 7. Keating discloses a process of isolating elastin from tissue, such as a
blood vessel, wherein:
The source tissue can be frozen,[ 12J but should be thawed before
isolation of the blood vessel.
[T]he blood vessel is generally rinsed in a physiological saline
solution ... [i.e.,] normal saline (0.9% NaCl), [or] any ofa
number of physiological balanced salt solutions ....
Preferably, the saline solution contains a standard bacteriostatic
agent, such as 0.9% benzyl alcohol.
12 Examiner finds "[ t ]he fact that the source tissue can be frozen implies that
the source tissue can be non-frozen" (Final Act. 4, n. 2).
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After rinsing [in a physiological saline solution], loose
adipose tissue and adventitia are removed from the blood vessel
... , [wherein,] [r]emoval of the adventitia is generally carried
out in a physiological buffered saline solution, preferably one
containing a detergent, such as, for example 0 .1 % Tween- I 00
in PBS.
After loose adventitia is removed, the vessel is washed
briefly in a physiological saline solution to remove residual
blood inside [the tissue's] lumen ....
The blood vessel is then treated with a detergent solution
to lyse and extract cellular material ... [and] washed to remove
the detergent. ...
Detergent treatment is followed by treatment with an
alkaline solution to solubilize and remove collagenous matter.
The alkaline solution is preferably an aqueous solution
containing a base at a concentration of between about 0.1 and
about 6 N[, wherein,] [ s ]uitable bases include, for example, ...
sodium hydroxide ....
A final collagen-removal step is employed to remove the
remaining collagen. Any method that removes collagen and
leaves the elastin matrix intact can be used. Examples include
autoclaving for a short period of time ... or collagenase
treatment. ...
The elastin matrix can be sterilized by any method that
inactivates any endotoxin contaminants without degrading
elastin. Preferably, the matrix is washed with a 70% ethanol
solution. The elastin matrix is then generally stored ... in fresh
30% ethanol solution.
(Keating 16: 41 - 17: 60; see Final Act. 4--5 and 12.)
FF 8. Keating discloses, inter alia, that "vascular smooth muscle cells
migrate towards [recombinantly produced human tropoelastin (elastin)] in a
dose-dependent manner" (Keating 5: 49---65 and 35: 43 - 37: 10; see also id.
32: 1 - 35: 42; cf FF 7).
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FF 9. Examiner relies on Daamen 2001 to establish that insoluble elastin,
produced by conventional protocols, has a molecular weight greater than 100
kDa (Final Act. 5 (citing Daamen 2001 's Fig. 2) and 12; see Daamen 2001
Title ("[ c ]omparison of five procedures for the purification of insoluble
elastin") and Fig. 1 ).
FF 10. Daamen 2001 discloses that "[i]nsoluble elastin preparations tend to
calcify, which may be due to calcium-binding microfibrillar (e.g. fibrillin)"
(Daamen 2001 Abstract).
FF 11. Daamen 2001 discloses that "[ e ]lastin is an important connective
tissue protein in man that provides elasticity to organs, such as lung, aorta,
and ligaments" and further discloses the isolation of insoluble elastin from
"[h]orse ligamentum nuchae" (Daamen 2001§§1and2.1).
FF 12. Examiner finds that although Keating discloses a composition
comprising non-human elastin, "Keating does not [disclose] a composition
further comprising non-human collagen and GAGs" and relies on Daamen
2003 to make up for this deficiency in Keating (Final Act. 7-8 and 12).
FF 13. Examiner finds that the combination of Keating, Daamen 2001, and
Daamen 2003 is "silent with respect to a kit comprising a composition
consisting of or comprising elastin and a pharmaceutically acceptable
carrier, a syringe, a sterile wrapper surrounding the syringe and one or more
reagents" and relies on Sclafani, Gloyer, and Berg to make up for these
deficiencies in the combination of Keating, Daamen 2001, and Daamen
2003 (Final Act. 10-12).
FF 14. Examiner relies on Gregory to disclose that "[ e ]lastin based
materials tend to calcify," but elastin, isolated from a natural source, that has
been "incubated in ethanol, prior to [the] sodium hydroxide digestion [step
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of the isolation process], showed no sign of in vivo calcification at ... six
months" (Final Act. 13).
ANALYSIS
Based on the combination of Keating, Daamen 2001, Daamen 2003,
Sclafani, Gloyer, Berg, and Gregory, Examiner concludes that, at the time
Appellants' invention was made, an injectable composition: (a) consisting
of, or (b) comprising, isolated non-human elastin, that is substantially
insoluble in water, and a pharmaceutically acceptable carrier would have
been prima facie obvious to those of ordinary skill in this art (see Final Act.
12-13; see also id. 3-12; FF 2-7, 9, and 14).
In this regard, Examiner finds that the combination of Keating,
Daamen 2001, Daamen 2003, Sclafani, Gloyer, Berg, and Gregory suggests:
insoluble elastin has a molecular weight of greater than 100 kDa (FF 9); the
isolation of non-human elastin from non-human vascular or non-vascular
tissue (see FF 5-7 and 11); a method of isolating non-human elastin without
the use of a protease, which includes decellularizing the tissue using a salt
solution and exposing the decellularized tissue to a strong base solution
followed by exposure to a hydrophobic solvent, such as a primary alcohol,
which inherently results in the isolation of a non-human elastin that has,
inter alia, an Ala residue concentration that is at least 200/1000 total
residues (see FF 7 and 14); and a composition, of an injectable non-human
elastin and pharmaceutically acceptable carrier, that does not induce
calcification in vivo (FF 14). We recognize Appellants' acknowledgement
that the prior art relied upon by Examiner discloses a composition that
contains an isolated insoluble non-human elastin that comprises 220 Ala
residues per 1000 amino acids, which satisfies the requirement of an alanine
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residue concentration that is at least 200/1000 total residues, as set forth in
Appellants' independent claims 1 and 68 (see Br. 10; Ans. 4--5; cf Br. 20
and 26-27; Niklason Dec. i-fi-18 and 9; Br. 15).
We find no error in Examiner's findings or conclusion of obviousness.
Examiner found that Hinds, as relied upon by Appellants, was not
timely presented on this record and, therefore, Examiner did not consider
Hinds (Ans. 2-3; cf Br. 6). We agree with Examiner's position and likewise
do not address Appellants' contentions relating to Hind.
For the foregoing reasons, we are not persuaded by Appellants'
contention that the combination of prior art relied upon by Examiner fails to
disclose "an injectable composition comprising non-human elastin that has a
molecular weight greater than 100 kDa, is substantially insoluble in water,
and has the claimed alanine ... residue concentration[]" (Br. 7).
Appellants fail to provide persuasive evidence or argument to support
a contention that the combination of prior art relied upon by Examiner
"describes a method of elastin isolation that is distinct from the steps used to
isolate the claimed elastin" (Br. 7; see also id. at 8; cf FF 7).
Notwithstanding Appellants' unsupported contention to the contrary,
Keating discloses a process of isolating elastin, from a source tissue that may
be a non-human tissue, wherein the method does not use a protease, but
instead comprises decellularizing the tissue using a salt solution and
exposing the decellularized tissue to a strong base solution followed by
exposure to a primary alcohol (see FF 7; cf Br. 20). Examiner does not rely
upon Daamen 2001 or Daamen 2003 to teach a method of preparing
insoluble non-human elastin (FF 1-7, 9, and 12). Therefore, we are not
persuaded by Appellants' contentions regarding the elastin preparation
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methodology disclosed in either or both of Daamen 2001 and Daamen 2003,
or the properties of the compositions prepared by either or both of Daamen
2001 and Daamen 2003 (see Br. 9--10; see also Niklason Dec. 13 i-f 4; Br. 15-
16). Because, Keating discloses a method of preparing insoluble elastin that
does not comprise collagen, we are not persuaded by Appellants' contention
that the prior art relied upon by Examiner fails to suggest "an elastin
composition that does not comprise collagen" (FF 7; cf Br. 11 ).
Keating discloses compositions that contain insoluble elastin (see FF
3; see also FF 9 (Daamen 2001, disclosing the isolation of insoluble elastin
from source tissue)). Therefore, we are not persuaded by Appellants'
contention that the combination of prior art relied upon by Examiner relates
to compositions comprising soluble elastin (Br. 7). In addition, Keating
discloses both elastin and elastin fragments (see FF 2). Daamen 2001
discloses the molecular weight of insoluble elastin as greater than 100 kDa
(FF 9). Therefore, we are not persuaded by Appellants' contention that the
combination of prior art relied upon by Examiner fails to disclose an elastin
having a molecular weight greater than 100 kDa (Br. 7-8; see id. at 16).
Keating discloses a variety of protocols that are useful in obtaining
elastin, including the use of recombinant techniques, solid-phase peptide
synthesis, and isolation of elastin from natural sources (see generally FF 6-
8). Keating also discloses that "vascular smooth muscle cells migrate
towards [recombinantly produced human tropoelastin ( elastin)] in a dose-
dependent manner" (FF 8). As Examiner points out, however, Keating's
observations regarding cell migration were in the context of elastin prepared
from methodologies other than isolation from natural sources using
13 Declaration of Laura E. Niklason, M.D., Ph.D., signed Sept. 13, 2013.
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conventional techniques (see Ans. 6-7). In this regard, we note that the art
relied upon by Examiner recognized that elastin's properties are affected by
the manner in which it is prepared (see FF 14 (Examiner relies on Gregory
to disclose that "[ e ]lastin based materials tend to calcify," but elastin,
isolated from a natural source, that has been "incubated in ethanol, prior to
[the] sodium hydroxide digestion [step of the isolation process], showed no
sign of in vivo calcification at ... six months"); see also Br. 13 ("Gregory
describes methods of producing elastins and elastin-based biomaterials that
have a reduced level of calcification")). Thus, we are not persuaded by
Appellants' contentions regarding Keating's disclosure of results obtained
with elastin prepared from methodologies other than the isolation of elastin
from natural sources (see Br. 8; see also Niklason Dec. i-f 5 (Appellants'
"composition ... compris[es] isolated non-human elastin and a
pharmaceutically acceptable carrier does not induce calcification in vivo in a
human"); Niklason Dec. i-f 7; Br. 14--15). To the contrary, as discussed
above, the combination of references relied upon by Examiner makes
obvious a composition, of an injectable isolated non-human elastin and
pharmaceutically acceptable carrier, which does not induce calcification
upon administration in vivo.
The combination of prior art relied upon by Examiner discloses the
isolation of elastin from "mammalian sources, such as, for example, porcine,
bovine, equine, or primate sources" (FF 5). In addition, we note that
Appellants' claims 1 and 68 are not method claims, but instead relate to
compositions and require only that the elastin is non-human elastin and does
not induce calcification, fibrosis, or encapsulation in vivo upon
administration to an undefined subject (see Br. 20 and 26-27). Therefore,
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we are not persuaded by Appellants' contentions or Declarant' s statements
regarding human elastin, implantation in allogenic or xenogeneic hosts,
methods of soft tissue augmentation, fibrosis induction, or host
inflammatory cell infiltration (see Br. 8-9; see also Niklason Dec. i-fi-16 and
10; Br. 14--15). Simply stated, Appellants' contentions and Declarant's
statements are not commensurate in scope with their claims.
For the reasons set forth above, we find no deficiency in Examiner's
combination of Keating, Daamen 2001, Daamen 2003, and Gregory.
Therefore, we are not persuaded by Appellants' contention that each of
Sclafani, Gloyer, and Berg fail to remedy such a deficiency (see App. Br.
11-13).
We are not persuaded by Appellants' contentions that Gregory fails to
disclose a "non-human elastin comprising the claimed alanine and/or valine
concentrations" or "an injectable composition," which fails to account for
the contributions of Keating, Daamen 2001, Daamen 2003, Sclafani, Gloyer,
and Berg to the combination of Keating, Daamen 2001, Daamen 2003,
Sclafani, Gloyer, Berg, and Gregory (see Br. 13-14; see also Niklason Dec.
i-f 11 ). Further, the process for isolating non-human elastin, as set forth in
Appellants' claims, excludes the use of a protease, but includes a salt
solution treatment step, a strong base solution treatment step, and a
hydrophobic solvent, such as a primary alcohol, treatment step (see Br. 20
and 26-26). The non-human elastin isolation process set forth in
Appellants' claims, however, does not exclude additional steps not recited in
the elastin isolation process recited in Appellants' claims, for example the
addition of a ethanol treatment step prior to treatment with a strong base
solution, as suggested by Gregory (FF 14) followed by exposure to a
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hydrophobic solvent, such as a primary alcohol as suggested by Keating (FF
7). Therefore, we are not persuaded by Appellants' contentions regarding
the timing of Gregory's ethanol step or intimation that the inclusion of an
ethanol treatment step prior to exposing non-human elastin to a hydrophobic
solvent, such as a primary alcohol, would preclude exposing the isolated
insoluble non-human elastin to a primary alcohol, which serves as a storage
solution, as suggested by Keating (FF 7), as a last step in the isolation
process (see Br. 13; see also Niklason Dec. i-f 12).
For the foregoing reasons, we are not persuaded by Appellants'
contention that the prior art relied upon by Examiner is not properly
combinable or that when combined "would not have led to the claimed
elastin compositions of the instant invention" (Br. 11; see id. at 16-17).
CONCLUSION
The preponderance of evidence relied upon by Examiner supports a
conclusion of obviousness. The rejection of claims 1 and 68 under 35
U.S.C. § 103(a) as unpatentable over the combination of Keating, Daamen
2001, Daamen 2003, Sclafani, Gloyer, Berg, and Gregory is affirmed.
Claims 4--6, 8, 9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61, 62, 64--67, and 69
are not separately argued and fall with claims 1 and 68 respectively.
Rejections III & IV:
Rejections III and IV are cumulative to Rejection V. Therefore, we
vacate rejections III and IV in favor of cumulative rejection V.
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Re} ection VI:
ISSUE
Does the preponderance of evidence relied upon by Examiner support
a conclusion of obviousness-type double patenting?
FACTUAL FINDINGS (FF)
FF 15. Niklason claims:
An injectable composition comprising isolated human elastin
and a pharmaceutically acceptable carrier in solution, wherein
said human elastin is isolated from human vascular tissue,
which has not been frozen, by decellularizing the vascular
tissue, expositing said decellularized tissue to a strong base and
subsequently exposing the tissue to a primary alcohol and,
wherein the human elastin is substantially insoluble in water
with a molecular weight greater than 100 kDa.
(Niklason 25: 50-57.)
ANALYSIS
Based on the claims of Niklason, Examiner concludes that, at the time
Appellants' invention was made, it would have been prima facie obvious to
"use non-human sources for [Niklason's] elastin because non-human sources
would be plentiful and readily available" (Final Act. 16). We find no error
in Examiner's conclusion.
Appellants' claimed invention is not directed to a method of
treatment, nor does Appellants' claimed composition require the
composition be administered to a subject of a particular species, i.e. human.
The same is true of Niklason' s claimed invention. Therefore, we are not
persuaded by Appellants' contentions regarding "compositions suitable for
use in humans," "biocompatib[ility] with a xenogeneic host," "xenogeneic or
allogeneic elastin-containing compositions," or immunogenicity in human
recipients (Br. 17-18).
17
Appeal2016-007943
Application 12/784,235
CONCLUSION
The preponderance of evidence relied upon by Examiner supports a
conclusion of obviousness-type double patenting. The rejection of claim 1
under the judicially created doctrine of obviousness-type double patenting as
being unpatentable over the claims ofNiklason is affirmed. Claims 4---6, 8,
9, 11, 12, 15-17, 30, 31, 33, 35, 57, 59, 61, 62, and 64--69 are not separately
argued and fall 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
18