Ex Parte Haab et al

Board of Patent Appeals and Interferences

Aug 10, 2009

09550303 (B.P.A.I. Aug. 10, 2009)

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.
09/550,303 04/14/2000 Brian Haab STAN-128 9147
77974 7590 08/10/2009
Stanford University Office of Technology Licensing
Bozicevic, Field & Francis LLP
1900 University Avenue
Suite 200
East Palo Alto, CA 94303
EXAMINER
FORMAN, BETTY J
ART UNIT PAPER NUMBER
1634
MAIL DATE DELIVERY MODE
08/10/2009 PAPER
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.
PTOL-90A (Rev. 04/07)
UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte BRIAN HAAB, PATRICK BROWN and TIDHAR SHALON
__________

Appeal 2008-0012
Application 09/550,303
Technology Center 1600
__________

Decided: August 10, 2009
__________

Before TONI R. SCHEINER, DEMETRA J. MILLS, and ERIC GRIMES,
GRIMES, Administrative Patent Judges.

GRIMES, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to a
polypeptide microarray. The Examiner has rejected the claims as anticipated
by or obvious in view of the prior art. We have jurisdiction under 35 U.S.C.
§ 6(b). We affirm in part.
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STATEMENT OF THE CASE
The Specification discloses “a substrate with a surface having a
microarray of at least 103 distinct polynucleotide or polypeptide biopolymers
in a surface area of less than about 1 cm2” (Spec. 3: 26-28). “The substrate
includes, in one aspect, a glass support, a coating of a polycationic polymer,
such as polylysine . . . , and an array of distinct biopolymers electrostatically
bound non-covalently to said coating, wherein each distinct biopolymer is
disposed at a separate, defined position” (id. at 4: 2-6).
Claims 10, 13-16, 18, 31, and 33-37 are pending and on appeal.
Claims 10, 31, and 36 are representative and read as follows:
10. A microarray of discrete polypeptides on a slide, wherein each
polypeptide is of at least 50 amino acids in length, wherein said microarray
comprises 1000 or more discrete regions of distinct polypeptide per cm2 of
slide wherein discrete regions have a diameter of from 20 to 200 µm,
produced by the method of:
(a) loading an aqueous solution of a selected polypeptide of at least 50
amino acids in length in a reagent-dispensing device having an elongate
capillary channel adapted to hold a quantity of the reagent solution and
having a tip region at which the solution in the channel forms a meniscus,
(b) tapping the tip of the dispensing device against a surface of a
planar solid support at a defined position, with an impulse effective to break
the meniscus in the capillary channel and deposit a selected volume between
0.002 and 2 nl of solution of the surface of the planar solid support, and
(c) repeating steps (a) and (b) until said microarray is formed.

31. A microarray of discrete polypeptides on a slide, wherein each
polypeptide is of at least 50 amino acids in length and wherein said
microarray comprises 1000 or more discrete regions of distinct polypeptide
per cm2 of slide, and wherein discrete regions have a diameter of from 20 to
200 µm.

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36. The microarray of polypeptides according to Claim 31, wherein
said slide comprises a cationic film which binds said polypeptide.

The claims stand rejected as follows:
• Claims 31 and 33-35 under 35 U.S.C. § 102(e) as anticipated by
Winkler1 (Ans. 3);
• Claims 10, 13-15, 18, 31, 33-35, and 37 under 35 U.S.C. § 102(e) as
anticipated by Barrett2 (Ans. 5);
• Claims 16 and 36 under 35 U.S.C. § 103(a) as obvious in view of
Barrett and Van Ness3 (Ans. 13);
• Claims 10, 13-15, 18, 31, and 33-35 under 35 U.S.C. § 103(a) as
obvious in view of Beattie,4 Zubay,5 and Chang6 (Ans. 6); and
• Claims 16 and 36 under 35 U.S.C. § 103(a) as obvious in view of
Beattie, Zubay, Chang, and Van Ness (Ans. 12).
ANTICIPATION: WINKLER
Issue
The Examiner finds that Winkler discloses a product meeting all of
the limitations of claims 31 and 33-35 (Ans. 3).
Appellants contend that Winkler describes “methods of synthesizing
polymers in situ on a substrate” (Appeal Br. 5). Appellants cite Fodor7 as

1 Winkler et al., US 5,677,195, Oct. 14, 1997
2 Barrett et al., US 5,252,743, Oct. 12, 1993
3 Van Ness et al. US 5,667,976 Sept. 16, 1997
4 Beattie, US 5,843,767, Dec. 1, 1998
5 Geoffrey Zubay, Biochemistry 3rd ed., 964-966, (1993)
6 Chang, US 4,829,010, May 9, 1989
7 Fodor et al., 251 Science 767-773 (1991).
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evidence that in situ synthesis provides coupling yields of 85-95% per cycle,
and calculate that synthesis of a polypeptide 50 amino acids long would
result in only 0.5% of the synthesized polypeptide having the desired
sequence (Appeal Br. 9). Appellants conclude that “synthesis of a 50-mer
using [Winkler’s] method will result in a heterogeneous mixture of
polypeptides, only 5 molecules in a 1000 of which will have the correct
sequence” (id.).
The Examiner does not dispute Appellants’ calculations regarding in
situ synthesis, but contends that “[t]he claims merely require polypeptides of
at least 50 amino acids positioned in discrete regions. The claims do not
define the composition of the polypeptides on the microarray or within any
give[n] region.” (Ans. 4.)
The issue with respect to this rejection is: Did the Examiner err in
concluding that claim 31 reads on the product disclosed by Winkler?
Findings of Fact
1. Winkler discloses “[m]ethods and devices for synthesizing high-
density arrays of diverse polymer sequences such as diverse peptides”
(Winkler, col. 2, ll. 15-16).
2. Winkler discloses that “the process may be readily adapted to form
polymers having 3, 4, 5, . . . 50, 75, 100 or more monomers therein” (id. at
col. 17, ll. 55-57).
3. Winkler discloses that “[i]n preferred embodiments, there are at
least about 1000 reaction regions per cm2 of substrate” (id. at col. 18, ll. 48-
49).
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4. Claim 31 is directed to a product that comprises “discrete regions
of distinct polypeptide” (claim 31).
5. The Specification states that it provides “[m]ethods and
compositions . . . for forming a microarray of polypeptide regions on a solid
support, where each region in the array has a known amount of a selected
polypeptide” (Spec. 4: 25-27).
6. The Specification states that “‘[d]istinct biopolymers’, as applied
to the biopolymers forming a microarray, means an array member which is
distinct from other array members on the basis of a different biopolymer
sequence, and/or different concentrations of the same or distinct
biopolymers, and/or different mixtures of distinct or different-concentration
biopolymers” (id. at 7: 12-16).
7. The Specification states that “[t]hus, an array of ‘distinct
polynucleotides’ means an array containing, as its members, (i) distinct
polynucleotides, which may have a defined amount in each member, (ii)
different, graded concentrations of given-sequence polynucleotides, and/or
(iii) different-composition mixtures of two or more distinct
polynucleotides.” (Id. at 7: 17-20.)
8. The Specification describes “embodiments of a substrate having a
microarray of biological polymers carried on the substrate surface, in
particular a microarray of distinct polypeptides” (id. at 15: 8-10).
9. The Specification describes making the microarray embodiments
by depositing “defined volumes of distinct biopolymers” on a derivatized
glass slide (id. at 16: 21-22).
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10. The Specification states that “in a preferred embodiment, the
biopolymers have lengths of at least about 50 units, e.g., amino acids,
nucleotides, etc., i.e., substantially longer than polymers which can be
formed in high-density arrays by various in situ synthesis schemes” (id. at
17: 5-8).
11. The Specification states that the “polypeptide biopolymers may
comprise polypeptides from any source. . . . Usually the polypeptides on
each discrete region of the array will be substantially pure.” (Id. at 17: 9-
17.)
Principles of Law
[T]he PTO applies to the verbiage of the proposed claims the
broadest reasonable meaning of the words in their ordinary
usage as they would be understood by one of ordinary skill in
the art, taking into account whatever enlightenment by way of
definitions or otherwise that may be afforded by the written
description contained in the applicant’s specification.
In re Morris, 127 F.3d 1048, 1054 (Fed. Cir. 1997).
Analysis
The Examiner does not dispute Appellants’ assertion that using
Winkler’s method to make a product having a 50-amino acid polypeptide
immobilized on a substrate would result in only 0.5% of the desired
polypeptide in the synthesized product; the remaining 99.5% of the
polypeptide in a given region would be a mixture of polypeptides having
different lengths and sequences. The Examiner, however, interprets claim
31 to read on such a product because the claim does not define the
composition of polypeptide in a given region (Ans. 4).
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In our view, the Examiner’s interpretation of claim 31 is broader than
is reasonable when the claim is read in light of the Specification. The
Specification discloses a method of making polypeptide microarrays that
begins with intact polypeptides, which are then deposited onto a substrate.
The Specification also expressly distinguishes the disclosed microarrays
from those that are made by in situ synthesis, like those of Winkler.
When the claims are read in light of the Specification’s definition of
“distinct biopolymers” and the description of the disclosed embodiments,
therefore, a person of ordinary skill in the art would understand claim 31’s
reference to “distinct polypeptides” to mean either a substantially pure
polypeptide, or a defined mixture of specific polypeptides. A skilled worker
would not interpret a “distinct polypeptide” to encompass the undefined
mixtures of polypeptides that would result from using Winkler’s method to
synthesize a 50-amino acid polypeptide in situ.
Conclusion of Law
The Examiner erred in concluding that claim 31 reads on the product
disclosed by Winkler.
ANTICIPATION: BARRETT
Issue
The Examiner has rejected claims 10, 13-15, 18, 31, 33-35, and 37
under 35 U.S.C. § 102(e) as anticipated by Barrett (Ans. 5). The Examiner
finds that Barrett discloses “a microarray of discrete polypeptides on a slide
(Column 8, lines 15-20) wherein each polypeptide is at least 50 amino acids
(e.g. antibody, Abstract), wherein the microarray comprises 1000 or more
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discrete regions of polypeptide/cm2 wherein the regions have a diameter o[f]
20 to 200 µm” (Ans. 5).
Appellants contend that Barrett does not disclose all the elements of
the claimed invention because it “fail[s] to teach a cationic film on a solid
support capable of binding peptide, as claimed in the present invention”
(Appeal Br. 12).
The issue with respect to this rejection is: Have Appellants shown
that the Examiner erred in finding that Barrett discloses the product of claim
31?
Additional Findings of Fact
12. Barrett discloses “methods for forming predefined regions on a
surface of a solid support, wherein the predefined regions are capable of
immobilizing anti-ligands” (Barrett, col. 5, ll. 14-17).
13. Barrett discloses that the “substrate may be . . . slides” (id. at col.
8, ll. 15-19).
14. Barrett discloses that “examples of anti-ligands that can be
investigated by this invention include . . . immunoglobulins, e.g.,
monoclonal and polyclonal antibodies” (id. at col. 20, ll. 52-60).
15. Barrett discloses that its methods “make use of caged binding
members attached to the surface to enable selective activation of the
predefined regions. The caged binding members are converted to binding
members ultimately capable of binding anti-ligands upon selective activation
of the predefined regions.” (Id. at col. 5, ll. 17-22.)
16. Barrett discloses that “selected regions of the surface may be
irradiated to provide activated binding members” (id. at col. 18, ll. 57-58).
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17. Barrett discloses that “[i]n preferred embodiments, the exposed
area is less than about 10,000 µm2 or, more preferably, less than about 100
µm2. Spaces between activated regions are not critical and will generally be
greater than about 1 µm.” (Id. at col. 18, l. 68 to col. 19, l. 4.)
Principles of Law
“[I]n an ex parte proceeding to obtain a patent, . . . the Patent Office
has the initial burden of coming forward with some sort of evidence tending
to disprove novelty.” In re Wilder, 429 F.2d 447, 450 (CCPA 1970).
“[W]hen the PTO shows sound basis for believing that the products of
the applicant and the prior art are the same, the applicant has the burden of
showing that they are not.” In re Spada, 911 F.2d 705, 708 (Fed. Cir. 1990).
“Any arguments or authorities not included in the brief or a reply brief
. . . will be refused consideration by the Board, unless good cause is shown.”
37 C.F.R. § 41.37(c)(1)(vii).
Analysis
Barrett discloses microarrays, on slides, of polypeptides including
antibodies. As evidenced by Zubay (see FF 31, infra), antibodies are at least
50 amino acids in length. Barrett does not expressly disclose 1000 discrete
regions of polypeptides per cm2 or discrete regions with a diameter of 20-
200 µm, but it describes a preferred embodiment with regions having an area
of 10,000 µm2. A circular region with an area of 10,000 µm2 would have a
diameter of about 113 µm.8 Since a square centimeter is 10,000 µm long on

8 The area of a circle is given by the formula Area = π x (radius)2, or
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each side, this embodiment also reasonably appears to describe a microarray
with at least 1000 regions per square centimeter.
We find that Barrett discloses a microarray meeting all the limitations
of claim 31.
The only argument Appellants rely on in contesting this rejection is
that Barrett does not teach a cationic film on the solid support (Appeal Br.
12). As the Examiner pointed out, however, a cationic film is only a
limitation of claims 16 and 36, which were not rejected as anticipated by
Barrett.
Conclusion of Law
Appellants have not shown that the Examiner erred in finding that
Barrett discloses the product of claim 31. Claims 10, 13-15, 18, 33-35, and
37 fall with claim 31 because they were not argued separately. 37 C.F.R.
§ 41.37(c)(1)(vii).
OBVIOUSNESS: BARRETT AND VAN NESS
Issue
The Examiner has rejected claims 16 and 36 under 35 U.S.C. § 103(a)
as obvious in view of Barrett and Van Ness (Ans. 13). The Examiner
acknowledges that Barrett does not teach a cationic film on the solid support,
but finds that “cationic films on solid supports for binding polypeptides were
well known in the art . . . as taught by Van Ness et al. who specifically teach
the cationic film provides for convenient attachment of the polypeptide” (id.

Area = π x (diameter/2)2. A circle with a diameter of 113 µm therefore has
an area of π x (113/2)2 = 10,029 µm2.
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at 14). The Examiner concludes that it would have been obvious to modify
Barrett’s device by providing a cationic film on a solid support (id.).
Appellants contend that Barrett teaches that its method is superior to
nonspecific attachment like that provided by a cationic film, because
Barrett’s method allows specifically addressable and modulatable levels of
attachment, and therefore a skilled worker would not have considered it
obvious to modify it to include a cationic film (Appeal Br. 20-21).
The issue with respect to this rejection is: Have Appellants shown
that the Examiner erred in concluding that a person of ordinary skill in the
art would have considered it obvious to modify Barrett’s product by
immobilizing polypeptides using a cationic film?
Additional Findings of Fact
18. Van Ness discloses “compositions comprising an activated
oligonucleotide, which can be covalently attached to a polymer-coated
support such as a bead” (Van Ness, col. 2, ll. 18-20).
19. Van Ness discloses that the solid support can be coated with a
polymer having an amine functionality (id. at col. 6, ll. 14).
20. Van Ness discloses that the “polymer-coated solid supports are
then conjugated with activated oligonucleotides or other substances of
interest. . . . [A]n amine-containing polymer can be covalently linked
through the amine to a protein. . . . Conveniently, the polymer is coupled to a
solid support, such as a bead.” (Id. at col. 6, ll. 20-28.)
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Principles of Law
An invention “composed of several elements is not proved obvious
merely by demonstrating that each of its elements was, independently,
known in the prior art. . . .[I]t can be important to identify a reason that
would have prompted a person of ordinary skill in the relevant field to
combine the elements in the way the claimed new invention does.” KSR
Int’l Co. v. Teleflex Inc., 550 U.S. 398, 418 (2007).
“[A]ny need or problem known in the field of endeavor at the time of
invention and addressed by the patent can provide a reason for combining
the elements in the manner claimed.” KSR, 550 U.S. at 420.
However, “[w]e must still be careful not to allow hindsight
reconstruction of references to reach the claimed invention without any
explanation as to how or why the references would be combined to produce
the claimed invention.” Innogenetics, N.V. v. Abbott Labs., 512 F.3d 1363,
1374 n.3 (Fed. Cir. 2008).
Analysis
Barrett discloses a method of immobilizing anti-ligands in which a
solid support is coated with inactive (caged) binding members which are
selectively activated in predefined regions by, e.g., irradiation. (FFs 15, 16.)
Barrett discloses that the irradiated areas are preferably less than 10,000 µm2
(FF 17), which corresponds to a square 100 µm on a side or a circle with a
diameter of 113 µm.
Van Ness discloses immobilizing proteins, among other things, on
beads coated with a polymer that can have an amine functionality (FF 20).
The Examiner concludes that it would have been obvious to modify Barrett’s
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device by immobilizing proteins using the cationic film disclosed by Van
Ness because Van Ness teaches that its film allows convenient attachment
(Ans. 14).
Appellants argue that Barrett teaches that its method has the
advantage of allowing reagents to be attached in specific, selectively
activated regions of a substrate, and that Barrett teaches avoiding methods of
nonspecific attachment like that of Van Ness (Appeal Br. 20). Appellants
conclude that it would not have been obvious to incorporate a method of
attachment using a cationic film coating in Barrett’s apparatus because that
would render inoperative Barrett’s selectively photoactivatable coating (id.).
We agree with Appellants that the Examiner has not adequately
shown that a skilled worker would have considered it obvious to modify
Barrett’s device by immobilizing the anti-ligands using Van Ness’ cationic
film rather than Barrett’s activated binding members. Barrett’s focus is on
making small regions capable of binding anti-ligand, while leaving the
binding members on the rest of its substrate inactive. The Examiner has
pointed to nothing in Van Ness that would support a finding that Van Ness’
method of immobilizing a protein would be capable of providing the same
capacity to activate only certain areas of a substrate for immobilizing a
particular anti-ligand.
The fact that other methods of immobilizing compounds on a
substrate were known, without more, does not mean that any known method
if immobilization would be suitable for Barrett’s apparatus. The evidence of
record does not support a conclusion that a skilled worker would consider
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Van Ness’ method of immobilization to be interchangeable with Barrett’s
method.
Conclusion of Law
Appellants have shown that the Examiner erred in concluding that a
person of ordinary skill in the art would have considered it obvious to
modify Barrett’s product by immobilizing polypeptides using a cationic
film.
OBVIOUSNESS: BEATTIE, ZUBAY, AND CHANG
Issue
The Examiner has rejected claims 10, 13-15, 18, 31, and 33-35 under
35 U.S.C. § 103(a) as obvious in view of Beattie, Zubay, and Chang (Ans.
6). The Examiner finds that Beattie teaches a microarray meeting most of
the limitations but does not “specifically teach polypeptides arrayed on a
slide” (id. at 7), Chang teaches an array of antibodies on a slide (id.), and
Zubay teaches that antibodies are at least 50 amino acids long (id. at 6). The
Examiner concludes that it would have been obvious to “apply the slide of
Chang to the broadly defined substrate of Beattie et al to thereby provide a
light-transparent support . . . for the obvious benefit of permitting detection
and analysis of reactions on the support” (id. at 7).
Appellants contend that it would not have been obvious to deposit
Beattie’s binding reagents on a slide because Beattie “specifically teach[es]
that a flat surface design is undesirable” (Appeal Br. 14) and “absolutely
requires the presence of channels through the substrate . . . in order to
function” (id. at 16).
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The issue with respect to this rejection is: Have Appellants shown
that the Examiner erred in concluding that it would have been obvious to
modify Beattie’s product by using Chang’s slide to immobilize the binding
reagents in Beattie’s product?
Additional Findings of Fact
21. Beattie discloses that “[g]enosensors, or miniaturized ‘DNA
chips’ are currently being developed . . . for hybridization analysis of DNA
samples. DNA chips typically employ arrays of DNA probes tethered to flat
surfaces.” (Beattie, col. 2, l. 66 to col. 3, l. 2.)
22. Beattie discloses that prior art chips have the disadvantage that “a
flat surface design introduces a rate-limiting step in the hybridization
reaction, i.e., diffusion of target molecules over relatively long distances
before encountering the complementary probes on the surface” (id. at col. 3,
ll. 19-22).
23. Beattie discloses “a novel flow-through genosensor, in which
nucleic acid recognition elements are immobilized within densely packed
pores or channels, arranged in patches across a wafer of solid support
material” (id. at col. 1, ll. 29-32).
24. Beattie discloses that its device “is designed to overcome the
inherent limitations in current solid phase hybridization materials,
eliminating the diffusion-limited step in flat surface hybridizations” (id. at
col. 3, ll. 23-26).
25. Beattie discloses that its device uses nanochannel glass (NCG)
wafers “as high surface area nanoporous support structures to tether DNA
targets or probes for hybridization” (id. at col. 9, ll. 44-49).
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26. Beattie discloses that “nanochannel glass structure can possess
packing densities in excess of 3x1010 channels per square centimeter. . . . A
variety of materials can be immobilized or fixed to the glass surfaces within
the channels of the NCG array.” (Id. at col. 9, ll. 54-58.)
27. Beattie discloses that the NCG wafer is “bonded on the upper side
to a polymeric layer containing an array of orifices which align with the
array of nanochannel bundles and serve as sample wells” (id. at col. 10, ll.
37-39).
28. Beattie teaches that the development of the polymeric array
involves, among other steps, “lamination tooling and process development”
(id. at col. 10, ll. 54-55).
29. Beattie discloses that “[i]nitial lamination process development is
carried out using unablated polymeric material (or alternatively, using glass
slides and/or silicon wafers)” (id. at col. 11, ll. 40-42).
30. Beattie discloses that porous silicon wafers can also be used to
immobilize the binding reagents in its device (id. at col. 11, ll. 56-64).
31. Zubay discloses that antibodies are more than 50 amino acids
long (Zubay 965, legend to Figure 33.2).
32. Chang discloses an “immunoassay device . . . compris[ing] a
support which has a substantially planar surface. On the support is an array
of small, closely-spaced, discrete, antibody coated areas. A cover is spaced
from the support surface and is positioned over the array of antibody coated
areas.” (Chang, col. 1, ll. 55-60.)
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33. Chang discloses that “[p]referably, the support and the cover are
light transparent. The support surface may be glass or plastic microscope
slides.” (Id. at col. 2, ll. 7-9.)
Analysis
Beattie teaches a device in which a binding reagent is immobilized in
the pores of a nanochannel glass or porous silicon wafer. The Examiner
concludes that it would have been obvious to use Chang’s glass slide for the
substrate in Beattie’s device in order to provide a light-transparent support
(Ans. 7). The Examiner reasons that “because Beattie and Chang teach the
structural element of the microarray as claimed, the process of making the
microarray as recited in [claim 10] does not distinguish the microarray over
that of prior art” (id. at 9).
Appellants argue that it would not have been obvious to substitute a
glass slide for Beattie’s channel-containing substrate because Beattie teaches
that a flat surface design is undesirable (Appeal Br. 14) and Beattie’s device
requires channels through the substrate in order to function (id. at 16).
We agree with Appellants that the Examiner has not adequately
explained why it would have been obvious to use Chang’s glass microscope
slide to immobilize the binding reagent in Beattie’s device. Beattie refers to
glass slides only in the context of developing the lamination process for
attaching a supporting polymeric layer to the nanochannel glass (NCG) layer
to which the binding reagents are immobilized. Beattie does not suggest a
planar, non-channeled glass layer for immobilizing its binding reagents.
Beattie’s entire disclosure, in fact, focuses on the benefits of
immobilizing binding reagents within the pores of a nanoporous support –
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either NCG or porous silicon. Beattie expressly discusses the advantages of
its approach over prior art approaches, like that of Chang, where the binding
reagent is immobilized on the surface of a planar support. A skilled worker,
reading Beattie and Chang, therefore would understand that substituting a
planar support for Beattie’s nanoporous support would create a product
having the disadvantage discussed by Beattie; specifically, it would require
diffusion of target molecules over relatively long distances, creating a rate-
limiting step in binding reactions.
The only offsetting advantage identified by the Examiner of using
Chang’s glass slide in Beattie’s device is that a glass slide would be light
transparent. But the Examiner has not identified any reason why light
transparency would be desirable in Beattie’s device, nor has she provided
any evidence that the NCG or porous silicon used by Beattie are not
themselves light transparent. The Examiner therefore has not provided
sufficient evidence or reasoning to support a conclusion that a skilled worker
would have considered it obvious to use a glass slide to immobilize the
binding reagents in Beattie’s device.
The Examiner also rejected claims 16 and 36 as obvious in view of
Beattie, Zubay, Chang, and Van Ness (Ans. 12). The Examiner, however,
has not pointed to any disclosure in Van Ness that would make up for the
deficiency discussed above. The rejection based on Beattie, Zubay, Chang,
and Van Ness is reversed as well.
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Conclusion of Law
Appellants have shown that the Examiner erred in concluding that it
would have been obvious to modify Beattie’s product by using Chang’s slide
to immobilize the binding reagents in Beattie’s product.
SUMMARY
We affirm the rejection of claims 10, 13-15, 18, 31, 33-35, and 37 as
anticipated by Barrett. We reverse the other rejections on appeal.
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-IN-PART

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