Ex Parte Dehal et al

Patent Trial and Appeal Board

Aug 31, 2016

12513348 (P.T.A.B. Aug. 31, 2016)

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.
12/513,348 02/08/2010 Prabhjyot Dehal 00033-020US1/312440US/CMH 1429
26138 7590 08/31/2016
Joseph R. Baker, APC
Gavrilovich, Dodd & Lindsey LLP
4660 La Jolla Village Drive, Suite 750
San Diego, CA 92122
EXAMINER
DO, PENSEE T
ART UNIT PAPER NUMBER
1677
MAIL DATE DELIVERY MODE
08/31/2016 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 PATENT TRIAL AND APPEAL BOARD
__________

Ex parte PRABHJYOT DEHAL, DAVID PRITCHARD,
and CLAIRE GEEKIE1
__________

Appeal 2016-000060
Application 12/513,348
Technology Center 1600
__________

Before ULRIKE W. JENKS, JACQUELINE T. HARLOW,
and TIMOTHY G. MAJORS, Administrative Patent Judges.

MAJORS, Administrative Patent Judge.

DECISION ON APPEAL
This is an appeal under 35 U.S.C. § 134 involving claims to
recognition labels which have been rejected as obvious. We have
jurisdiction under 35 U.S.C. § 6(b).
We affirm.
STATEMENT OF THE CASE
“The present invention concerns magnetic recognition labels, capable
of attaching small quantities of a magnetic (or magnetisable) substance to an

1 Appellants identify the Real Party in Interest as ITI Scotland Limited.
(App. Br. 3.)
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analyte via a recognition agent for the analyte.” (Spec. 1.) Also, “in its most
preferred embodiments, the present invention makes use of a multi-moiety
label, typically formed from one or more antigen binding arms of one or
more antibodies, for recognising one or more analytes, and one or more
copies of a metal-binding protein attached to the antigen binding arm[.]”
(Id. at 14.) Applicants disclose that “[i]t is particularly preferred that the
labels are fusion proteins . . . a protein that has been expressed as a single
entity recombinant protein.” (Id. at 5.)
Claims 1, 4–6, 11–16, 69–73, and 80–92 are on appeal. Claim 1 is
illustrative:
1. A label for an analyte, which label is attached to a
magnetic or magnetizable substance, the label comprising:
(a) a recognition moiety for attaching the label to the
analyte; and
(b) a moiety for binding or encapsulating the magnetic or
magnetizable substance comprising a metal-binding protein, or a
metal-binding domain of a protein, the protein being ferritin,
wherein the label contains a fusion protein comprising the
recognition moiety and the moiety for binding or encapsulating
the magnetic or magnetizable substance, characterized in that the
magnetic or magnetizable substance comprises magnetite such
that the label is suitable for use in a method of processing a
sample according to claim 33.2

2 Claim 33, recited as a limitation of claim 1, is withdrawn from
examination. (Final Act. 4; App. Br. 2.) The inclusion of withdrawn subject
matter would render claim 1 uncertain. However, neither Appellants nor the
Examiner raise issues concerning this limitation, and we decline to exercise
our discretion to enter a new grounds of rejection of claim 1. Examiner
interprets the limitation of the claim 33 subject matter part of claim 1 as an
intended use (Ans. 3, Final Act. 8), which is not rebutted by Appellants.
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(App. Br. 12 (Claims App’x).)
The claims stand rejected as follows:
I. Claims 1, 11–15, and 69–73 under 35 U.S.C. § 103(a) over
Lansdorp3 and Carter.4
II. Claims 4–6 under 35 U.S.C. § 103(a) over Lansdorp and Carter, in
further view of Zborowski.5
III. Claims 16 and 83–92 under 35 U.S.C. § 103(a) over Lansdorp
and Carter, in further view of Kraus.6
IV. Claims 80–82 under 35 U.S.C. § 103(a) over Lansdorp and
Carter, in further view of Kraus and Zborowski.
On appeal, we determine whether, based on the preponderance of the
evidence, the Examiner established that the claims would have been obvious
under Rejections I–IV.
DISCUSSION
I. Obviousness of Claims 1, 11–15, and 69–73 over Lansdorp and Carter
Findings of Fact (FF)
FF 1. The Examiner’s findings of fact and statement of the rejection
of claims 1, 11–15, and 69–73 may be found at pages 6–8 and 12–16 of the
Final Rejection dated February 26, 2014. (See also, Ans. 2–4, 8–12; Adv.
Act. 3–5, 9–11.)

3 Lansdorp et al., US 5,514,340, issued May 7, 1996 (“Lansdorp”).
4 Carter et al., US 2004/0006001 A1, published Jan. 8, 2004 (“Carter”).
5 Maciej Zborowski et al., Immunomagnetic Isolation of Magnetoferritin-
Labeled Cells in a Modified Ferrograph, 24 CYTOMETRY 251–259 (1996)
(“Zborowski”).
6 Kraus et al., US 2004/0002169 A1, published Jan. 1, 2004 (“Kraus”).
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FF 2. Lansdorp teaches a device and method for magnetically
labeling and separating cells in a sample using a magnetic field. (Lansdorp
Abstract; see also, id. at col. 16, ll. 34–60 (regarding large scale
separations).) Lansdorp teaches “[t]he device . . . may be used to deplete
selected cells from a sample, such as cells which express cell surface
antigens recognized by antibodies.” (Id. at col. 7, ll. 60–62.) According to
Lansdorp, “[t]he selected cells to be depleted in the sample may be
magnetically labelled by conjugating the cells to magnetic particles.” (Id. at
col. 8, ll. 5–7.) Lansdorp teaches the particles comprise “a magnetic core,
such as magnetite (Fe3O4) coated or embedded in material that prevents the
crystals from interacting. Examples of such materials include proteins, such
as ferritin, [and] polysaccharides, such as dextrans . . . .” (Id. at col. 8, ll. 7–
13). Lansdorp further teaches
Substances which are capable of binding to the selected cells to
be depleted . . . preferably antibodies, may be chemically bound
to the surface of the magnetic particles . . . . When the magnetic
particles are reacted with a sample containing the selected cells,
conjugates will form between the selected cells and the magnetic
particles with bound substances.

(Id. at col. 8, ll. 29–37.)
FF 3. Carter teaches ferritin fusion proteins “useful in a variety of
applications, including human and veterinary vaccines and therapeutics, . . .
protein purification platforms, and therapeutic receptor-binding proteins.”
(Carter Abstract.) Carter teaches that “[f]erritin is a highly conserved 24
subunit protein that [is] found in all animals, bacteria, and plants. . . . [and]
ferritin accumulates iron at concentrations orders of magnitude greater than
the solubility of free iron under physiological conditions.” (Id. at ¶ 3.)
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FF 4. Carter further teaches
suitable proteins or peptides can be fused with the ferritin protein
either as an exocapsid product by fusion with the N-terminal
sequence[,] . . . as an endocapsid product by fusion with the C-
terminus extending inside the capsid core, or a combination
thereof[.] By ferritin is meant the ferritin protein and/or its H
and/or L chains as well as ferritin analogs such as disclosed in
U.S. Pat. No. 5,304,382, incorporated herein by reference . . . .
The proteins or peptides useful in the invention will include those
proteins, peptides, [and] antibodies . . . which can be linked to
ferritin, and which can link to ferritin without disrupting its
structure and which when expressed will self assemble into a
large macromolecular or polymeric assembly.

(Id. at ¶32.) According to Carter, “when the fusion protein of the invention
is formed by linking of ferritin with an antibody, a spacer may be desirable
to allow the antibody to seek and bind with a target with less steric
hindrance from the ferritin portion of the fusion protein.” (Id. at ¶ 33.)
Analysis
We select claim 1 as representative.
The Examiner finds Lansdorp teaches all the limitations of claim 1,
except for the limitation concerning a “fusion protein.” (Ans. 3.) Because
“Lansdorp fails to teach that the label coated in the magnetic particles
comprises [] a fusion protein comprising the recognition moiety and the
moiety for binding or encapsulating the magnetic substance,” the Examiner
turns to Carter. (Id. (emphasis added).) According to the Examiner, “Carter
et al. teaches a fusion protein comprising ferritin linked to an antibody which
is specific for target sets of tissue of cells which fusion protein can be used
for protein[] purification.” (Id.)
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The Examiner concludes the skilled artisan would have predictably
modified Lansdorp’s device for magnetically labeling and separating
analytes by using a fusion protein of ferritin and antibody, such as taught in
Carter. (Ans. 3.) The Examiner reasons this modification would bring
multiple advantages. Among them, the Examiner finds the proposed
modification would “eliminate the step of attaching antibody to the magnetic
particles coated [with] ferritin [as in Lansdorp]. Thus, assay time would be
shorten[ed].” (Id.) Moreover, the Examiner finds “the fusion product of
ferritin and protein . . . can self-assemble into a large macromolecular or
polymeric assembly . . . [t]hus, more target proteins can be selected or bound
to the fusion product.” (Id.) The Examiner further finds the modified
product would “enhance the half-life of the protein fused to the ferritin and
[] avoid immune-related problems.” (Id. at 10.)
Notwithstanding Appellants’ arguments to the contrary, we conclude
the Examiner has provided sufficient evidence and articulated reasoning to
show that claim 1 would have been prima facie obvious over Lansdorp and
Carter. Lansdorp and Carter both teach cell and/or protein purification
methods. (FF 2–4.) Both references teach the use of a label that includes
the protein ferritin and a recognition moiety, such as an antibody for binding
to a target. (Id.) True, in a preferred embodiment, Carter teaches ferritin
that encapsulates a non-magnetic form of iron (Fe(III)2O3). (Carter ¶ 30.)
But the Examiner is not specifically relying on Carter for teaching ferritin
that binds or encapsulates magnetite — the most magnetic iron oxide, with
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the formula Fe3O4. (Spec. 25.) Lansdorp supplies that teaching. (FF 2.)7
And nonobviousness cannot be shown by attacking Carter individually
where, as here, the obviousness rejection is based on the combination of
Lansdorp and Carter. See, e.g., In re Merck & Co., 800 F.2d 1091, 1097
(Fed. Cir. 1986) (“Non-obviousness cannot be established by attacking
references individually where the rejection is based upon the teachings of a
combination of references [].”)
Appellants also argue the teachings of Lansdorp and Carter may not
be combined. (App. Br. 6–9.) Appellants contend the combination
proposed by the Examiner would “disregard the express teachings of
Lansdorp et al. of the preferential use of polysaccharides (i.e., dextran) in
iron complexes,” rather than proteins like ferritin. (Id. at 9.)
This argument is unpersuasive. The teachings of the prior art are not
limited to preferred embodiments; the art must instead be considered for all
that it teaches and suggests to the skilled artisan. Merck & Co., Inc. v.
Biocraft Labs., Inc., 874 F.2d 804, 807 (Fed. Cir. 1989) (“[I]n a section 103
inquiry, the fact that a specific [embodiment] is taught to be preferred is not
controlling, since all disclosures of the prior art, including unpreferred
embodiments, must be considered.”) (internal quotation marks omitted). So,
the fact that Lansdorp “preferably” uses a dextran-iron complex is not
decisive in an obviousness inquiry because Lansdorp also expressly teaches

7 Carter at paragraph 32, which the Examiner relies upon in making the
rejection, refers to and incorporates by references US 5,304,382, for its
description of ferritin and ferritin analogs. The ’382 Patent expressly
discloses that ferritin analogs may comprise magnetite. (’382 Patent col. 4,
l. 52 to col. 5, l. 5.)
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an alternative embodiment having magnetite embedded in ferritin (FF 2) as
in claim 1.
Appellants also argue “it would not have been obvious to combine
[Lansdorp and Carter] as the teachings are directed to different fields of
endeavor.” (App. Br. 6.) According to Appellants, “Carter . . . only
describes therapeutic/diagnostic applications and the purification of proteins
based upon their size,” rather than based on magnetic separation of cells as
in Lansdorp.” (App. Br. 9.)
This argument is also unpersuasive. Appellants’ assertion that
Lansdorp uses a magnetic field to purify cells, while Carter purifies proteins
by gel filtration based on size is, here again, an argument that attacks the
references individually rather than dealing with the combination as
presented. In re Merck & Co., 800 F.2d at 1097. And Appellants have
presented insufficient persuasive evidence or reasoning to rebut the
Examiner’s finding that the fusion proteins, such as illustrated in Carter, are
suitable for use in the device and method, such as described in Lansdorp,
which purifies analytes based on a well-known technique using the magnetic
properties of the label attached to the analyte. (FF 1–2; Ans. 10–12.)8
A key question is whether Lansdorp and Carter are in the same field
of applicants’ endeavor or reasonably pertinent to the problem with which
the applicants were concerned. In re Klein, 647 F.3d 1343, 1348 (Fed. Cir.
2011). They are. The fact that the Specification cites various prior art

8 Appellants’ argument related to the purification of cells in Lansdorp versus
proteins in Carter (App. Br. 8) fails for similar reasons.
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related to magnetic separation techniques (similar to Lansdorp) and Carter9
as background is evidence that Lansdorp and Carter are within the same
field of applicants’ endeavor. (Spec. 1–4.) In addition, insofar as Lansdorp
and Carter both disclose purification systems that combine ferritin and
recognition moieties (e.g., antibodies) for binding and purifying target
substances (FF 2–4), the references are reasonably pertinent to problems the
present application purports to address. (See, e.g., Spec. 4 (“a further aim of
the present invention [is] to provide an improved label for an analyte that
could be advantageously employed, for example, in a microfluidic or
nanofluidic device.”) In re Klein, 647 F.3d at 1348 (a reference is
reasonably pertinent and thus analogous if it “would have commended itself
to an inventor’s attention in considering his problem.”).
Appellants also argue that certain reasons cited by the Examiner as
providing motivation for combining Lansdorp and Carter are flawed.
Appellants contend one of the advantages cited by the Examiner for using
the fusion proteins of Carter — enhanced half-life and avoidance of
immune-related problems — is “achieved only when the protein or peptide
is fused inside the ferritin . . ., that is, in the C-terminal region.” (App. Br.
7.) Appellants further contend the Examiner’s finding that “one of ordinary
skill would have purchased an already made ferritin-antibody fusion protein
to reduce assay time instead of generating the fusion protein from scratch”
(Ans. 16) is incorrect. (App. Br. 9 (“There is no indication that magnetic

9 The Specification discloses U.S. 7,097,841, which is the patent that issued
from Carter.
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antibody fusion products were commercially available.”); see also, Reply
Br. 4.)
Appellants’ arguments on these points are persuasive. In order to
obtain the advantage cited by the Examiner of enhanced half-life and
avoidance of immune problems, Carter teaches the protein or peptide may be
fused on the inner surface (C-terminus) of the ferritin, where it is shielded
from environmental factors that might otherwise inactivate or degrade the
proteins. (Carter ¶ 34.) Yet shielding the protein or peptide (e.g., and
antibody) in this way runs counter to the desired labeling in Lansdorp and as
claimed. Stated differently, in order to optimize the targeting and separation
of analytes, the recognition moiety (e.g., antibody) should be exposed in the
sample, not shielded. In addition, we are not persuaded that assay time
would shorten when preparing fusion proteins versus chemically attached
proteins. As the Specification confirms, “a fusion protein is a protein that
has been expressed as a single entity recombinant protein.” (Spec. 5.) In the
face of Appellants’ arguments, the Examiner has not adequately
demonstrated that it would be faster or easier to design fusion proteins, nor
that suitable fusion proteins could simply be purchased as suggested by the
Examiner. (Ans. 16; Final Act. 16.)
The Examiner has, however, provided further findings in support of
the combination of Lansdorp and Carter. In particular, the Examiner
reasoned that preparing a label as a fusion protein would, as taught in Carter,
permit the label to form a macromolecular or polymeric assembly (FF 4) that
would be able to bind with more target analyte. (Ans. 3.) Appellants have
not provided evidence or argument sufficient to rebut the Examiner’s
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findings in this respect. Appellants argue Carter teaches “the protein or
peptide that is to be fused with the ferritin is provided at both inner and outer
surfaces of the ferritin to form a fusion protein capable of self-assembly.”
(Reply Br. 4.) We are not persuaded. Carter teaches “fusion of additional
protein or peptide segments to either or both of the N and C termini.”
(Carter ¶ 2 (emphasis added). Carter further teaches the protein or peptide
“may be fused outside the core [i.e., to the N-terminus] when it is desired
that the fused protein or peptide be unshielded such as when more rapid
immunogenicity is desired.” (Carter ¶ 34.) Appellants have not
persuasively shown that Carter teaches desirable formation of
macromolecular or polymeric assembly of the fusion protein occurs only
when the desired protein or peptide is fused to both the inner and outer
surfaces of the ferritin. (Id. at ¶¶ 8–9, 14–15, 34–35.)
Because Carter teaches and suggests that antibodies may, in
embodiments, be fused to the exterior of ferritin alone, we are not persuaded
that Carter teaches against including magnetite in the ferritin core, nor that
the Examiner’s combination defeats the function of Carter. Appellants’
arguments to the contrary (Reply Br. 5.) presume the antibody must be fused
to both the interior and exterior of ferritin, and are thus unpersuasive.
Conclusion of Law
For the above reasons, we conclude the Examiner established by a
preponderance of the evidence that claim 1 would have been obvious over
Lansdorp and Carter. Claims 11–15 and 69–73 have not been argued
separately and thus fall with claim 1. 37 C.F.R. § 41.37(c)(1)(iv).

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II. Obviousness of Claims 4–6 over Lansdorp, Carter, and Zborowski
Finding of Fact (FF)
FF 5. The Examiner’s findings of fact and statement of the rejection
of claims 4–6 may be found at pages 8–9 and 16 of the Final Rejection dated
February 26, 2014. (See also, Ans. 4–5, 12–13; Adv. Act. 5–6, 11–12.)
FF 6. Zborowski teaches cell isolation using native ferritin and
magnetoferritin. (Zborowski Abstract.) According to Zborowski,
“[m]agnetoferritin, but not native ferritin, imparted a sufficient magnetic
moment to cells to deplete the labeled cell population . . . in a magnetic
field.” (Id.) Zborowski teaches “increas[ing] the efficiency and specificity
of magnetic separation . . . by increasing the magnetic moment per protein
molecule through chemical synthesis of a ferromagnetic mineral core within
the protein cavity.” (Id.) Zborowski further teaches “[s]ynthesis of
magnetite (Fe3O4) within demetallated horse spleen ferritin molecules . . .
[with] discrete 5 nm cores of crystalline magnetite encapsulated within the
polypeptide shell. Samples, on average, contained approximately 2,000 Fe
atoms per protein molecule.” (Id. at 252.)
Analysis
Claims 4–6 depend directly or indirectly from claim 1. Claims 4–6
specify a volume of the magnetic or magnetizable substance (i.e., magnetite)
bound or encapsulated by ferritin. For example, claim 4 recites “the
magnetic or magnetizable substance having a volume of not more than 1x105
nm3.” We select claim 4 as representative.
The Examiner finds that Lansdorp and Carter do not specifically
“teach the quantity of the magnetic or magnetizable substance having a
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volume of not more than 1x105 nm3” and thus turns to Zborowski. (Ans. 4–
5.) The Examiner finds Zborowski teaches ferritin with a magnetic core of
5nm and an average of approximately 2000 Fe atoms, which corresponds to
“a total volume of not more than 100 nm[3].” (Id. at 5.) The Examiner
further finds that Zborowski “teaches that the modified magnetoferritin
increases in magnetic susceptibility which would increase the magnetic
signal during detection and thus increasing in sensitivity of the label as
compared to native ferritin.” (Id.) The Examiner thus concludes it would
have been obvious to use a volume of magnetoferritin as disclosed in
Zborowski in the modified labelling system taught and suggested by the
combination of Lansdorp and Carter. (Id.)
Appellants argue “Zborowski et al. do[es] not remedy or provide the
motivation lacking in the primary references.” (App. Br. 9.) Appellants also
argue the Examiner incorrectly stated that Carter and Zborowski “each
disclose magnetoferritin comprising magnetite.” (Id. at 10.) According to
Appellants, “[n]o other iron oxides [besides Fe(III)2O3] are disclosed in
Carter et al. . . . [and] [t]he iron oxide found in native ferritin is not
magnetic.” (Id.)
Appellants’ arguments are unpersuasive. Even if Carter did not
disclose magnetite (see supra, n. 7), that would not render the Examiner’s
combination improper. As discussed above, the combination of Lansdorp
and Carter is not improper merely because Carter does not expressly disclose
purification techniques that use the magnetism to separate target analytes in
a sample. Lansdorp supplies those teachings and, like Zborowski, teaches
ferritin that encapsulates a magnetite core. (FF 2; FF 6.) The Examiner
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relies on Carter for teaching a fusion protein comprising ferritin. (FF 1; FF
3–4.) Appellants are again arguing the references individually, and have not
presented sufficiently persuasive argument or evidence to demonstrate that a
fusion protein prepared from the combined teachings of Lansdorp and Carter
would not encapsulate or bind a volume of magnetite such as taught in
Zborowski.
In Appellants’ Reply Brief, they argue “the magnetoferritin used in
Zborowski et al. is entirely incompatible with a fusion construct.” (Reply
Br. 5.) More specifically, Appellants argue
The sequential labelling steps in the immunostaining
protocol is essential to the method of Zborowski et al. due to
amplification of the number of ferritin molecules per cell
surface antigen . . . [and] [t]he use of a fusion protein
comprising an antibody fused to magnetoferritin would remove
the successive labeling steps . . . [and thus] destroy the intended
use of Zborowski et al.

(Id. at 6.)
This argument is also unpersuasive. We are not persuaded the
Examiner’s proposed modification requires changing Zborowski or
incorporating a volume of magnetite in the fusion protein taught by the
combination of Lansdorp and Carter precisely according to Zborowski’s
method. To the contrary, we find the Examiner relies on Zborowski as
teaching a desirable volume of magnetite to increase a label’s magnetic
signal, and concludes that it would have been obvious to embed or bind such
a volume (irrespective of method) in a fusion protein taught by the
combination of Lansdorp and Carter. (Ans. 5.)
Conclusion of Law
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We conclude the Examiner established by a preponderance of the
evidence that claim 4 would have been obvious over Lansdorp and Carter, in
further view of Zborowski. Claims 5–6 have not been argued separately and
thus fall with claim 4.

III. Obviousness of Claims 16 and 83–92 over Lansdorp, Carter, and Kraus
Findings of Fact
FF 7. The Examiner’s findings of fact and statement of the rejection
of claims 16 and 83–92 may be found at pages 9–11 and 16 of the Final
Rejection dated February 26, 2014. (See also, Ans. 5–7 and 13; Adv. Act.
6–8.)
FF 8. Kraus teaches a high-throughput magnetic sorting device
allowing multiple analyses of a sample (i.e., multiplex assay). (See, e.g.,
Kraus Abstract, see also, id. at ¶ 19.) Kraus teaches
processes of separating, analyzing and/or collecting selected
species within a target sample by use of magnetic microspheres
including magnetic particles . . . . adapted for attachment to a
receptor agent that can subsequently bind to selected species
within the target sample. The magnetic microspheres can be
sorted into a number of distinct populations, each population
with a specific range of magnetic moments.

(Id. at Abstract; see also, id. at ¶¶ 15–16) Kraus further teaches “suitable
chemical compositions for the magnetic particles . . . [include]
superparamagnetic materials such as iron oxide (Fe3O4).” (Id. at ¶ 27.)
Analysis
We select claim 16 as representative. Claim 16 includes overlapping
elements with claim 1, but also requires a “set of labels . . . wherein each
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label in the set has a unique number of metal-binding moieties.” (App. Br.
13–14 (Claims App’x).)
The Examiner finds that Lansdorp and Carter do not teach that “each
label has a unique number of metal-binding moieties.” (Ans. 5.) The
Examiner thus turns to Kraus. The Examiner finds Kraus
teaches a high-throughput magnetic sorting device and method
based on the magnetic moments of the magnetic microsphere
label. Each magnetic microsphere label in a population has a
unique magnetic moment to give off a unique magnetic signal for
each population of analytes.

(Id. at 5–6.) The Examiner finds Carter teaches ferritin accumulates iron
and Lansdorp teaches large scale cell separation using magnetic particles
coated with ferritin. (Id. at 6.) According to the Examiner, ferritin’s ability
to accumulate iron “obviously contributes to the magnetic moment or
magnetic susceptibility and thus ferritin labels yield a stronger magnetic
signal.” (Id.) The Examiner finds “[i]n high throughput screening [such as
taught in Kraus], different labels are needed to label different analytes and
thus by varying the number of irons in the ferritin label results in different
labels with different magnetic signals.” (Id.) The Examiner concludes “it
would have been obvious . . . to vary the number of metal-binding moieties
such as ferritin on the magnetic particles taught by Lansdorp and Carter to
perform large scale magnetic separation of cells/analytes as taught by
Kraus.” (Id.)
Appellants incorporate their arguments regarding claim 1. (App. Br.
10.) Appellants also argue
Lansdorp et al. and Carter et al. even if appropriately combinable
fail to teach or suggest that “each label in the set has a unique
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number of metal-binding moieties”. The addition of Kraus et al.
do[es] not remedy or provide the motivation lacking in the
primary references.
Kraus et al. make no mention of fusion proteins, constructs
or the like.

(App. Br. 10.)
Appellants’ arguments are not persuasive. We reject Appellants’
arguments concerning claim 1 for the reasons stated above. Appellants’
additional arguments fail to sufficiently or persuasively respond to the
Examiner’s determination that it would have been obvious to vary the
number of metal-binding moieties in the modified label taught by Lansdorp
and Carter — thus forming labels with different magnetic moments — in
view of the teachings in Kraus and in order to take advantage of high-
throughput/multiplex analyte screening, as taught and suggested in Kraus.
(FF 8.) Appellants’ contention that Kraus makes no mention of fusion
proteins is an unpersuasive attack on Kraus individually when the Examiner
is relying on the combination of references and Carter’s teaching of fusion
proteins. (FF 1, 3–4.) Moreover, Appellants’ arguments are unconvincing
inasmuch as they simply recite a claim limitation and contend the limitation
is absent in the art. In re Lovin, 652 F.3d 1349, 1357 (Fed. Cir. 2011) (37
C.F.R. § 41.37 requires “more substantive arguments in an appeal brief than
a mere recitation of the claim elements and a naked assertion that the
corresponding elements were not found in the prior art.”).
Appellants raise new and untimely arguments concerning the
combination of Lansdorp, Carter, and Kraus in the Reply Brief. (Reply Br.
6–7.) Appellants have shown no good cause why these arguments were not
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raised in the Appeal Brief. We thus decline to consider such new arguments
in the present appeal. 37 C.F.R. § 41.41(a)(2).
Conclusion of Law
We conclude the Examiner established by a preponderance of the
evidence that claim 16 would have been obvious over Lansdorp and Carter,
in further view of Kraus. Claims 83–92 have not been argued separately and
thus fall with claim 16.

IV. Obviousness of Claims 80–82 over Lansdorp, Carter, Kraus, and
Zborowski
Findings of Fact
FF 9. The Examiner’s findings of fact and statement of the rejection
of claims 80–82 may be found at pages 11–12 of the Final Rejection dated
February 26, 2014. (See also, Ans. 7–8 and 13; Adv. Act. 8–9.)
Analysis
Claims 80–82 are similar to claims 4–6, except that claims 80–82
depend (directly or indirectly) from claim 16 rather than claim 1.
Appellants’ arguments concerning claims 80–82 are repetitive of the
arguments concerning Rejections I–III. (App. Br. 11.) We are unpersuaded
that claims 80–82 are nonobvious for the reasons discussed above.
Conclusion of Law
We conclude the Examiner established by a preponderance of the
evidence that claims 80–82 would have been obvious over Lansdorp and
Carter, in further view of Kraus and Zborowski.
Appeal 2016-000060
Application 12/513,348

19
SUMMARY
We affirm the rejection of claims 1, 4–6, 11–16, 69–73, and 80–92.
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