Trials@uspto.gov
`571-272-7822
`
`
`
`
` Paper No. 11
`
`
` Entered: February 22, 2017
`
`
`
`
`
`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`BIOEQ IP AG,
`Petitioner,
`
`v.
`
`GENENTECH, INC.,
`Patent Owner.
`____________
`
`Case IPR2016-01608
`Patent 6,716,602 B2
`____________
`
`
`Before TONI R. SCHEINER, ERICA A. FRANKLIN, and
`MICHELLE N. ANKENBRAND, Administrative Patent Judges.
`
`FRANKLIN, Administrative Patent Judge.
`
`DECISION
`Denying Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
`
`
`
`
`
`
`
`571-272-7822
`
`
`
`
` Paper No. 11
`
`
` Entered: February 22, 2017
`
`
`
`
`
`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`BIOEQ IP AG,
`Petitioner,
`
`v.
`
`GENENTECH, INC.,
`Patent Owner.
`____________
`
`Case IPR2016-01608
`Patent 6,716,602 B2
`____________
`
`
`Before TONI R. SCHEINER, ERICA A. FRANKLIN, and
`MICHELLE N. ANKENBRAND, Administrative Patent Judges.
`
`FRANKLIN, Administrative Patent Judge.
`
`DECISION
`Denying Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
`
`
`
`
`
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`
`
`INTRODUCTION
`
`bioeq IP AG (“Petitioner”) filed a Petition requesting an inter partes
`review of claims 1, 3–4, 6–16, 18, 20, 22–25, 27–28, and 30–39 of U.S.
`Patent No. 6,716,602 B2 (Ex. 1001, “the ’602 patent”). Paper 3 (“Pet.”).
`Genentech, Inc. (“Patent Owner”) filed a Preliminary Response to the
`Petition. Paper 9 (“Prelim. Resp.”). Petitioner filed an authorized Reply to
`Patent Owner’s Preliminary Response, Paper 10 (“Reply”), to address
`corrections to the ’602 patent claims requested by Patent Owner in its
`Request for Certificate of Correction Under 35 U.S.C. § 254, Ex. 2009,
`submitted to the Director after the filing of the Petition.
`We have jurisdiction under 35 U.S.C. § 314, which provides that an
`inter partes review may not be instituted “unless . . . there is a reasonable
`likelihood that the petitioner would prevail with respect to at least 1 of the
`claims challenged in the petition.” 35 U.S.C. § 314(a).
`Upon considering the Petition, Preliminary Response, and Reply, we
`determine that Petitioner has not established a reasonable likelihood that it
`would prevail in showing the unpatentability of at least one of the
`challenged claims. Accordingly, we deny the Petition and decline to
`institute an inter partes review.
`Related Proceedings
`A.
`Petitioner and Patent Owner indicate that there are no related matters
`to this proceeding. Pet. 65; Paper 6, 2.
`
`2
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`
`The ’602 Patent
`B.
`The ’602 patent is directed to methods for increasing the yield of a
`heterologous recombinant protein produced by recombinant host cells.
`Ex. 1001, 3:12–14. The Specification explains that those methods involve
`“first increasing the protein production capacity of the cells in culture by
`culturing the cells at a high growth rate, and then decreasing metabolic rate
`of the cells (rate shift) to permit proper folding or assembly of the
`heterologous protein.” Id. at 3:14–18. Properly folded or assembled
`functional protein can be revealed by activity assays. Id. at 5:11–12.
`Illustrative Claim
`C.
`Claim 1 is representative of the challenged claims and is reproduced
`below:
`
`1. A method for increasing the product yield of a properly
`folded polypeptide of interest produced by recombinant host
`cells, wherein expression of
`the polype[]ptide by
`the
`recombinant host cells is regulated by an inducible system, which
`method comprises
`(a) culturing the recombinant host cells under conditions of
`high metabolic growth rate; and
`(b) reducing the metabolic rate of the cultured recombinant
`host cells at the time of induction of polypeptide expression,
`wherein reducing the metabolic rate comprises reducing the feed
`rate of a carbon/energy source, or reducing the amount of
`available oxygen, or both, and wherein the reduction in
`metabolic rate result in increase yield of properly folded
`polypeptide.
`Ex. 1001, 18:11–24.
`
`
`The Asserted Grounds of Unpatentability
`D.
`Petitioner challenges the patentability of claims 1, 3–4, 6–16, 18, 20,
`22–25, 27–28, and 30–39 of the ’602 patent on the following grounds:
`
`3
`
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`
`IPR2016-01608
`Patent 6,716,602 B2
`Reference(s)
`Seeger1
`
`Seeger
`
`Basis
`§ 102(b)
`
`§ 103(a)
`
`Claim(s) challenged
`1, 3–4, 6, 9, 15–16, 20–22, 24–25,
`27–28, 30, 33, 39
`7–8, 31–32
`
`Seeger and Makrides2
`
`§ 103(a)
`
`10, 12, 23, 34, 36
`
`Seeger and Cabilly3
`
`§ 103(a)
`
`11, 13–14, 18, 35, 37–38
`
`Petitioner also relies on the declaration of Dr. Morris Z. Rosenberg
`(Ex. 1002).
`
`
`
`ANALYSIS
`Claim Construction
`A.
`In an inter partes review, the Board interprets claim terms in an
`unexpired patent according to the broadest reasonable construction in light
`of the specification of the patent in which they appear. 37 C.F.R.
`§ 42.100(b); Cuozzo Speed Techs., LLC v. Lee, 136 S. Ct. 2131, 2142 (2016)
`(affirming applicability of broadest reasonable construction standard to inter
`partes review proceedings). Under that standard, and absent any special
`definitions, we give claim terms their ordinary and customary meaning, as
`would be understood by one of ordinary skill in the art at the time of the
`
`
`1 Anke Seeger et al., Comparison of temperature- and isopropyl-ß-D-
`thiogalacto-pyranoside-induced synthesis of basic fibroblast growth factor
`in high-cell-density cultures of recombinant Escherichia coli, 17 ENZYME &
`MICROBIAL TECH. 947–53 (1995) (Ex. 1010).
`2 Savvas C. Makrides, Strategies for Achieving High-Level Expression of
`Genes in Escherichia coli, 60 MICROBIOLOGICAL REVIEWS 512–38 (1996)
`(Ex. 1023).
`3 Shmuel Cabilly, Growth at sub-optimal temperatures allows the
`production of functional, antigen-binding Fab fragments in Escherichia coli,
`85 GENE 553–57 (1989) (Ex. 1032).
`
`4
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`invention. In re Translogic Tech., Inc., 504 F.3d 1249, 1257 (Fed. Cir.
`2007). Any special definitions for claim terms must be set forth with
`reasonable clarity, deliberateness, and precision. In re Paulsen, 30 F.3d
`1475, 1480 (Fed. Cir. 1994).
`Petitioner proposes a construction for the claim phrase “reducing the
`metabolic rate,” that is recited in each of the challenged independent
`claims.4 Pet. 24. According to Petitioner, a person of ordinary skill in the
`art would have understood from the Specification that claim phrase means
`“altering the fermentation conditions to reduce or stop the growth/expansion
`of cells undergoing rapid growth and expansion, or for cells no longer
`undergoing rapid growth and expansion, reducing the oxygen uptake rate
`and/or the corresponding uptake of the corresponding carbon/energy source
`by the cells.” Id. at 25–26 (emphasis added).
`Patent Owner asserts that Petitioner argues for “an overly complex
`‘bifurcated definition’” that “attempts to import limitations from the
`specification.” Prelim. Resp. 18. According to Patent Owner, the phrase
`“reducing the metabolic rate” should be construed as defined by the
`Specification, i.e., “altering the host cell culture such that the host cells
`undergoing rapid growth and expansion reduce (or stop) growth and
`expansion.” Id. (quoting Ex. 1001, 4:12–15).
`We agree with Patent Owner that the Specification provides an
`explicit definition for the claim phrase “reducing the metabolic rate.” The
`Specification states, “[a]s used herein, ‘reducing metabolic rate’ or ‘shifting
`down metabolic rate’ means altering the host cell culture such that the host
`
`
`4 See Ex. 1001, 18:10–20:32; Ex. 2009, 7.
`
`5
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`cells undergoing rapid growth and expansion reduce (or stop) growth and
`expansion.” Ex. 1001, 4:12–15. Following that definition, the Specification
`describes “the case of cells already in a reduced growth state,” explaining
`that “the rates of oxygen uptake and the corresponding rates of uptake of a
`carbon/energy source are reduced.” Id. at 4:15–18. The Specification then
`states, “[s]ince, in the case of respiring cells, the metabolic rates are
`determined primarily by the rate at which the cell oxidizes the available
`carbon/energy source using the available oxygen, the metabolic rate can be
`reduced by limiting either of these two reactants.” Id. at 4:18–22. Thus, the
`Specification provides an explicit definition for the phrase “reducing
`metabolic rate,” followed by instructions for achieving that reduction in a
`particular circumstance. We disagree with Petitioner that the instructions
`provided by the Specification for reducing the metabolic rate in an
`exemplary situation serve to modify the express definition disclosed.
`Specifically, we do not find that the Specification provides an alternative
`definition of the claim phrase, as indicated by Petitioner’s use of the term
`“or” in its proposed construction of the phrase. Pet. 26.
`Accordingly, we determine that the ’602 patent expressly defines the
`claim phrase “reducing [the] metabolic rate” as meaning “altering the host
`cell culture such that the host cells undergoing rapid growth and expansion
`reduce (or stop) growth and expansion,” Ex. 1001, 4:12–15, and that
`definition is “set forth with reasonable clarity, deliberateness, and
`precision,” see In re Paulsen, 30 F.3d at 1480.
`In view of our analysis, we determine that no additional claim terms
`require construction for the purpose of this Decision. See Vivid Techs., Inc.
`v. Am. Sci. & Eng’g, Inc., 200 F.3d 795, 803 (Fed. Cir. 1999) (Only terms
`
`6
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`which are in controversy need to be construed, and only to the extent
`necessary to resolve the controversy).
`Anticipation by Seeger
`B.
`Petitioner asserts that Seeger discloses a method that meets each
`element of claims 1, 3–4, 6, 9, 15–16, 20–22, 24–25, 27–28, 30, 33, and 39.
`Pet. 28–43. Patent Owner disagrees. Prelim. Resp. 23–33.
`“A claim is anticipated only if each and every element as set forth in
`the claim is found, either expressly or inherently described, in a single prior
`art reference.” Verdegaal Bros. v. Union Oil Co. of Cal., 814 F.2d 628, 631
`(Fed. Cir. 1987). “Inherency … may not be established by probabilities or
`possibilities. The mere fact that a certain thing may result from a given set of
`circumstances is not sufficient.” MEHL/Biophile Int'l. Corp. v. Milgraum,
`192 F.3d 1362, 1365 (Fed. Cir. 1999) (quoting In re Oelrich, 666 F.2d 578,
`581 (CCPA 1981)).
`
`Seeger
`1.
`Seeger is a journal article discussing a comparison of two different
`expression systems for the expression of the cDNA encoding human basic
`fibroblast growth factor (bFGF) using E. coli as the host organism.
`Ex. 1010, Abstract. The bFGF structural gene was cloned into two vectors
`with different promoters, and the resulting expression systems were studied
`in high-cell density cultures. Id. Cells were grown at 30○C in a fed-batch
`procedure, with a predetermined exponential feeding rate to ensure constant
`specific growth rates. Id. Seeger explains that product formation was
`induced by shifting either the temperature from 30○C to 42○C, or by adding
`isopropyl-ß-D-thiogalacto-pyranoside (IPTG). Id. Seeger observes acetic
`acid accumulation in response to temperature-induced product expression.
`Id. at 952. To prevent that accumulation, and allow expression of bFGF, the
`
`7
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`exponential feeding rate was reduced from μset = 0.12 h-1 to μset = 0.08 h-1
`after the temperature shift to 42○C. Id. Seeger notes that a further reduction
`in the exponential feeding rate did not allow expression of bFGF. Id.
`Upon comparison, Seeger determined that the temperature-induced
`production of bFGF “generated more total and more soluble bFGF compared
`to IPTG-induced cultures.” Id. at 953. Seeger determined that the majority
`of bFGF produced was in the soluble cell fraction of the temperature-
`induced cultures. Id. at 952–953. The soluble and insoluble fractions were
`subjected to SDS-PAGE analysis, revealing that the formation of inclusion
`bodies and soluble bFGF occurred simultaneously after the temperature
`shift. Id. at 953.
`
`Analysis
`2.
`Petitioner asserts that Seeger’s temperature-induced production of
`bFGF meets every element of claims 1, 3–4, 6, 9, 15–16, 20–22, 24–25, 27–
`28, 30, 33, and 39, including “reducing the metabolic rate of the cultured
`recombinant host at the time of induction . . . wherein the reduction in
`metabolic rate results in increased yield of properly folded polypeptide,”
`recited by each of the challenged independent claims.5 Pet. 28. In
`particular, Petitioner asserts that “Seeger specifically discloses reducing the
`metabolic rate of cultured recombinant E. coli host cells at the time of
`induction of polypeptide expression by reducing the feed rate of a
`carbon/energy source—glucose.” Id. In support of that assertion, Petitioner
`relies on the description in the ’602 patent for “reducing metabolic rate,” and
`the testimony of its declarant, Dr. Rosenberg, that Seeger’s reduction in the
`amount of available glucose resulted in a decreased rate of glucose uptake
`
`
`5 See Ex. 1001, 18:10–20:32; Ex. 2009, 7.
`
`8
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`by the recombinant host cells. Pet. 28, 32–36. To support his opinion,
`Dr. Rosenberg used Seeger’s data “to calculate the specific glucose uptake
`rate (GUR) by the E. coli cells during growth and induction.” Ex. 1002 ¶ 56
`(citing id. at App. A). According to Dr. Rosenberg, his calculation revealed
`that GUR decreased in Seeger’s phases 1 and 2, indicating a reduction in the
`metabolic rate at the time of induction. Id.
`Regarding the claim recitation, “wherein the reduction in metabolic
`rate results in increased yield of properly folded polypeptide,” Petitioner
`asserts that is an intended result of the positively-recited method steps and
`does not impart patentable weight to the claims. Id. at 28, 36. Petitioner
`asserts further that even if considered a claim limitation, “Seeger’s metabolic
`rate shift results in increased yield of soluble, i.e., properly-folded, bFGF
`polypeptide.” Id. at 28. In support of that assertion, Petitioner states that
`“Seeger quantified the yield of bFGF following temperature shift induction
`at ‘70% of the bFGF produced . . . present in the soluble cell fraction.” Id. at
`37 (quoting Ex. 1010, 953:1–2). According to Petitioner and Dr. Rosenberg,
`that percentage of bFGF produced in the soluble cell fraction represents
`properly folded bFGF. Id. (citing Ex. 1002 ¶¶ 57, 73).
`Patent Owner argues that Seeger fails to disclose reducing the
`metabolic rate at the time of induction of polypeptide expression. Prelim.
`Resp. 23. According to Patent Owner, Seeger’s method of inducing
`expression by increasing temperature introduced another variable affecting
`the growth rate. Id. In particular, Patent Owner asserts that it was well
`known in the art that increasing temperature, within the range disclosed by
`
`9
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`Seeger, increases the growth rate of E. coli. Id. at 24–26 (citing Herendeen,6
`Ex. 2002, 1). Patent Owner asserts that, although Seeger reduced the
`glucose feeding rate in phase 2 of the fed-batch process, Seeger did not
`address the competing effect of increasing temperature on the growth rate,
`“leaving unanswered the question of whether Seeger actually reduced the
`metabolic rate at the time of induction.” Id. at 26–27.
`Additionally, Patent Owner asserts that Dr. Rosenberg’s GUR
`calculation does not reflect the true metabolic rate of Seeger’s temperature-
`induced E. coli fermentation because Dr. Rosenberg’s model does not take
`into account the variable of temperature. Id. at 27–28. Specifically, Patent
`Owner asserts that Dr. Rosenberg’s calculation included the variable for
`growth, μ, as a function of time, rather than as a function of both time and
`temperature. Id. at 27 (citing Ex. 1002, App. A, Equation 2). According to
`Patent Owner, given the temperature increase in Seeger’s method,
`“Dr. Rosenberg’s calculation provides no basis for concluding that there was
`a reduction in metabolic rate,” as required by each of the challenged claims.
`Prelim. Resp. 28.
`Further, Patent Owner asserts that Seeger reports the total expression
`of polypeptide without disclosing whether the polypeptides are properly
`folded. Id. at 29. In particular, Patent Owner asserts that Seeger’s two
`measuring techniques employed the denaturing agent, sodium dodecyl
`sulfate (SDS), to prepare the polypeptides for analysis by polyacrylamide
`electrophoresis (PAGE). Id. (citing Ex. 1010, 949). Thus, Patent Owner
`
`
`6 Sherrie L. Herendeen et al., Levels of Major Proteins of Escherichia coli
`During Growth at Different Temperatures, 139 J. BACTERIOLOGY 185–94
`(1979) (Ex. 2002).
`
`10
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`asserts, “Seeger only measures denatured polypeptides and thus provides no
`information regarding amounts of properly folded polypeptides.” Id.
`(emphasis omitted). According to Patent Owner, a person of skill in the art
`would have understood that SDS-PAGE linearized protein molecules, i.e.,
`eliminates any folding. Id. at 30 (citing Laemmli,7 Ex. 2001, 1).
`Moreover, Patent Owner asserts that Seeger’s disclosure of bFGF
`levels in the “soluble cell fraction” does not necessarily amount to a
`disclosure of the yield of properly folded polypeptide. Prelim. Resp. 32.
`According to Patent Owner, a person of ordinary skill in the art would have
`understood that misfolded proteins may also be found in the soluble fraction
`of the cell lysates and that solubility is not proof of proper folding.” Id.
`(citing, e.g., Sachdev, Ex. 2007,8 2; Schrodel, Ex. 2008,9 4). Patent Owner
`asserts that, in the ’602 patent, the inventors recognized that solubility does
`not imply proper folding, and further analyzed the soluble fraction by
`loading it onto a CsX column to separate properly folded polypeptides from
`misfolded ones prior to quantifying the properly folded portion. Prelim.
`Resp. 33 (citing Ex. 1001, 16:14–21). Thus, Patent Owner asserts that
`Seeger does not expressly or inherently address proper folding of proteins.
`Id.
`
`
`7 U.K. Laemmli, Cleavage of Structural Proteins during the Assembly of the
`Head of Bacteriophage T4, 227 NATURE 680–85 (1970) (Ex. 2001).
`8 Deepali Sachdev et al., Properties of Soluble Fusions Between Mammalian
`Aspartic Proteinases & Bacterial Maltose-Binding Protein, 18 J. PROTEIN
`CHEMISTRY 127–36 (1999) (Ex. 2007).
`9 Schrodel et al., Characterization of the aggregates formed during
`recombinant protein expression in bacteria, 6:10 BMC BIOCHEMISTRY 1–11
`(2005) (Ex. 2008).
`
`11
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`Based upon our review of the arguments and evidence, we are
`persuaded that Petitioner has not established that Seeger discloses reducing
`the metabolic rate of the cultured recombinant host cells at the time of
`induction of polypeptide expression, as required by the challenged claims,
`for the reasons discussed by Patent Owner. In particular, Petitioner relies
`upon the disclosure of the ’602 patent describing reducing metabolic rate in
`cells already in a reduced growth state by reducing the rates of oxygen
`uptake and the corresponding rates of uptake of a carbon/energy source. Pet.
`32–36 (citing Ex. 1001, 4:15–18). However, Petitioner has not addressed
`adequately how Seeger’s method of inducing expression by increasing
`temperature from 30 to 42○C may have affected the metabolic rate. Id. at
`32–36.
`In the Reply, Petitioner acknowledges that temperature is one of the
`“external factors that influence[s] the metabolic rate,” along with amount of
`glucose and oxygen supplied. Reply 2. According to Petitioner, Dr.
`Rosenberg’s GUR calculation is a “‘read-out’ of the cells’ metabolic rate,”
`and accounts for each of those external factors, including temperature. Id.
`In support of that contention, Petitioner states, “Dr. Rosenberg calculated
`GUR throughout Seeger’s fed-batch phases, i.e., before and after
`temperature change induced bFGF expression, thus accounting for
`temperature.” Id. at 2–3 (citing Ex. 1002 ¶ 56) (emphasis omitted).
`Petitioner’s assertion is not supported by the evidence of record. Dr.
`Rosenberg’s discussion of his calculation for the GUR in the paragraph cited
`by Petitioner explains only that Seeger increased the temperature, without
`describing or suggesting that he considered that temperature increase in his
`calculation or conclusions. Ex. 1002 ¶ 56. Moreover, as Patent Owner has
`asserted, Dr. Seeger’s calculation set forth in Appendix A does not include a
`
`12
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`variable accounting for the temperature shift. Ex. 1002, App. A. Thus,
`Petitioner has not shown persuasively that a person of skill in the art would
`have understood Seeger’s method to have included reducing the metabolic
`rate of the cultured recombinant host cells at the time of expression
`induction. See MEHL/Biophile Int'l. Corp., 192 F.3d at 1365.
`In that vein, even if we accept Petitioner’s position that the claim
`recitation “wherein the reduction in metabolic rate results in increased yield
`of properly folded polypeptide” is an intended result of the positively-recited
`method steps, Pet. 28, 36, Petitioner has not shown persuasively that Seeger
`discloses the positive step of reducing the metabolic rate so as to achieve
`that result. Moreover, if considered a limitation, Petitioner has not shown
`sufficiently that Seeger discloses such a result for the same reason. Further,
`for the reasons discussed by Patent Owner, Petitioner has not shown
`persuasively that Seeger’s soluble fraction of bFGF necessarily represents
`properly folded polypeptide. Prelim. Resp. 29–33.
`Therefore, we determine that Petitioner has not established a
`reasonable likelihood that it would prevail in showing that Seeger anticipates
`claims 1, 3–4, 6, 9, 15–16, 20–22, 24–25, 27–28, 30, 33, and 39.
`Consequently, we decline to institute an inter partes review of claims 1, 3–4,
`6, 9, 15–16, 20–22, 24–25, 27–28, 30, 33, and 39 based on this ground.
`C. Obviousness over Seeger Alone or in Combination with Additional
`References
`Each of Petitioner’s obviousness grounds is directed to a set of
`dependent claims. Pet. 27. Petitioner relies upon Seeger alone as disclosing
`the elements of the independent claims from which those challenged claims
`depend. Id. at 43–57. Indeed, Petitioner does not address the elements
`recited in the independent claims in any of the obviousness grounds. Id. To
`
`13
`
`
`
`IPR2016-01608
`Patent 6,716,602 B2
`the extent that Petitioner cites Makrides or Cabilly, those references are
`relied upon only to address additional elements of dependent claims, and are
`not asserted to cure any deficiencies of Seeger with respect to elements of
`the independent claims. Id. at 46–58.
`Therefore we determine that Petitioner has not demonstrated a
`reasonable likelihood of prevailing in showing the unpatentability of
`dependent claims 7–8 and 31–32 over Seeger, dependent claims 10, 12, 23,
`34, and 36 over Seeger and Makrides, or dependent claims 11, 13–14, 18,
`35, and 37–38 over Seeger and Cabilly, under 35 U.S.C. § 103(a), for the
`same reasons discussed regarding the independent claims from which they
`depend. Consequently, we decline to institute an inter partes review of
`claims 7–8, 10–14, 18, 23, 31–32, and 34–38 based on the respective ground
`challenging those claims.
`CONCLUSION
`
`For the foregoing reasons, we conclude that Petitioner has not
`established a reasonable likelihood of prevailing in showing the
`unpatentability of any challenged claim.
`
`
`ORDER
`
`Accordingly, it is hereby:
`ORDERED that Petitioner’s request for an inter partes review of
`claims 1, 3–4, 6–16, 18, 20, 22–25, 27–28, and 30–39 of the ’602 patent is
`denied.
`
`
`
`
`
`
`14
`
`
`
`15
`
`IPR2016-01608
`Patent 6,716,602 B2
`
`PETITIONER:
`
`Deborah Sterling
`dsterlin@skgf.com
`
`Jeremiah Frueauf
`jfrueauf-ptab@skgf.com
`
`Olga Partington
`opartington-ptab@skgf.com
`
`Timothy Shea
`tshea-ptab@skgf.com
`
`
`
`PATENT OWNER:
`
`David J. Ball, Jr.
`dball@paulweiss.com
`
`Jennifer Gordon
`jgordon@paulweiss.com
`
`Steven M. Balcof
`sbalcof@paulweiss.com
`
`
`
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