Trials@uspto.gov
`571-272-7822
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`Paper No. 17
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`Entered: March 29, 2018
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`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`BOEHRINGER INGELHEIM PHARMACEUTICALS, INC.,
`Petitioner,
`
`v.
`
`GENENTECH, INC.,
`Patent Owner.
`____________
`
`Case IPR2017-02032
`Patent 6,407,213 B1
`____________
`
`
`
`Before SHERIDAN K. SNEDDEN, ZHENYU YANG, and
`ROBERT A. POLLOCK, Administrative Patent Judges.
`
`YANG, Administrative Patent Judge.
`
`
`
`
`DECISION
`Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
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`571-272-7822
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`
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`Paper No. 17
`
`Entered: March 29, 2018
`
`
`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`BOEHRINGER INGELHEIM PHARMACEUTICALS, INC.,
`Petitioner,
`
`v.
`
`GENENTECH, INC.,
`Patent Owner.
`____________
`
`Case IPR2017-02032
`Patent 6,407,213 B1
`____________
`
`
`
`Before SHERIDAN K. SNEDDEN, ZHENYU YANG, and
`ROBERT A. POLLOCK, Administrative Patent Judges.
`
`YANG, Administrative Patent Judge.
`
`
`
`
`DECISION
`Institution of Inter Partes Review
`37 C.F.R. § 42.108
`
`
`
`
`
`
`
`
`
`
`
`IPR2017-02032
`Patent 6,407,213 B1
`
`
`INTRODUCTION
`Boehringer Ingelheim Pharmaceuticals, Inc. (“Petitioner”) filed a
`Petition for an inter partes review of claims 1, 2, 4, 25, 29, 62–64, 66, 67,
`69, 71–73, 75–78, 80, and 81 of U.S. Patent No. 6,407,213 B1 (“the ’213
`patent,” Ex. 1001). Paper 1 (“Pet.”). Genentech, Inc. (“Patent Owner”)
`timely filed a Preliminary Response. Paper 9 (“Prelim. Resp.”). We review
`the Petition, Preliminary Response, and accompanying evidence under
`35 U.S.C. § 314.
`For the reasons provided below, we determine Petitioner has satisfied
`the threshold requirement set forth in 35 U.S.C. § 314(a). Because
`Petitioner has established a reasonable likelihood that it would prevail in
`showing the unpatentability of at least one challenged claim, we institute an
`inter partes review of claims 1, 2, 4, 25, 29, 62–64, 66, 67, 69, 71, 73, 75–
`78, 80, and 81.
`
`Related Proceedings
`According to the parties, the ’213 patent is at issue in several district
`court cases, including Genentech, Inc. v. Amgen Inc., No. 1-17-cv-01407
`(D. Del.); Amgen Inc. v. Genentech, Inc., No. 2-17-cv-07349 (C.D. Cal.);
`Genentech, Inc. v. Amgen Inc., No. 1-17-cv-01471 (D. Del.); Genentech,
`Inc. et al. v. Pfizer, Inc. 1-17-cv-01672 (D. Del.); Celltrion, Inc. v.
`Genentech, Inc., No. 18-cv-00274 (N.D. Cal.); and Genentech, Inc. v.
`Celltrion, Inc., No. 18-cv-00095 (D. Del.). Paper 7, 5; Paper 8, 3;
`Paper 16, 2.
`Petitioner has concurrently filed IPR2017-02031, challenging the
`same claims of the ’213 patent based on different prior art references.
`Paper 1, 2.
`
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`2
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`IPR2017-02032
`Patent 6,407,213 B1
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`
`The ’213 patent is the subject of IPR2016-01693 and IPR2016-01694,
`filed by Mylan Pharmaceuticals Inc. Paper 1, 2. We terminated those two
`proceedings before issuing an institution decision because the parties settled.
`Mylan Pharm. Inc. v. Genentech, Inc., IPR2016-01693 (PTAB March 10,
`2017) (Paper 24); IPR2016-01694 (PTAB March 10, 2017) (Paper 23).
`The ’213 patent is also the subject of the following pending matters:
`IPR2017-01373 and IPR2017-01374 brought by Celltrion, Inc.; and
`IPR2017-01488 and IPR2017-01489 brought by Pfizer, Inc. We previously
`instituted inter partes reviews in those cases, and joined IPR2017-02139 and
`IPR2017-02140, brought by Samsung Bioepis Co., Ltd., to IPR2017-01488
`and IPR2017-01489, respectively.
`The ’213 Patent and Relevant Background
`The ’213 patent relates to “methods for the preparation and use of
`variant antibodies and finds application particularly in the fields of
`immunology and cancer diagnosis and therapy.” Ex. 1001, 1:12–14.
`A naturally occurring antibody (immunoglobulin) comprises two
`heavy chains and two light chains. Id. at 1:18–20. Each heavy chain has a
`variable domain (VH) and a number of constant domains. Id. at 1:21–23.
`Each light chain has a variable domain (VL) and a constant domain. Id. at
`1:23–24.
`The variable domains are involved directly in binding the antibody to
`the antigen. Id. at 1:36–38. Each variable domain “comprises four
`framework (FR) regions, whose sequences are somewhat conserved,
`connected by three hyper-variable or complementarity determining regions
`(CDRs).” Id. at 1:40–43. The constant domains are not involved directly in
`
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`IPR2017-02032
`Patent 6,407,213 B1
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`binding the antibody to an antigen, but are involved in various effector
`functions. Id. at 1:33–34.
`Before the ’213 patent, monoclonal antibodies targeting a specific
`antigen, obtained from animals, such as mice, had been shown to be
`antigenic in human clinical use. Id. at 1:51–53. The ’213 patent recognizes
`efforts to construct chimeric antibodies and humanized antibodies in the
`prior art. Id. at 1:59–2:52. According to the ’213 patent, chimeric
`antibodies are “antibodies in which an animal antigen-binding variable
`domain is coupled to a human constant domain” (id. at 1:60–62), whereas
`“humanized antibodies are typically human antibodies in which some CDR
`residues and possibly some FR residues are substituted by residues from
`analogous sites in rodent antibodies” (id. at 2:32–35).
`The ’213 patent also acknowledges the following as known in the
`prior art:
`In certain cases, in order to transfer high antigen binding
`1.
`affinity, it is necessary to not only substitute CDRs, but also replace one or
`several FR residues from rodent antibodies for the human CDRs in human
`frameworks. Id. at 2:53–61.
`“For a given antibody[,] a small number of FR residues are
`2.
`anticipated to be important for antigen binding” because they either directly
`contact antigen or “critically affect[] the conformation of particular CDRs
`and thus their contribution to antigen binding.” Id. at 2:62–3:8.
`In a few instances, a variable domain “may contain
`3.
`glycosylation sites, and that this glycosylation may improve or abolish
`antigen binding.” Id. at 3:9–12.
`
`
`
`4
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`IPR2017-02032
`Patent 6,407,213 B1
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`
`The function of an antibody is dependent on its three-
`4.
`dimensional structure, and amino acid substitutions can change the three-
`dimensional structure of an antibody. Id. at 3:40–43.
`The antigen binding affinity of a humanized antibody can be
`5.
`increased by mutagenesis based upon molecular modelling. Id. at 3:44–46.
`Despite such knowledge in the field, according to the ’213 patent, at
`the time of its invention, humanizing an antibody with retention of high
`affinity for antigen and other desired biological activities was difficult to
`achieve using then available procedures. Id. at 3:50–52. The ’213 patent
`purportedly provides methods for rationalizing the selection of sites for
`substitution in preparing humanized antibodies and, thereby, increasing the
`efficiency of antibody humanization. Id. at 3:53–55. This involves:
`
`a. obtaining the amino acid sequences of at least a portion of an
`import antibody variable domain and of a consensus variable
`domain;
`b. identifying Complementarity Determining Region (CDR)
`amino acid sequences in the import and the human variable
`domain sequences;
`c. substituting an import CDR amino acid sequence for the
`corresponding human CDR amino acid sequence;
`d. aligning the amino acid sequences o( a Framework Region
`(FR) of the import antibody and the corresponding FR of the
`consensus antibody;
`e. identifying import antibody FR residues in the aligned FR
`sequences that are non-homologous to the corresponding
`consensus antibody residues;
`f. determining if the non-homologous import amino acid residue
`is reasonably expected to have at least one of the following
`effects:
`1. non-covalently binds antigen directly,
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`IPR2017-02032
`Patent 6,407,213 B1
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`
`2. interacts with a CDR; or
`3. participates in the VL-VH interface; and
`g. for any non-homologous import antibody amino acid residue
`which is reasonably expected to have at least one of these effects,
`substituting that residue for the corresponding amino acid
`residue in the consensus antibody FR sequence.
`Id. at 4:43–5:5.
`Figures 1A and 1B of the ’213 patent show alignments of light and
`heavy chain variable regions of mouse antibody muMAb4D5 with human
`antibody huMAb4D5, along with their resulting consensus sequences
`(HUVLκI and HUVHIII), respectively. Id. at 6:57–7:8.
`Illustrative Claim
`Among the challenged claims, claims 1, 62–64, 66, and 80 are
`independent. Claim 1 is illustrative and is reproduced below:
`1.
`A humanized antibody variable domain comprising non-
`human Complementarity Determining Region (CDR) amino acid
`residues which bind an antigen incorporated into a human
`antibody variable domain, and further comprising a Framework
`Region (FR) amino acid substitution at a site selected from the
`group consisting of: 4L, 38L, 43L, 44L, 58L, 62L, 65L, 66L,
`67L, 68L, 69L, 73L, 85L, 98L, 2H, 4H, 36H, 39H, 43H, 45H,
`69H, 70H, 74H, and 92H, utilizing the numbering system set
`forth in Kabat.
`Asserted Grounds of Unpatentability
`Petitioner asserts the following grounds of unpatentability:
`Ground
`Claim(s)
`Basis
`Reference(s)
`1
`1, 2, 25, 29, 63, 66, 67,
`§ 103
`Queen 19891 and Protein
`71–73, 75–78, 80, 81
`Data Bank (PDB database)
`
`
`1 Queen et al., A Humanized Antibody that Binds to the Interleukin 2
`Receptor, 86 PRO. NAT’L ACAD. SCI. 10029–33 (1989) (Ex. 1034).
`6
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`IPR2017-02032
`Patent 6,407,213 B1
`
`
`Ground
`2
`
`3
`
`4
`
`5
`
`6
`
`Claim(s)
`1, 2, 4, 25, 29, 62–64,
`66, 67, 69, 71–73, 75–
`78, 80, 81
`75–77
`
`75–77
`
`4, 62, 64, 69
`
`1, 2, 4, 25, 29, 62–64,
`66, 67, 69, 71, 73, 75–
`78, 80, 81
`
`Basis
`§ 103
`
`Reference(s)
`Queen 19902 and PDB
`database
`
`§ 103 Queen 1989, PDB database,
`and Tramontano3
`§ 103 Queen 1990, PDB database,
`and Tramontano
`§ 103 Queen 1989, PDB database,
`and Kabat 19874
`The ’101 patent5
`
`§ 102
`
`Pet. 4.
`In support of its patentability challenges, Petitioner relies on the
`Declaration of Dr. Geoffrey Hale (Ex. 1003).
`ANALYSIS
`Grounds 1–5
`Patent Owner requests that we exercise our discretion under
`35 U.S.C § 325(d) to deny institution with respect to Grounds 1–5 because
`“Boehringer copied Grounds 1–5 of this Petition from IPR2017-01373
`
`
`2 Queen et al., International Publication No. WO 90/07861 A1, published
`July 26, 1990 (Ex. 1050).
`3 Tramontano et al., Framework Residue 71 is a Major Determinant of the
`Position and Conformation of the Second Hypervariable Region in the VH
`Domains of Immunoglobulins, 215 J. MOL. BIOL. 175–82 (1990) (Ex. 1051).
`4 Kabat et al., Sequences of Proteins of Immunological Interest 4th Ed.,
`Tabulation and Analysis of Amino Acid and Nucleic Acid Sequences of
`Precursors, V-Regions, C-Regions, J-Chain, T-Cell Receptor for Antigen, T-
`Cell Surface Antigens (National Institutes of Health, Bethesda, Md.) (1987)
`(Ex. 1052).
`5 U.S. Patent No. 5,530,101, issued June 25, 1996 (Ex. 1136).
`7
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`IPR2017-02032
`Patent 6,407,213 B1
`
`(Celltrion) and IPR2017-01489 (Pfizer), and copied Grounds 1–3 and 5 of
`IPR2017-02031 from IPR2017-01374 (Celltrion) and IPR2017-01488
`(Pfizer)—without seeking joinder with those earlier-filed proceedings.”
`Prelim. Resp. 1. According to Patent Owner, “[t]his redundancy would
`waste the Board’s and Patent Owner’s resources, and also would unfairly
`allow Boehringer to preview the parties’ arguments before having to address
`them itself.” Id. at 2. We find Patent Owner’s argument persuasive.
`In determining whether to institute an inter partes review, we “may
`take into account whether, and reject the petition or request because, the
`same or substantially the same prior art or arguments previously were
`presented to the Office.” 35 U.S.C. § 325(d). As Patent Owner correctly
`points out, Grounds 1–5 asserted in the Petition “are essentially identical to
`those already instituted in” IPR2017-01373 and IPR2017-01489. Prelim.
`Resp. 12–13. Petitioner filed this Petition before we issued the decisions
`instituting inter partes reviews in IPR2017-01373 and IPR2017-01489.
`Thus, Petitioner could have sought to join the pending IPRs. Yet, it did not
`do so. See 37 C.F.R. § 42.122. The time for requesting joinder has since
`expired. See id. As such, we exercise our discretion under § 325(d) and
`deny the Petition with respect to Grounds 1–5.
`Ground 6: Anticipation by the ’101 Patent
`Petitioner asserts that claims 1, 2, 4, 25, 29, 62–64, 66, 67, 69, 71, 73,
`75–78, 80, and 81 are anticipated by the ’101 patent. Pet. 52–60. Patent
`Owner does not respond on the merits, but argues that that we should deny
`institution of this ground under § 325(d). Prelim. Resp. 15–17. We address,
`in turn, Patent Owner’s § 325(d) argument and the merits of Petitioner’s
`challenge.
`
`
`
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`IPR2017-02032
`Patent 6,407,213 B1
`
`§ 325(d)
`Patent Owner argues that we should deny ground 6 because “the PTO
`Already Determined that the ’101 Patent is Not Prior Art.” Prelim. Resp. 15.
`According to Patent Owner, the ’101 patent “was not only specifically raised
`during prosecution, but antedated by Patent Owner.” Id. As a result, Patent
`Owner contends that we should deny ground 6 under § 325(d). Id. at 16–17.
`We are not persuaded.
`During prosecution, the examiner rejected the then pending claims
`under 35 U.S.C. 102(e) as anticipated by the ’101 patent. Ex. 1002, 738–40.
`In response, the applicant submitted a Declaration under 37 C.F.R. §1.131,
`swearing behind the reference. Id. at 802–03. In the Declaration, the
`inventors stated that, prior to September 28, 1990, they had conceived and
`reduced to production a humanized antibody comprising “a[n] FR amino
`acid substitution at site 73H.” Id. at 803. Thereafter, the examiner allowed
`the claims. Id. at 835.
`Claim 1 recites an FR “amino acid substitution at a site selected from
`the group consisting of: 4L, 38L, 43L, 44L, 58L, 62L, 65L, 66L, 67L, 68L,
`69L, 73L, 85L, 98L, 2H, 4H, 36H, 39H, 43H, 45H, 69H, 70H, 74H, and
`92H.” Because 73H is not recited in the challenged claim 1, the § 1.131
`Declaration submitted during prosecution cannot antedate the ’101 patent.6
`
`
`6 We acknowledge that certain challenged claims, such as claims 66 and 80,
`recite amino acid substitution at site 73H as a member of a Markush group.
`For purpose of this Decision, however, we do not need to decide whether the
`§ 1.131 Declaration is sufficient to antedate those claims. See 35 U.S.C.
`§ 314(a) (authorizing institution when “there is a reasonable likelihood that
`the petitioner would prevail with respect to at least 1 of the claims
`challenged in the petition”).
`
`9
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`IPR2017-02032
`Patent 6,407,213 B1
`
`As a result, we decline to exercise our discretion under § 325(d) to deny
`ground 6.
`Prior-Art Status of the ’101 patent
`Patent Owner argues that Petitioner “failed to meet its burden to
`establish that the ’101 patent is prior art.” Prelim. Resp. 16.
`In an inter partes review, the burden of persuasion is on the petitioner
`to prove unpatentability by a preponderance of the evidence, and that burden
`never shifts to the patentee. Dynamic Drinkware, LLC v. Nat’l Graphics,
`Inc., 800 F.3d 1375, 1378 (Fed. Cir. 2015). The petitioner also has the
`initial burden of production to show that an asserted reference qualifies as
`prior art under 35 U.S.C. § 102. Id. at 1378–79. Once the petitioner has met
`that initial burden, the burden of production shifts to the patent owner to
`argue or produce evidence that either the asserted reference does not render
`the challenged claims unpatentable, or the reference is not prior art. Id.
`(citing Tech. Licensing Corp. v. Videotek, Inc., 545 F.3d 1316, 1327 (Fed.
`Cir. 2008)).
`The ’101 patent issued from an application No. 07/634,278, which
`was filed on December 19, 1990 and claims priority to a series of earlier
`applications. Ex. 1136, [63], 1:6–11. The earliest possible priority date of
`the challenged claims is June 14, 1991. Ex. 1001, (21), (63). Thus, we
`determine that Petitioner has satisfied its initial burden of showing that the
`’101 patent qualifies under § 102(e) as prior art to at least challenged
`claim 1.
`Claim Construction
`In an inter partes review, the Board interprets a claim term in an
`unexpired patent according to its broadest reasonable construction in light of
`10
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`IPR2017-02032
`Patent 6,407,213 B1
`
`the specification of the patent in which it appears. 37 C.F.R. § 42.100(b);
`Cuozzo Speed Techs., LLC v. Lee, 136 S. Ct. 2131, 2144–46 (2016). Under
`that standard, and absent any special definitions, we assign claim terms their
`ordinary and customary meaning, as would be understood by one of ordinary
`skill in the art at the time of the invention, in the context of the entire patent
`disclosure. In re Translogic Tech., Inc., 504 F.3d 1249, 1257 (Fed. Cir.
`2007).
`Claim 1 of the ’231 patent recites “[a] humanized antibody variable
`domain . . . comprising a Framework Region (FR) amino acid substitution at
`a site selected from the group consisting of: 4L, 38L, 43L, 44L, 58L, 62L,
`65L, 66L, 67L, 68L, 69L, 73L, 85L, 98L, 2H, 4H, 36H, 39H, 43H, 45H,
`69H, 70H, 74H, and 92H.” Depending from claim 1, claim 4 limits the
`humanized antibody variable domain of claim 1 to “a consensus human
`variable domain.”7
`Petitioner reasons that “[b]ecause claim 1 requires substitutions in the
`variable domain, claim 4 must also require substitutions in the variable
`domain” such that the claim “encompass[] humanized antibody variable
`domains where only some of the residues in the sequence are ‘consensus’
`residues, and where other, non-consensus residues are ‘substitutions’ in the
`consensus sequence.” Pet. 7–8.
`
`
`7 Although we focus our analysis on claim 4, similar usages are found
`throughout the challenged claims. Claim 64, for example, recites “a human
`variable domain comprising the most frequently occurring amino acid
`residues at each location in all human immunoglobulins of a human heavy
`chain immunoglobulin subgroup . . . compris[ing] a Framework Region (FR)
`substitution.”
`
`11
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`IPR2017-02032
`Patent 6,407,213 B1
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`
`Petitioner further argues “substitution,” and the related term
`“substituted,” do not require the intentional replacement of amino acids in a
`human consensus variable domain. See id. at 8–9. Rather, Petitioner argues,
`as used in the challenged claims, these terms invoke product-by-process
`limitations, which should be disregarded in the patentability analysis. Id. at
`8, 53 (citing Purdue Pharma L.P. v. Epic Pharma, LLC, 811 F.3d 1345,
`1353–54 (Fed. Cir. 2016); Ex. 1003 ¶ 321). Taken together, Petitioner
`argues that “any differences from the consensus sequence can be considered
`a ‘substitution’ of the consensus residue for a non-consensus reside, whether
`or not it was deliberately placed.” Id. at 55.
`Based on the current record, and for purposes of this Decision, we
`find Petitioner’s argument reasonable and adopt Petitioner’s interpretation of
`“substitution.” We further construe claim 4 as encompassing humanized
`variable domains where only some of the residues in the sequence are amino
`acids of a consensus human variable domain.
`Based on the current record, and for purposes of this Decision, no
`other claim term requires express construction. See Wellman, Inc. v.
`Eastman Chem. Co., 642 F.3d 1355, 1361 (Fed. Cir. 2011) (instructing that
`claim terms need only be construed to the extent necessary to resolve the
`controversy).
`Analysis of Ground 6
`Petitioner contends that “a prior art antibody prepared without
`intentional substitutions, but with the same sequence (and thus structure and
`function) as an antibody prepared according to the claims of the ’213 patent,
`would anticipate those claims.” Pet. 54. According to Petitioner, “[t]he
`’101 patent discloses just such a prior art antibody.” Id.
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`IPR2017-02032
`Patent 6,407,213 B1
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`
`The ’101 patent discloses “humanized immunoglobulins having one
`or more complementarity determining regions (CDR’s) and possible
`additional amino acids from a donor immunoglobulin and a framework
`region from an accepting human immunoglobulin.” Ex. 1136, Abstract.
`Specifically, the ’101 patent discloses a humanized CMV5 antibody. Id. at
`60:45–64:26.
`Petitioner refers us to Hale Exhibit R, which allegedly compares the
`consensus sequence (as shown in Fig 1A of the ’213 patent) with the
`sequences of Wo1, mouse CMV5, and humanized CMV5 (as shown in
`Figures 6A and 40A of the ’101 patent). Pet. 54–55. According to
`Petitioner, “this comparison [shows] there are both consensus and non-
`consensus residues in the humanized CMV5 variable domain.” Id. at 55.
`Relying on the testimony of Dr. Hale, Petitioner argues that the ’101 patent
`discloses humanized CMV5 antibody with substitutions “at least at
`4L;58L;85L; and 69H,” among which “[a]t least residues 4L;58L; and 69H
`are the same as the corresponding murine residue at those locations. Pet. 54
`(citing Ex. 1003 ¶ 126; Ex. 1003C, 780 (Hale Exhibit R)), see also id. at 23
`(the same). Because 4L, 58L, and 69H are members of the Markush group
`recited in claim 1, Petitioner argues that the ’101 patent anticipates that
`claim. Id. at 55; see also Ex. 1003 ¶ 321 (“[S]o long as the humanized
`variable domain disclosed by the ’101 patent differs with the consensus
`variable domain at least at one of the sites recited by claim 1, then the ’101
`patent meets the requirement for a ‘Framework Region (FR) amino acid
`substitution’ at that site.”).
`Based on the current record, we find Petitioner’s arguments
`persuasive. Because we determine that Petitioner has shown a reasonable
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`IPR2017-02032
`Patent 6,407,213 B1
`
`likelihood that it would prevail in showing the unpatentability of at least
`claim 1 of the ’231 patent, we institute inter partes review to determine
`whether claims 1, 2, 4, 25, 29, 62–64, 66, 67, 69, 71, 73, 75–78, 80, and 81
`are anticipated by the ’101 patent.
`CONCLUSION
`For the foregoing reasons, the information presented in the Petition
`and accompanying evidence establishes a reasonable likelihood that
`Petitioner would prevail in showing the unpatentability of at least one
`challenged claim.
`At this stage of the proceeding, the Board has not made a final
`determination as to the construction of any claim term or the patentability of
`any challenged claim.
`
`ORDER
`
`Accordingly, it is
`ORDERED that pursuant to 35 U.S.C. § 314, an inter partes review is
`hereby instituted to determine whether claims 1, 2, 4, 25, 29, 62–64, 66, 67,
`69, 71, 73, 75–78, 80, and 81 are anticipated by the ’101 patent;
`FURTHER ORDERED that no other ground of unpatentability is
`authorized in this inter partes review;
`FURTHER ORDERED that pursuant to 35 U.S.C. § 314(a), inter
`partes review of the ’213 patent is hereby instituted commencing on the
`entry date of this Order, and pursuant to 35 U.S.C. § 314(c) and 37 C.F.R.
`§ 42.4, notice is hereby given of the institution of a trial.
`
`
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`IPR2017-02032
`Patent 6,407,213 B1
`
`PETITIONER:
`Ire J. Levy
`Brian A. Fairchild
`GOODWIN PROCTER LLP
`ilevy@goodwinlaw.com
`bfairchild@goodwinlaw.com
`
`PATENT OWNER:
`David L. Cavanaugh
`Rebecca A. Whitfield
`WILMER CUTLER PICKERING HALE AND DORR LLP
`david.cavanaugh@wilmerhale.com
`Rebecca.Whitfield@wilmerhale.com
`
`Adam R. Brausa
`DURIE TANGRI LLP
`abrausa@durietangri.com
`
`
`
`15
`
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