NOTE: This disposition is nonprecedential.
`United States Court of Appeals
`for the Federal Circuit
`______________________
`
`AMGEN INC., AMGEN MANUFACTURING
`LIMITED,
`Plaintiffs-Appellants
`
`v.
`
`APOTEX INC., APOTEX CORP.,
`Defendants-Appellees
`______________________
`
`2017-1010
`______________________
`
`Appeal from the United States District Court for the
`Southern District of Florida in Nos. 0:15-cv-61631-JIC,
`0:15-cv-62081-JIC, Judge James I. Cohn.
`______________________
`
`Decided: November 13, 2017
`______________________
`
` NICHOLAS P. GROOMBRIDGE, Paul, Weiss, Rifkind,
`Wharton & Garrison LLP, New York, NY, argued for
`plaintiffs-appellants.
` Also represented by JENNIFER
`GORDON, ARIELLE K. LINSEY, STEPHEN ACCURSIO
`MANISCALCO, CATHERINE NYARADY, PETER SANDEL, ERIC
`ALAN STONE, JENNIFER H. WU; JOHN F. O’SULLIVAN,
`ALLEN P. PEGG, JASON STERNBERG, Hogan Lovells US
`LLP, Miami, FL; LOIS M. KWASIGROCH, KIMBERLIN L.
`
`Amgen
`Exhibit 2065
`Apotex Inc., et al. v. Amgen Inc., et al.
`IPR2016-01542
`
`Ex. 2065-001
`
`

`

`
`
` 2
`
` AMGEN INC. v. APOTEX INC.
`
`MORLEY, WENDY A. WHITEFORD, Amgen Inc., Thousand
`Oaks, CA.
`
`BARRY P. GOLOB, Cozen O’Connor, Washington, DC,
`
`argued for defendants-appellees. Also represented by
`WILLIAM BLAKE COBLENTZ, AARON S. LUKAS, KERRY
`BRENDAN MCTIGUE.
`______________________
`
`Before LOURIE, O’MALLEY, and TARANTO, Circuit
`Judges.
`
`TARANTO, Circuit Judge.
`Amgen Inc. and Amgen Manufacturing Limited (col-
`lectively, Amgen) own U.S. Patent No. 8,952,138, which
`describes and claims methods of refolding recombinant
`proteins expressed in non-mammalian cells, such as
`bacteria and yeast. ’138 Patent, col. 1, lines 10–20; col. 2,
`lines 52–61. Amgen also holds Biologics License Applica-
`tion Nos. 125031 and 103353, approved by the Food and
`Drug Administration (FDA), for therapeutic products
`made
`from the recombinant proteins pegfilgrastim
`(Neulasta®) and filgrastim (Neupogen®).
`Apotex Inc. and Apotex Corp. (collectively, Apotex)
`filed abbreviated Biologics License Applications Nos.
`761026 and 761027 under 42 U.S.C. § 262(k) of the Bio-
`logics Price Competition and Innovation Act (BPCIA),
`seeking permission from the FDA to market biosimilar
`versions of pegfilgrastim and filgrastim products, and
`listing Neulasta® and Neupogen®, respectively, as the
`reference products. Apotex and Amgen then engaged in
`the information exchange described in the BPCIA, 42
`U.S.C. § 262(l)(3). After Apotex provided Amgen with
`copies of its applications, Amgen identified the ’138 patent
`as a patent that the Apotex-proposed products would
`infringe, and Apotex replied by sending Amgen a detailed
`statement describing, claim by claim, the factual and
`
`Ex. 2065-002
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`3
`
`legal basis for its opinion that it did not infringe. Amgen
`responded with its contrary, detailed view of infringe-
`ment. Amgen eventually filed two infringement suits
`against Apotex, one for each of Apotex’s applications,
`pursuant to 35 U.S.C. § 271(e)(2)(C), (a) and (g).
`The two suits were consolidated. The district court
`held a bench trial in July 2016, and it issued findings of
`fact and conclusions of law on September 6, 2016. The
`court found that Amgen had failed to prove that Apotex’s
`proposed commercial marketing of the two products,
`pursuant to Apotex’s applications, would infringe the ’138
`patent, either literally or under the doctrine of equiva-
`lents.
`Amgen appeals. We have jurisdiction under 28 U.S.C.
`§ 1295(a)(1). We affirm.
`
`I
`A
`The ’138 patent explains that when recombinant pro-
`teins are formed in non-mammalian expression systems,
`such as bacterial cells, they can precipitate into limited-
`solubility aggregates of misfolded proteins called “inclu-
`sion bodies.” ’138 patent, col. 1, lines 20–24. To obtain
`properly folded proteins from inclusion bodies, practition-
`ers developed various methods to accomplish refolding.
`Id., col. 1, lines 36–38. Those methods, the patent ex-
`plains, commonly include steps of (1) extracting the
`inclusion bodies from the expression system; (2) solubiliz-
`ing the inclusion bodies in a solubilization buffer, which
`disassembles the inclusion bodies into individual protein
`chains and unfolds the proteins; and (3) diluting or wash-
`ing the unfolded proteins in a refolding buffer, which
`causes the proteins to refold in the proper manner. Id.,
`col. 1, lines 38–51.
`Industry faced a challenge in producing certain re-
`folded proteins on an industrial scale. Id., col. 1, lines 55–
`
`Ex. 2065-003
`
`

`

`
`
` 4
`
` AMGEN INC. v. APOTEX INC.
`
`60. For larger, complicated molecules (e.g., antibodies
`and peptibodies, which often have between 8 and 24
`disulfide bonds), the refolding mixture used for the pro-
`cess had to be maintained at a relatively low protein
`concentration, typically 0.01–0.5 g/L. Id., col. 1, lines 51–
`54; col. 2, lines 10–16. As a result, a very large volume of
`the mixture was required to produce a large amount of
`the desired protein. Id., col. 1, lines 55–60; see also id.,
`col. 1, lines 64–67.
`The ’138 patent purports to solve this problem by us-
`ing a carefully controlled reduction-oxidation (redox)
`reaction to refold proteins—even
`large, complicated
`protein molecules—at a higher concentration than was
`possible in the prior art. Claim 1, the ’138 patent’s only
`independent claim, reads as follows:
`1. A method of refolding a protein expressed in a
`non-mammalian expression system and present in
`a volume at a concentration of 2.0 g/L or greater
`comprising:
`(a) contacting the protein with a refold
`buffer comprising a redox component com-
`prising a final thiol-pair ratio having a
`range of 0.001 to 100 and a redox buffer
`strength of 2 mM or greater and one or
`more of:
`(i) a denaturant;
`(ii) an aggregation suppressor; and
`(iii) a protein stabilizer;
`to form a refold mixture;
`(b) incubating the refold mixture; and
`(c) isolating the protein from the refold
`mixture.
`Id., col. 17, lines 47–59.
`
`Ex. 2065-004
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`5
`
`B
`Claim 1, in its preamble (which all agree is limiting),
`calls for protein present in “a volume at a concentration of
`2.0 g/L or greater.” Id., col. 17, line 49. During claim
`construction, Amgen argued that the claimed “volume”
`was the volume of protein before, not after, the contact
`with the refolding buffer that forms the refold mixture.
`Amgen also argued, based on the specification, that the
`“refold mixture,” as a matter of claim construction, must
`have a protein concentration at or above about 1.0 g/L.
`Apotex, for its part, contended that the claim 1 “volume”
`refers to the refold mixture, so that the claimed refold
`mixture must have a protein concentration of 2.0 g/L or
`more. The district court agreed with Amgen on both
`points, construing “a protein . . . present in a volume at a
`concentration of 2.0 g/L or greater” to mean “a protein as
`it existed in a volume before contacting the volume with a
`refold buffer” and construing “refold mixture” to have a
`“high protein concentration[] . . . at or above about 1 g/L.”
`C
`For the 1.0 g/L claim requirement, Amgen alleged on-
`ly literal infringement, not infringement under the doc-
`trine of equivalents. In seeking to prove that Apotex’s
`accused processes meet this claim requirement, Amgen
`relied at trial on the fact that Apotex’s abbreviated Biolog-
`ics License Applications identified an “inclusion body
`concentration” of 0.9–1.4 g/L for the refold mixture in its
`processes for refolding filgrastim and pegfilgrastim. J.A.
`23–24, 5594, 5902. In the BPCIA information exchange
`that occurred before this suit was filed, Apotex had sent
`Amgen several “pre-litigation” letters, at least one with
`respect to the filgrastim application and one with respect
`to the pegfilgrastim application. In both letters, Apotex
`stated that it did not infringe the ’138 patent because its
`“concentration of [filgrastim or filgrastim critical inter-
`mediate] in the refold buffer” was limited to 0.9–1.4 g/L
`
`Ex. 2065-005
`
`

`

`
`
` 6
`
` AMGEN INC. v. APOTEX INC.
`
`(i.e., the “inclusion body concentration” listed on the
`applications).
`At trial, however, Apotex’s fact witness, Dr. Jason
`Dowd, presented evidence that the maximum concentra-
`tion of protein in its refold mixture would actually be
`0.708 g/L. Dr. Dowd testified, during cross examination,
`that the statements in Apotex’s pre-litigation letters were
`factually inaccurate. He explained that the inclusion
`bodies in Apotex’s process were not pure protein, but,
`rather, were a paste of which about two-thirds was water.
`In addition, to resolve any potential ambiguity created by
`the numbers presented on the face of its application,
`Apotex presented two “batch records” showing the actual
`data from the manufacturing process of its filgrastim
`product. According to Dr. Dowd, those records showed
`that the protein (not the inclusion-body) concentration in
`the refold mixture never exceeded about 0.56 g/L. Both
`that figure and the 0.708 g/L figure are well below the 1.0
`g/L minimum level required under the Amgen-urged and
`court-adopted claim construction.
`The court ruled in favor of Apotex on this issue. It
`found that Amgen had failed to prove by a preponderance
`of the evidence that Apotex’s processes would meet the 1.0
`g/L requirement of claim 1 of the ’138 patent. For that
`reason, the court found, Amgen failed to prove direct
`infringement.
`On Amgen’s appeal, we affirm that finding. We there-
`fore need not and do not reach Amgen’s challenge to the
`district court’s other, independent ground for finding no
`infringement, which involves the claim term “2mM or
`greater.” In particular, we do not decide the correctness
`or incorrectness of the district court’s construction of that
`claim term.
`
`Ex. 2065-006
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`7
`
`II
`Amgen challenges the district court’s finding of no di-
`rect infringement of the ’138 patent on three grounds: (1)
`that the district court erred in finding Apotex’s pre-
`litigation letters to lack probative value; (2) that the
`district court erred in not treating “protein concentration”
`as interchangeable with “inclusion body concentration”;
`and (3) that the district court erred in not finding the
`required 1.0 g/L protein concentration based on what
`Apotex’s abbreviated Biologics License Applications
`permit. We review the finding of non-infringement for
`clear error, Alza Corp. v. Mylan Labs., Inc., 464 F.3d
`1286, 1289 (Fed. Cir. 2006), and we decide any legal
`issues de novo, Jack Guttman, Inc. v. Kopykake Enters.,
`Inc., 302 F.3d 1352, 1356 (Fed. Cir. 2002).
`A
`Amgen first focuses on the pre-litigation letters sent
`by Apotex to Amgen during the information exchange
`conducted before the litigation pursuant to the BPCIA.
`Amgen does not argue that Apotex is legally bound by its
`statements about protein concentration in those letters;
`indeed, both in the district court and in this court, Amgen
`has disclaimed such an argument. See J.A. 3807; Reply
`Br. 17–18. Rather, Amgen argues that the district court,
`acting as fact-finder during the bench trial, erred by
`disregarding those letters.
`We do not question the general legal principle that
`Amgen asserts: we agree that a district court cannot
`ignore letters sent during the BPCIA’s information ex-
`change if properly offered into evidence. Indeed, the pre-
`litigation information exchange is part of the BPCIA’s
`“carefully calibrated scheme for preparing to adjudicate,
`and then adjudicating, claims of infringement.” Sandoz
`Inc. v. Amgen Inc., 137 S. Ct. 1664, 1670 (2017). The
`purpose of the exchange is “to identify relevant patents
`and to flesh out the legal arguments that the[] [parties]
`
`Ex. 2065-007
`
`

`

`
`
` 8
`
` AMGEN INC. v. APOTEX INC.
`
`might raise in future litigation.” Id. at 1671. Through
`the information exchange, the BPCIA seeks to facilitate
`the efficient resolution of patent disputes. The state-
`ments in the pre-litigation letters are party admissions
`and therefore have some probative weight. The district
`court’s statement that the letters “are not probative on
`the issue of protein concentration,” J.A. 24 ¶ 39, is there-
`fore an overstatement to the extent it suggests that the
`letters lack probative value as a matter of law.
`We read the district court’s statement in context,
`however, to mean only that the letters are not sufficiently
`probative to outweigh other evidence presented at trial
`indicating that the information in the letters was inaccu-
`rate. Indeed, the district court did not ignore the pre-
`litigation letters. Rather, it first concluded that the
`letters were not binding on Apotex, a conclusion that
`Amgen does not dispute, and it then found that the letters
`lacked probative value in light of the other evidence
`presented at trial. Thus, the court gave the letters their
`evidentiary due. We do not believe that the court’s phras-
`ing reflects an error in the approach it actually took to
`reach its findings or calls the court’s ultimate conclusion
`into question.
`The letters do not render the finding of fact regarding
`the protein concentration clearly erroneous. The district
`court found that the letters were “not probative on the
`issue of protein concentration” because they were “factual-
`ly incorrect,” J.A. 24, and it had a sufficient basis in the
`evidence to make that finding. On direct examination,
`Dr. Dowd testified that the inclusion bodies produced by
`the Apotex process are wet—i.e., a paste. He then testi-
`fied that, based on the description of the refolding process
`given in Apotex’s abbreviated Biologics License Applica-
`tions, the maximum protein concentration that could
`occur in Apotex’s process is 0.708 g/L. On cross examina-
`tion, when asked about the pre-litigation letters, Dr.
`Dowd stated that the letters were factually incorrect.
`
`Ex. 2065-008
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`9
`
`That is, he reiterated that his calculation of a 0.708 g/L
`protein concentration was accurate and that the 0.9–1.4
`g/L mentioned in the letter was not. Amgen did not
`attempt to challenge the accuracy of Dr. Dowd’s state-
`ments regarding the pre-litigation letters during cross-
`examination. Amgen also did not present any evidence,
`other than the pre-litigation letters themselves, to con-
`tradict Dr. Dowd’s statements.
`On this record, we conclude that the district court did
`not err by crediting Dr. Dowd’s testimony and finding that
`the factually inaccurate letters were not probative on the
`issue of the protein concentration.
`B
`Amgen argues, as a matter of claim construction, that
`“protein concentration” in the claims of the ’138 patent is
`interchangeable with “washed-inclusion-body concentra-
`tion.” We review this claim-construction argument, which
`rests entirely on intrinsic evidence, de novo. Teva Pharm.
`USA, Inc. v. Sandoz, Inc., 135 S. Ct. 831, 841 (2015). We
`reject the argument.
`Amgen’s argument depends on its equating of inclu-
`sion bodies with protein. Only on that basis does Amgen
`then treat the concentration of one as necessarily identi-
`cal to the concentration of the other. But the specification
`pervasively disproves rather than supports the equation
`of inclusion bodies with proteins.
`The specification repeatedly makes clear that the pro-
`teins are not the same as, but instead are “in” or “depos-
`it[ed] . . . into” or “disposed in,” the “aggregates” called
`“inclusion bodies.” See, e.g., ’138 patent, col. 1, lines 23–
`25 (“the precipitation of the expressed proteins in limited-
`solubility intracellular precipitates typically referred to as
`inclusion bodies”); id., col. 9, lines 44–46 (“Often the cells
`will deposit the recombinant proteins into large insoluble
`or limited solubility aggregates called inclusion bodies.”);
`
`Ex. 2065-009
`
`

`

`
`
` 10
`
` AMGEN INC. v. APOTEX INC.
`
`id., col. 10, lines 43–44 (“disposed in”); id., col. 1, lines 23,
`38–44; id., col. 7, line 59–60; id., col. 9, line 50; id., col. 12,
`line 61–62. Amgen’s own description reflects that fact.
`Appellant’s Br. at 9 (“The misfolded proteins precipitate
`within the bacterial cells in aggregates called ‘inclusion
`bodies.’” (emphasis added)). The specification also makes
`clear that it is individual proteins, disaggregated from the
`inclusion bodies, that are refolded. See ’138 patent, col. 1,
`lines 35–51 (background describing methods “for obtain-
`ing correctly folded proteins from bacterial inclusion
`bodies” by, e.g., “solubilizing the inclusion bodies,” “which
`unfolds the proteins and disassembles the inclusion
`bodies into individual protein chains,” allowing the “re-
`folding”); id., col. 2, line 52 (summary: “[a] method of
`refolding a protein” (emphasis added)); id., col. 6, lines
`13–14 (“the term ‘refolding’ means a process of reintroduc-
`ing secondary and tertiary structure to a protein” (em-
`phasis added)). Amgen’s description reflects that fact as
`well. Appellant’s Brief at 9 (“The inclusion bodies must
`be isolated and solubilized so that the incorrectly folded
`proteins are unfolded and subsequently refolded to form
`the proper three-dimensional conformation.”).
`Amgen argues otherwise by first pointing to the
`Background of the ’138 patent, which, according to
`Amgen, shows that “the patent specification contemplates
`that, for purposes of calculating concentration, the pro-
`tein . . . and the inclusion bodies are one and the same.”
`Appellant’s Brief at 52 (internal quotation marks omit-
`ted). But the Background material, quoted above, does
`not support that characterization. Indeed, it speaks of
`proteins “in” inclusion bodies; it does not equate them.
`And it does not mention concentration at all, or give any
`indication that the patent contemplates calculating the
`concentration from the total mass of the inclusions bodies
`rather than from the amount of protein contained in the
`inclusion bodies.
`
`Ex. 2065-010
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`11
`
`Amgen next points to the specification’s description of
`an embodiment of the claimed refolding method, which
`states that “[w]hen the protein is disposed in inclusion
`bodies, the inclusion bodies can be harvested . . . , washed,
`concentrated and refolded.” ’138 Patent, col. 10, lines 39–
`44. Amgen contends that the passage teaches the folding
`and washing of inclusion bodies and therefore must be
`equating inclusion bodies with proteins. But even this
`passage speaks of a protein “disposed in” inclusion bodies,
`thereby recognizing the distinction—as does the usage
`throughout the specification cited above. In this context,
`we read the second half of the sentence as nothing more
`than a somewhat imprecise shorthand reference to a
`process that the rest of the patent makes clear involves
`refolding the proteins, not the aggregates called “inclusion
`bodies.” Accordingly, no inference of equating proteins
`with the aggregates of proteins that are inclusion bodies
`can fairly be drawn from this passage. And the passage
`gives no indication that protein concentration should be
`derived from the concentration of inclusion bodies rather
`than from the proteins contained within the inclusion
`bodies.
`Amgen’s final basis for its contention is no more per-
`suasive. A specification passage states that “the disclosed
`method is particularly useful for proteins expressed in
`bacterial expression systems[] . . . in which the protein is
`expressed in the form of inclusion bodies.” Id., col. 12,
`lines 54–57. But the language of “expressed in the form
`of” does not imply interchangeability, but refers instead to
`the problem of agglomeration that the method is meant to
`help solve: “the precipitation of the expressed proteins in
`limited-solubility
`intracellular precipitates
`typically
`referred to as inclusion bodies,” id., col. 1, lines 22–24,
`which must be disassembled to “unfold[] the proteins”
`contained in them, id., col. 1, line 43, where doing so at an
`industrial scale is challenging. It is not reasonable to
`read the particular language Amgen cites to mean, coun-
`
`Ex. 2065-011
`
`

`

`
`
` 12
`
` AMGEN INC. v. APOTEX INC.
`
`ter to the specification as a whole, that inclusion bodies
`are the proteins inside them, even though there also is
`water and other non-protein content inside them. In
`particular, that reading is wrong in a context of identify-
`ing concentration levels, where the distinction might well
`(and does here) matter.
`Thus, we reject Amgen’s proposed claim construction
`of “protein concentration” as
`interchangeable with
`“washed-inclusion-body concentration.”
`C
`the district court’s non-
`that
`Amgen argues
`infringement finding rests on too restrictive a view of
`Apotex’s FDA applications. It challenges that view as
`contrary to this court’s decision in a Hatch-Waxman Act
`case, Sunovion Pharm., Inc. v. Teva Pharm. USA, Inc.,
`731 F.3d 1271 (Fed. Cir. 2013), under which, Amgen
`argues, the district court here was required to assess
`infringement based on the full range of processes that
`would be consistent with Apotex’s applications. Apotex
`does not challenge the importation of Sunovion’s analysis
`into the BPCIA context, but it does dispute Sunovion’s
`applicability to the facts of this case. We agree with
`Apotex.
`Sunovion involved an abbreviated new drug applica-
`tion that, on its face, authorized the applicant to engage
`in actions that would, in fact, infringe the patent in
`question. Sunovion, 731 F.3d at 1274–75. The district
`court had granted
`summary
`judgment of non-
`infringement because the defendant had “certified” that it
`did not actually intend to run its process in an infringing
`manner and presented evidence of internal manufactur-
`ing guidelines showing non-infringement. Id. This court
`reversed, reasoning that internal guidelines and a certifi-
`cation were insufficient to avoid a finding of infringement
`when the application itself authorized the activity that
`would infringe. Id. at 1280.
`
`Ex. 2065-012
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`13
`
`Here, in contrast, the district court had a sufficient
`basis for reading Apotex’s applications as not authorizing
`processes that infringe, indeed, as constraining the pro-
`cesses to non-infringing levels. The district court credited
`the testimony of Dr. Dowd, based on the numbers in the
`applications, that the maximum protein concentration
`possible in the refold mixtures of Apotex’s applications is
`0.708 g/L. J.A. 3618–20. Dr. Dowd arrived at this calcu-
`lation using the high-end of the “key process parameter”
`range for solubilized inclusion bodies, 11.8 mg/mL, and
`the minimum 75 percent purity of the target protein (i.e.,
`filgrastim or pegfilgrastim) specified by the applications.
`Amgen argues that the key process parameters do not
`prevent Apotex from infringing the ’138 patent because
`they are not absolute limits. But the applications indicate
`that close adherence to the key process parameters is
`critical to the function of the process. J.A. 6725 (noting
`that key process parameters must be “carefully controlled
`within a narrow range and are essential for process
`performance”); J.A. 6728 (identifying the 11.8 mg/ml
`figure as a “qualified upper limit”). Consistent with this
`description, Dr. Dowd testified at trial that Apotex needs
`to maintain its process within the key process parameters
`in order “for the batch to be acceptable,” and that, if those
`ranges are exceeded, “the batch would be thrown out.”
`J.A. 3622–23. The district court found this testimony
`credible. J.A. 26. In light of the evidence, we see no basis
`for deeming the district court’s finding as to the con-
`straints in Apotex’s applications to be clearly erroneous.
`At oral argument in this court, Amgen pointed to the
`fact that Apotex’s applications contain a “dash” in the
`“Acceptance Criterion” column of the solubilized inclusion
`body concentration parameters. See J.A. 5595. Amgen
`argued that the lack of an explicit acceptance criterion
`means that there is effectively no upper bound for the
`concentration of solubilized inclusion bodies—and there-
`fore protein—that can be used in the process. But Amgen
`
`Ex. 2065-013
`
`

`

`
`
` 14
`
` AMGEN INC. v. APOTEX INC.
`
`has given us no evidence to justify setting aside the
`district court’s contrary reading of the applications. The
`dash in Apotex’s applications is not on its face an affirma-
`tive statement authorizing the infringing levels, contrary
`to the other evidence recited above. And Amgen has
`pointed us to no evidence that the dash would be under-
`stood as such an authorization. In these circumstances,
`the content of the applications does not bring this case
`within Sunovion.
`Even if we did not read the applications as affirma-
`tively constraining the processes in the way at issue here,
`the most that we could conclude about the applications is
`that they are silent on the point. In such a case, this
`court’s reasoning in Glaxo, Inc. v. Novopharm, Ltd., 110
`F.3d 1562 (Fed. Cir. 1997), is applicable. In Glaxo, the
`court looked to extrinsic evidence, such as the samples
`and data submitted to the FDA, to resolve a question of
`infringement left open by the abbreviated new drug
`application. Id. at 1569. In this case, Apotex submitted
`batch records of its actual manufacturing process to
`resolve any question of infringement left open by Apotex’s
`application. Between the two batch records submitted by
`Apotex, the maximum protein concentration observed in
`the process was roughly 0.56 g/L—even further from
`infringing levels than the 0.708 g/L level derived from the
`applications. J.A. 3645; J.A. 4512.
`Amgen disputes the probative value of the batch rec-
`ords, arguing that Apotex failed to provide batch records
`for the other 89 times it has run the process. But it was
`not Apotex’s burden to prove non-infringement. Glaxo,
`110 F.3d at 1567. It was Amgen’s burden to prove that
`Apotex’s processes would infringe the ’138 patent. Amgen
`presents us with no challenge to a restriction on discovery
`or an exclusion of evidence. In these circumstances, we
`see no basis in the mere existence of other records for
`disturbing the district court’s finding that Amgen failed to
`provide adequate evidence to prove infringement.
`
`Ex. 2065-014
`
`

`

`AMGEN INC. v. APOTEX INC.
`
`15
`
`III
`For the foregoing reasons, we affirm the judgment of
`the district court.
`
`AFFIRMED
`
`Ex. 2065-015
`
`