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2059 Exhibit: EX2059

Document IPR2018-00162, No. 2059-71 Exhibit - EX2059 (P.T.A.B. Feb. 20, 2018)
Tubulin Microtubules and TaxoidsPurified calf brain tubulin and chemicals were as described 27 For glycerol induced assembly tubu lin was directly equilibrated in 10 mm phosphate 1 mm EDTA 01 mm GTP 34 m glycerol pH 67 buffer All tubulin samples were clarified by at 50000 rpm 4 °C for 10 min using TL1002 or TL1004 centrifugation rotors in a Beckman Optima TLX centrifuge After centrifugation 6 mm MgC12 and up to 1 mm GTP were added to the solution final pH 65 GAB Microtubules were assembled by raising the temperature to of the assembled mi 37 °C for 30 min The length and morphology crotubules were checked by negative stain electron microscopy as described 27 Axonemes from sea urchin Strongylocentrotus purpuratus sperm tail were kindly provided by Dr Philippe Huitorel Universite Pierre et France and diluted a minimum of Marie Curie VillefranchesurMer 100 times in the experimental buffer Docetaxel was kindly provided by RhonePoulenc Rorer Antony France Flutax1 was synthesized as described 35 Their concentra 10 24 Flutax2 was syn tions were measured spectrophotometrically thesized by the reaction of 70alanyl Taxol with Oregon Green 488 carboxylic acid succinimidyl ester 5 isomer Molecular Probes refer ence no 06147 following the described procedures 35 and purified by preparative TLC on silica gel with chloroformmethanolacetic acid 41015 vvv as eluent mass spectrum and NMR data were in ac cordance with its structure 58 Flutax2 purity high performance Ref 24 was 94 Flutax2 induced the assem liquid chromatography bly of GDPtubulin similarly to Flutax1 24 except for the critical tubulin concentration which was coincident with Taxol Flutax2 con centrations were measured in 05 SDS 50 mm sodium phosphate M cm at 496 nm buffer pH 70 employing an extinction coefficient2 of 49100 1100 to stabilize mi Preparation of Cross linked MicrotubulesIn order crotubules against disassembly by dilution and low temperatures 50 tm tubulin in GAB was assembled at 37 °C for 30 min and then 20 mm glutaraldehyde EMscope microscopy grade was added to the solution which was incubated at 37 °C for 10 min more The remains of the cross linking agent were quenched by adding 60 mm NaB114 Fluka on these conditions 90 of ice and the mixture degassed Under the tubulin was found to be incorporated into the microtubules The mor by electron mi phology of the cross linked microtubules was checked croscopy and found to be normal They were found to be stable against dilution and low temperatures The taxoid binding was found to be unaffected by the treatment as judged by the stoichiometry and the kinetics of the binding reaction which were not altered The number of active sites was found to decay at a relatively slow rate5 decay in 24 h at 4 °C to MicrotubulesThe Binding of Fluorescent Taxoids binding of Flutax1 and Flutax2 to the microtubules was measured using a cen trifugation assay Samples of cross linked microtubules were incubated The sam for 1 h at different temperatures and taxoid concentrations ples were then centrifuged for 20 min at 50000 rpm in a TL100 rotor employing a Beckman Optima TLX ultracentrifuge The supernatants were taken and the pellets were resuspended in a 10 mm phosphate 2 J A Evangelio and J M Andreu unpublished observations Fast Kinetics of Taxoid Binding to Microtubules buffer pH 70 containing 1 SDS The pellets and supernatants were Downloaded from httpwwwjbcorg by guest on May 2017 diluted 15 in the same buffer and their fluorescence was measured employing a Shinnadzu RF540 excitation wave spectrofluorometer 522 nm 5nm excitation length 492 nm emission wavelength and of ligand in the samples was calcu emission slits The concentration lated using Flutax1 and Flutax2 spectrophotometric concentration standards The percentage of inactive ligand in the stock solutions was obtained two different concentrations by measuring the titration curves at of sites 1 and 01 pm The binding constant has to be the same at both concentrations of sites and can be calculated from the apparent binding constant by discounting the percentage of the inactive ligand from the total free ligand The value fitting both curves with the same binding constant and the minimal error was calculated using a program based on the Marquardt algorithm 36 The percentages found at each exper and the effective binding con temperature were averaged imental stants were calculated using the averaged values The binding of Flutax1 and Flutax2 can also be monitored by the in ligand anisotropy The anisotropy change of the fluorescence of Flutax1 and Flutax2 bound and free were measured in a SLM8000D fluorometer using an excitation wavelength of 470 nm and an emission wavelength of 560 nm with 2nm excitation and emission slits The binding of Flutax1 and Flutax2 to the microtubules was measured using a ligand anisotropy assay Samples of taxoids were incubated for and concentrations 15 min at different of cross linked temperatures the samples were measured in a Po microtubules The anisotropy of lastarGalaxy BMG Labtechnologies plate reader using the 485P excitation filter and the 520P emission filter Since with this method the binding constants are determined of using the free concentration sites total measured binding sites minus bound ligand measured they are not influenced by the percentage of inactive ligand Kinetics of Binding and Dissociation of Fluorescent Taxoids to Mi crotubulesThe kinetics of Flutax1 and Flutax2 binding to and dis sociation from microtubules were measured by following the change of the fluorescence of the probe employing a High Tech Sci intensity of entific SS 51 stopped flow device equipped with a fluorescence detec of 492 nm 2nm slit tion system A wavelength in the excitation pathway and a filter with a cutoff of 530 nm in the emission pathway were used The dead time of the instrument was determined using the of Nbromosuccinimide with Nacetyltryptophanamide 37 reaction and was found to be 2 ms With these conditions both Flutax1 and Flutax2 are photostable within the time of the measurement The kinetics of the binding of Flutax1 and Flutax2 to microtubules were also measured by the change in the fluorescence anisotropy of the probe in a Spex spectrofluorometer Fluorolog 1691 excitation wave length 492 nm emission wavelength 570 nm 16nm slits a cutoff filter of 550 nm was employed in the emission pathway to eliminate any contribution due to scattered light The device was equipped with a of Biomo stopped flow module designed and built at the Laboratory these lecular Dynamics K U Leuven Flutax2 is photostable under photoquenching 1 of conditions while Flutax1 shows appreciable the total intensity per second during the measurement The dead time of the instrument was measured as described above and was found to be 10 ms A minimum of 8 curves were averaged for each measurement The slower dissociation of Flutax1 and Flutax2 from microtubules was measured by the decrease in fluorescence anisotropy in the SLM8000D fluorometer equipped with a home built mixing device consisting of two 1 ml syringes fixed to a thermostated aluminum block in such a way to a threeway Hamil that they moved simultaneously and connected ton valve which acted as a mixing chamber The output of the valve was to the cuvette The dead time of the complete system was connected 2 s comparable with the 1s time constant employed in the fluorometer curves was done using a nonlinear least The fitting of squares fitting program based on the Marquardt algorithm 36 when pseudo first order conditions were used otherwise the FITSIM pack age 38 was employed Xray Scattering SolutionsMeasurements were by Microtubule made at station 21 of the Daresbury Laboratory Synchrotron Radiation and and processing Source Instruments employed data acquisition the microtubule xray scattering were as described interpretation of previously 23 about the kinetic
Anisotropy of the fluorescence emission of the fluorescent 1 iim in GAB at 37 °C A = 470 nm = 560 nm Bound a Ligand Free Displaced taxoids Flutaxl Flutax2 assembled from 20 pm pure tubulin in GAB a Bound to microtubules or displaced by the addition of 50 pm docetaxel Downloaded from httpwwwjbcorg by guest on May 2017 Log Flutax Log Sites FIG 2 A solid line and circles titration curve of 1 jM taxoid sites in stabilized microtubules with Flutax1 at 27 °C measured by centrifu gation data are corrected for the percentage of inactive ligand Dashed line and open circles uncorrected data and fit A small part of the ligand remained in the supernatant in use was found to be inactive since it at very high concentrations of microtubules disturbing the measurement of the free ligand concentration and artifactually decreasing the appar ent binding constant measured This effect was corrected as described under Experimental Procedures This percentage was found to be 4 1 in the case of Flutax1 and 6 1 in the case of Flutax2 Solid squares and dotted line titration curve of 25 nm Flutax1 with taxoid sites in stabilized microtubules measured by anisotropy B solid line jM taxoid sites in stabilized microtu and circles titration curve of 1 bules with Flutax2 at 27 °C corrected for the percentage of inactive ligand Dashed line and open circles uncorrected data Solid squares and dotted line titration curve of 25 nm Flutax2 with stabilized micro tubules measured by anisotropy centrifugation
Flutax1 and Flutax2 to microtubules assembled from pure tubulin in GAB were measured by sedimentation and anisot ropy using diluted cross linked microtubules This was neces sary since in preliminary experiments using nonstabilized mi crotubules the reaction was essentially displaced toward the bound ligand state due to the high concentration of binding sites The cross linking employed did not affect the binding stoichiometry or the kinetics of binding described below The titration curves corrected for the small percentage of inactive ligand in the experiments in the case of the sedimen tation assays are shown in Fig 2 The stoichiometry was found to be 11 099 ± 007 mol of Flutax2mol of assembled tubu lin and the affinity was high K = 66 ± 10 X 107 NI 1 1 anisotropy for or 60 ± 02 X 107 Flutax1 and lc = 61 ± 17 X 107 NI 1 centrifugation 59 ± 03 X 107 NI 1 anisotropy for Flutax2 at 27 °C The affinity constants determined or at different temperatures are
FIG 10 Models of the Flutax bind ing site A in the microtubule configura tion described by Nogales et al 30 B with the protofilament rotated 30° clock wise as seen from the plus end The mod els were constructed by overimposing us ing the software package SIMLYS 56 the NMRdeter the taxane moiety of mined solution structures of Flutax1 57 with the docetaxel molecule modeled in the 1TUB PDB entry 34 and placing the either in the same resulting structures orientation as in Ref 30 A or rotated 30° B Note that the conformation depicted of the bound Flutax1 is only one of the conformations The solution fluorescein freedom group has a large conformational with three main orientations one of them being not allowed for bound Flutax since it will collide with the protein From the two types of configurations 1 with other the fluorescein in the interprotofilament region and 2 with it pointing to the lu men the first one has been selected since 1 the internalization of the fluorescein group would be kinetically unfavorable and 2 the dianionic form of the chro mophore is stabilized by the positive charge or Arg282 Nevertheless is pos it sible that Flutax binds first in configura tion 1 and that the second step of binding observed entails flipping to conformation bules at 37 °C is 138 X 106 NI 1 s1 thus 21 of the collisions have to be effective The problem of the efficiency of collisions has been addressed for proteinprotein recognition 49 50 A typical factor between frequency of collisions and frequency of binding is about Vi000 and lower for proteinprotein interac tions This value holds on the percentage of the surface area of the proteins that forms the binding interface typically 10 of the exposed area and other factors like electrostatic or hydro phobic interactions The value of 15o can be a possible ratio for an exposed site in the microtubule The interface area of Flutax can be roughly estimated in 25 of its total surface by super imposing the taxane moiety of Flutax with the docetaxel mol ecule bound to tubulin 34 The percentage of interface area of tubulin is also increased with respect to unassembled protein since the exposed area of f3tubulin available for collision with ligand is largely reduced in the microtubules thus increasing the chances of an effective collision In this way mechanism 1 is the easiest possible explanation for the kinetic data This is supported as well by preliminary results which show that the presence of microtubuleassociated proteins which bind to the outer microtubule surface slows down the binding of Taxo14 Mechanisms of type 1 are in con trast with the location of the Taxol site in the high resolution model microtubules 30 which shows the Taxol site clearly facing the lumen thus reducing its accessibility Let us consider the alternative mechanisms of type 4 Taxol may reach the binding site by diffusing though the microtubule wall It can be shown that in order to feed the binding reaction at the observed association rate the effective viscosity of the microtubule wall has to be only 100 times larger than that of water ie approximately the viscosity of glycerol which is highly unreasonable for a protein Therefore holes in the mi crotubule wall would be required Following the high resolution J F Diaz and J M Andreu unpublished observations Abraxis EX2059 Cipla Ltd. v. Abraxis Bioscience, LLC
26276 position 7 this work on the curvature of the microtubule wall A rotated protofilament model Fig 10B has important struc implications for the mainly electrostatic tural interprotofila ment interactions and the interaction with motor proteins The M loop 30 is displaced outwards and makes a closer approach to helix H3 displaced inwards instead of the H1 S2 loop of the In addition the C terminal helices H11 subunit neighboring and H12 are displaced and should engage in modified interac tions with the microtubule binding sites of kinesin motors 51 Experimental distinction between the two types of models Fig 10 A and B with direct low resolution structural methods is difficult However locating the fluorescein moiety of Flutax at the outer microtubule surface would strongly favor the rotated model This problem may be addressed by employing macro molecular antifluorescein fluorescence quenchers antibodies and perturbants of the binding kinetics and Dr AcknowledgmentsWe thank Dr Francisco AmatGuerri Ulises Acuna for continued support with the synthesis of fluorescent taxoids and useful clarifying discussions Dr Pilar Lillo for help with the SLM8000 fluorometer Dr Juan Evangelio for initial the use of help with the fluorescent probes Dr Consuelo Lopez for use of the and Dr Pablo Chacon for stopped flow apparatus Dr Greg Diakun help with small angle xray scattering measurements Dr P Huitorel for the axonemes and Aurelio Hurtado and Lorenzo Alonso CIB Tech for helping with the design and manufacturing of the nical Services manual mixing device Fast Kinetics of Taxoid Binding to Microtubules Kingston D G and Bane S 1996 Biochemistry 35 1417314183 22 Vulevic B and Correia J J 1997 Biophys J 72 13571375 23 Diaz J F Valpuesta J M Chacon P Diakun G and Andreu J M 1998 J Biol Chem 273 3380333810 24 Evangelio J A Abal M Barasoain I Souto A A Lillo M P Acuna A U AmatGuerri F and Andreu J M 1998 Cell Motil Cytoskeleton 39 7390 25 Li Y Edsall R Jr Jagtap P G Kingston D G I and Bane S 2000 Biochemistry 39 616623 26 Andreu J M Bordas J Diaz J F Garcia de Ancos J Gil R Medrano F J Nogales E Pantos E and Towns Andrews E 1992 J Mol Biol 226 169184 27 Andreu J M Diaz J F Gil R de Pereda J M Garcia de Lacoba M Peyrot V Briand C Towns Andrews E and Bordas J 1994 J Biol Chem 269 3178531792 28 Dye R B Fink S P and Williams R C Jr 1993 J Biol Chem 268 68476850 29 Nogales E Wolf S G Khan I A Luduena R F Downing K H 1995 Nature 375 424427 30 Nogales E Whittaker M Milligan R A and Downing K H 1999 Cell 96 7988 31 Rao S Orr G A Chaudhary A G Kingston D G I and Horwitz S B 1995 J Biol Chem 270 2023520238 32 Gonzalez Garay M L Chang L Blade K Menick D R and Cabral F 1999 J Biol Chem 274 2387523882 33 Rao S He L Chakravarty S Ojima I Orr G A and Horwitz S B 1999 J Biol Chem 274 3799037994 34 Nogales E Wolf S G and Downing K 1998 Nature 391 199203 35 Souto A A Acuna A U Andreu J M Barasoain I Abal M and AmatGuerri F 1995 Angew Chem Int Ed Engl 34 27102712 36 Bevington P R 1969 Data Reduction and Error Analysis for the Physical Sciences pp 235240 McGrawHill Book Co New York 37 Peterman B F 1979 Anal Biochem 93 442444 38 Barshop B A Wrenn R F and Frieden C 1983 Anal Biochem 130 134145 39 Scheele R B Bergen L G and Borisy G G 1982 J Mol Biol 154 485500 40 Evans L Mitchinson T and Kirschner M 1985 J Cell Biol 100
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2006 Exhibit: EX2006

Document IPR2018-00152, No. 2006-35 Exhibit - EX2006 (P.T.A.B. Feb. 16, 2018)
Abraxis EX2006 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
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2080 Exhibit: EX2080

Document IPR2018-00152, No. 2080-91 Exhibit - EX2080 (P.T.A.B. Feb. 16, 2018)
In some cases, broader therapeutic windows might be ultimately achieved by refining the paralogue selectivity of the compounds, such that they avoid inhibiting essential cellular functions and target only the members of a protein family that are prominent in tumours.
Activation of apoptosis pathways ABL (Gleevec; Interference with signal Novartis) transduction, response Cathepsin K Inhibition of tumour spread Telomerase Induction of senescence VEGF (Avastin; Interference with blood supply Genentech/Roche) of tumour Antibody-directed cytotoxicity CD20 (Rituxan; Biogen Idec/ Genentech) Microtubules (Taxol) Signalling Invasion/metastasis Immortalization Senescence Host Angiogenesis Tumour-associated membrane proteins Traditional cytotoxics Replication/ cytokinesis Metabolism Neocytotoxics Protein turnover Interference with DNA synthesis, cell division Reduction of essential metabolite Inhibition of acceleration of protein degradation Table 1 | Therapeutic mechanisms of action of anticancer drugs Therapeutic Targeted Mechanism of action target or process of therapeutics modality Transformation Apoptosis Target example (drug)
The anticancer activity of a drug might depend on the dozens of cellular efflux pumps, proliferation rate, checkpoint apparatus, repair processes and apoptotic machinery, to mention only a few possibili- ties.
Although a substantial fraction of this acquired resistance can be reversed by drugs such as the second-generation BCR– ABL inhibitor dasatinib (Sprycel; Bristol- Myers Squibb), which has broader activity against clones of BCR–ABL mutants that are insensitive to imatinib, remissions are transitory31.
Litz, J., Sakuntala Warshamana-Greene, G., Sulanke, G., Lipson, K. E. & Krystal, G. W. The multi-targeted kinase inhibitor SU5416 inhibits small cell lung cancer growth and angiogenesis, in part by blocking Kit- mediated VEGF expression.
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2016 Exhibit: EX2016

Document IPR2018-00152, No. 2016-45 Exhibit - EX2016 (P.T.A.B. Feb. 16, 2018)
Abraxis EX2016 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2016 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2016 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2016 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2016 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
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2091 Exhibit: EX2091

Document IPR2018-00152, No. 2091-102 Exhibit - EX2091 (P.T.A.B. Feb. 16, 2018)
Safety and Efficacy of nab-Paclitaxel in the Treatment of Patients with Breast Cancer Prakash vishnu and vivek Roy Division of Hematology Oncology, Mayo Clinic, Jacksonville, FL, USA.
The nano-particle protein platform utilizes the natural properties of albumin to increase drug delivery to the tumor and eliminates the need for solvents.
This stability causes inhibition of the normal dynamic reorganization of the microtubules which is necessary for important interphase and mitotic functions in the cells Dosing and administration 260 mg/m2 intravenous infusion over 30 minutes once every 3 weeks Pharmacokinetics Distribution: extensive extra-vascular distribution and/or tissue binding; does not penetrate blood brain barrier Protein binding: 89% to 98% Metabolism: Hepatic; P450 (CYP2C8 and CYP3A4) excretion: Fecal (20%); renal (4%) elimination half life: 27 hours Side effects Common: Cardiovascular: abnormal eKG (60%), edema (10%) Dermatologic: alopecia (90%) Gastrointestinal: diarrhea (27%), nausea (30%), vomiting (18%) Hematologic: Anemia (33%), Neutropenia, (any grade, 80%) Hepatic: raised transaminases (39%), raised alkaline phosphatase (36%) Neurologic: asthenia/myalgia/fatigue (47%), sensory neuropathy (any grade, 71%) Ophthalmic: visual disturbance (13%) Renal: raised serum creatinine (11%) Respiratory: dyspnea (12%) Serious: Cardiovascular: cardiac arrest, cerebrovascular accident, supraventricular tachycardia, transient ischemic attack (3%) Hematologic: severe anemia (1%), bleeding (2%), febrile neutropenia (2%), neutropenia, grade 4 (9%), severe thrombocytopenia (,1% ) Neurologic: severe sensory neuropathy (10%) Special precaution Paclitaxel has been shown to be clastogenic, teratogenic and fetotoxic and should not be used in pregnancy.
Abbreviations: ORR, overall response rate; TTP, time to progression; OS, overall survival; HR: hazard ratio; NR, not reported; pCR, pathologic complete response; PFS, progression free or ixabepilone Bevacizumab plus paclitaxel, nab-paclitaxel Capecitabine plus nab-paclitaxel metastatic Locally recurrent, Locally advanced
Publish with Libertas Academica and every scientist working in your field can read your article “I would like to say that this is the most author-friendly editing process I have experienced in over 150 publications.
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2068 Exhibit: EX2068

Document IPR2018-00152, No. 2068-79 Exhibit - EX2068 (P.T.A.B. Feb. 16, 2018)
The most recognized biological effect of paclitaxel formulated with CrEL is an acute hypersensitivity reaction, characterized by dyspnea, flushing, rash, chest pain, tachycardia, hypotension, angioedema, and generalized urticaria.
Positions and Honors Positions and Employment 1985-1986 Research Associate, Pathology Department, Hahnemann Hospital, Philadelphia, PA 1986-1987 Internship (Medical), St. Agnes Hospital, Caton and Wilkens Avenue, Baltimore, MD 1987-1989 Residency (Medical), St. Agnes Hospital, Caton and Wilkens Avenue, Baltimore, MD 1989-1992 Fellowship (Hematology/Oncology), University of Maryland Cancer Center, 22 South Greene Street, Baltimore, MD Assistant Instructor, University of Maryland School of Medicine, Department of Medicine, University of Maryland Cancer Center 1990-1992 Recipient of the American Cancer Society Clinical Oncology Fellowship Abraxis EX2001 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Breast Cancer Research and Treatment 111, 355-364. b. Tkaczuk KH, Tait NS Ioffe O, Tan M, Goloubeva OG, Lesko SA, Deamond SF, Zhou D, Lum ZP, Sutula MJ, Van Echo D and Ts’o PO.
We found that GP-88 is a negative prognostic marker in BC patients with hormone sensitive cancer, which may be independent of Her2; additionally, overexpression of GP-88 may render BC tumors resistant to anti Her2 therapy with trastuzumab.
Progranulin (GP88) tumor tissue expression is associated with increased risk of recurrence in breast cancer patients diagnosed with estrogen receptor positive invasive ductal carcinoma.
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2075 Exhibit: EX2075

Document IPR2018-00152, No. 2075-86 Exhibit - EX2075 (P.T.A.B. Feb. 16, 2018)
2/8/2018 Abraxane Prices, Coupons & Patient Assistance Programs - Drugs.com Abraxane Prices, Coupons and Patient Assistance Programs Abraxane (paclitaxel protein-bound) is a member of the mitotic inhibitors drug class and is commonly used for Breast Cancer, Breast Cancer - Metastatic, Non-Small Cell Lung Cancer and others.
Prices are for cash paying customers only and are not valid with insurance plans.
Some offers may be printed right from a website, others require registration, completing a questionnaire, or obtaining a sample from the doctor's office.
2/8/2018 Abraxane Prices, Coupons & Patient Assistance Programs - Drugs.com Patient Assistance Programs for Abraxane Patient assistance programs (PAPs) are usually sponsored by pharmaceutical companies and provide free or discounted medicines to low income or uninsured and under-insured people who meet specific guidelines.
This program provides financial assistance to eligible individuals to cover coinsurance, copayments, healthcare premiums and deductibles for certain treatments.
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2031 Exhibit: EX2031

Document IPR2018-00152, No. 2031-53 Exhibit - EX2031 (P.T.A.B. Feb. 16, 2018)
Abraxis EX2031 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2031 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2031 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2031 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
Abraxis EX2031 Apotex Inc. and Apotex Corp. v. Abraxis Bioscience, LLC
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2067 Exhibit: EX2067

Document IPR2018-00152, No. 2067-78 Exhibit - EX2067 (P.T.A.B. Feb. 16, 2018)

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2043 Exhibit: EX2043

Document IPR2018-00152, No. 2043-64 Exhibit - EX2043 (P.T.A.B. Feb. 16, 2018)

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2081 Exhibit: EX2081

Document IPR2018-00152, No. 2081-92 Exhibit - EX2081 (P.T.A.B. Feb. 16, 2018)

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2008 Exhibit: EX2008

Document IPR2018-00152, No. 2008-37 Exhibit - EX2008 (P.T.A.B. Feb. 16, 2018)

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2013 Exhibit: EX2013

Document IPR2018-00152, No. 2013-42 Exhibit - EX2013 (P.T.A.B. Feb. 16, 2018)

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2061 Exhibit: EX2061

Document IPR2018-00152, No. 2061-76 Exhibit - EX2061 (P.T.A.B. Feb. 16, 2018)

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2076 Exhibit: EX2076

Document IPR2018-00152, No. 2076-87 Exhibit - EX2076 (P.T.A.B. Feb. 16, 2018)

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