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69671 Thrombin, Restriction Grade

69671
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      Plastic ampoule 50 u
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      Description
      OverviewRestriction Grade Thrombin is a highly purified preparation qualified to specifically cleave target proteins produced with appropriate vectors. This preparation is functionally tested for activity with fusion proteins and is free of detectable contaminating proteases. Prepared from human plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. Thrombin is supplied as a solution in 50% glycerol and includes 10X Thrombin Cleavage Buffer and a Cleavage Control Protein.
      Catalogue Number69671
      Brand Family Novagen®
      References
      Product Information
      CAS number9002-04-4
      Unit of DefinitionOne unit is defined as the amount of enzyme needed to cleave 1 mg of fusion protein in 16 hours at 20°C in a 200 µl reaction containing 20 mM Tris-HCl pH 8.4, 150 mM NaCl, 2.5 mM CaCl₂, 50 µg fusion protein.
      Components
      Quality LevelMQ400
      Applications
      Biological Information
      SourcePrepared from human plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      RTECSXO8950000
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Shipped with Blue Ice or with Dry Ice
      Toxicity Multiple Toxicity Values, refer to MSDS
      Storage -20°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Thrombin, Restriction Grade Certificates of Analysis

      TitleLot Number
      69671

      Brochure

      Title
      Bulk packaging
      Protein Purification and Detection Tools

      Citations

      Title
    • Damien Bessière, et al. (2008) Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways. Journal of Biological Chemistry 283, 4352-4363.
    • Amanda J. Davis, et al. (2007) Arabidopsis phosphatidylinositol phosphate kinase 1 binds F-actin and recruits phosphatidylinositol 4-kinase beta1 to the actin cytoskeleton. Journal of Biological Chemistry 282, 14121-14131.
    • Hua A. J. Lu, et al. (2007) Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking. Journal of Biological Chemistry 282, 28721-28732.
    • Hideaki Unno, et al. (2007) Structural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysis. Journal of Biological Chemistry 282, 15812-15822.
    • Fanny Boissier, et al. (2006) Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis. Journal of Biological Chemistry 281, 4434-4445.
    • Alyssa Carré-Mlouka, et al. (2006) A new rubisco-like protein coexists with a photosynthetic rubisco in the planktonic cyanobacteria Microcystis. Journal of Biological Chemistry 281, 24462-24471.
    • Hong Ye, et al. (2006) CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation. Journal of Biological Chemistry 281, 8958-8969.
    • Agnes E. Hamburger, et al. (2005) Steric accessibility of the HIV-1 gp41 N-trimer region. Journal of Biological Chemistry 280, 12567-12572.
    • Kenneth L. Madsen, et al. (2005) Molecular determinants for the complex binding specificity of the PDZ domain in PICK 1. Journal of Biological Chemistry 280, 20539-20548.
    • Frederic H. Vaillancourt, Jun Yin and Christopher T. Walsh. (2005) SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase. Proceedings of the National Academy of Sciences (USA) 102, 10111-10116.
    • Yasuo Yamakoshi, et al. (2005) Porcine dentin sialoprotein is a proteoglycan with glycosaminoglycan chains containing chondroitin 6-sulfate. Journal of Biological Chemistry 280, 1552-1560.
    • Yang Chao and Dax Fu. (2004) Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. Journal of Biological Chemistry 279, 17173-17180.
    • Jeffrey M. Vargason, et al. (2004) Size selective recognition of siRNA by an RNA silencing suppressor. Cell 115, 799-811.
    • Marilyn H. Perrin, et al. (2003) A soluble form of the first extracellular domain of mouse type 2 corticotropin-releasing factor receptor reveals differential ligand specificity. Journal of Biological Chemistry 278, 15595-15600.
    • Songmin Cai and John H. Exton. (2001) Determination of interaction sites of phospholipase D1 for RhoA. Biochemical Journal 355, 779-785.
    • U. Vinkemeir, et al. (1998) Structure of the amino-terminal protein interaction domain of STST-4. Science 279, 1048-1052.
    • Alexy Bochkarev, et al. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. 385, 176-181.
    • Susan V. Pena, et al. (1997) Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins. Journal of Immunology 2680-2688.
    • John A. Lupisella, et al. (1995) The ligand binding domain of the human retinoic acid receptor Is predominantly α-helical with a trp residue in the ligand binding site. Journal of Biological Chemistry 270, 24884-24890.
    • Harikrishna Nakshatri, Poornima Nakshatri and R. Alexander Currie. (1995) Interaction of Oct-1 with TFIIB. Journal of Biological Chemistry 270, 19613-19623.
    • Kelvin Nurse, et al. (1995) Purification, cloning, and properties of the tRNA ψ55 synthase from Escherichia coli. RNA 1,.
    • User Protocols

      Title
      TB188 Thrombin Kits

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      Categories

      Life Science Research > Protein Sample Preparation > Protein Purification > Kits & Enzymes for Fusion Tags
      Life Science Research > Proteins and Enzymes > Other Enzymes