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444148 West Nile Virus NS3 Protease, Recombinant, E. coli

444148
  
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      Übersicht

      Replacement Information
      Description
      Overview

      This product has been discontinued.





      Recombinant, human West Nile virus NS3 proteinase expressed in E. coli as a fusion protein with the cofactor, NS2B, and a C-terminal His•Tag® sequence. Amino acids 1476-1687 of the West Nile polyprotein precursor is fused to amino acids 1393-1440 of NS2B via a 9-amino acid linker (GGGGSGGGG). The C-terminal lysine (Lys48) is mutated to alanine to inactivate autolytic cleavage in and improve stability. It is believed that West Nile Virus protease is an important target for the development of therapeutics that prevent viral replication.
      Catalogue Number444148
      Brand Family Calbiochem®
      SynonymsWNV NS2B-NS3pro
      References
      ReferencesErbel, P., et al. 2006. Nat. Struct. Mol. Biol. 13, 372.
      Seidah, N. G. 2006. Biochem. J. 393, e1;
      Shiryaev, S. A., et al. 2006. Biochem. J. 393, 503.
      Chappell, K.J., et al. 2005 J. Biol. Chem. 280, 2896.
      Nall, T. A., et al. 2004. J. Biol. Chem. 279, 48535.
      Leung, D., et al. 2001. J. Biol. Chem. 276, 45762.
      Product Information
      Unit of DefinitionProtease activity is measured by its ability to cleave a fluorescence peptide substrate pyroglutamic acid-Arg-Thr-Lys-Arg-7-amino-4-methylcoumarin per min per mg protein at 30°C.
      FormLiquid
      FormulationIn 10 mM Tris-HCl buffer, 0.005% BRIJ® 35 Detergent, pH 8.0.
      Applications
      Biological Information
      Purity≥95% by SDS-PAGE
      Specific Activity≥1 µmol/min/mg protein
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      ContaminantsDNase, RNase, and protease activity: none detected
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Bestellnummer GTIN
      444148 0

      Documentation

      West Nile Virus NS3 Protease, Recombinant, E. coli Analysenzertifikate

      TitelChargennummer
      444148

      Literatur

      Übersicht
      Erbel, P., et al. 2006. Nat. Struct. Mol. Biol. 13, 372.
      Seidah, N. G. 2006. Biochem. J. 393, e1;
      Shiryaev, S. A., et al. 2006. Biochem. J. 393, 503.
      Chappell, K.J., et al. 2005 J. Biol. Chem. 280, 2896.
      Nall, T. A., et al. 2004. J. Biol. Chem. 279, 48535.
      Leung, D., et al. 2001. J. Biol. Chem. 276, 45762.
      Datenblatt

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision06-August-2008 RFH
      SynonymsWNV NS2B-NS3pro
      DescriptionRecombinant, human West Nile virus NS3 proteinase expressed in E. coli as a fusion protein with the cofactor, NS2B, and a C-terminal His•Tag® sequence. Amino acids 1476-1687 of the West Nile polyprotein precursor is fused to amino acids 1393-1440 of NS2B via a 9-amino acid linker (GGGGSGGGG). The C-terminal lysine (Lys48) is mutated to alanine to inactivate autolytic cleavage in and improve stability. It is believed that West Nile Virus protease is an important target for the development of therapeutics that prevent viral replication.
      FormLiquid
      FormulationIn 10 mM Tris-HCl buffer, 0.005% BRIJ® 35 Detergent, pH 8.0.
      Concentration Label Please refer to vial label for lot-specific concentration
      Purity≥95% by SDS-PAGE
      ContaminantsDNase, RNase, and protease activity: none detected
      Specific activity≥1 µmol/min/mg protein
      Unit definitionProtease activity is measured by its ability to cleave a fluorescence peptide substrate pyroglutamic acid-Arg-Thr-Lys-Arg-7-amino-4-methylcoumarin per min per mg protein at 30°C.
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesErbel, P., et al. 2006. Nat. Struct. Mol. Biol. 13, 372.
      Seidah, N. G. 2006. Biochem. J. 393, e1;
      Shiryaev, S. A., et al. 2006. Biochem. J. 393, 503.
      Chappell, K.J., et al. 2005 J. Biol. Chem. 280, 2896.
      Nall, T. A., et al. 2004. J. Biol. Chem. 279, 48535.
      Leung, D., et al. 2001. J. Biol. Chem. 276, 45762.