Millipore Sigma Vibrant Logo
Attention: We have moved. Merck Millipore products are no longer available for purchase on MerckMillipore.com.Learn More

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

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: WNV NS2B-NS3pro

444148
  
Purchase on Sigma-Aldrich

Přehled

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
Katalogové číslo GTIN
444148 0

Documentation

West Nile Virus NS3 Protease, Recombinant, E. coli Certificates of Analysis

TitleLot Number
444148

References

Přehled odkazů
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.
Data Sheet

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.