WNV NS2B-NS3pro

Liquid. In 10 mM Tris-HCl buffer, 0.005% BRIJ^® 35 Detergent, pH 8.0. AVOID FREEZE/THAW CYCLES. 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. Specific activity: ≥1 µmol/min/mg protein. Protease 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. Purity: ≥95% by SDS-PAGE. Contaminants: DNase, RNase, and protease activity: none detected.

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