Description
Quantity: 500 units
Unit Size: Each
Thermo Scientific WELQut Protease is highly specific, recombinant serine protease of Staphylococcus aureus. It recognizes and precisely cleaves recombinant proteins containing an engineered recognition sequence† W- E- L- Q↓X (Trp, Glu, Leu, Gln, X can be any amino acid). The protease cleaves outside the recognition sequence without leaving additional amino acids bound to the target protein. The WELQut Protease is active in a broad temperature (4 to 30°C) and pH (pH 6.5 to 9.0) range and does not require specific buffers. In addition, this new protease has several procedural advantages - it is ideal for on-column proteolysis reactions and can be easily removed from reaction mixtures using its built-in His-tag. Highlights
• Cleaves outside WELQ recognition sequence, without leaving additional amino acids bound to the target protein
• Highly specific to cognate recognition site, does not generate non-specific product bands, even after long incubation and using excess of protease
• Easy to remove from the reaction mixture using built-in His-tag
• Ideal for on-column proteolysis reactions Applications
• Removal of N-terminal fusion tags from recombinant protein preparations. Footnote † This cleavage sequence is present in expression vector pLATE52 included into the Thermo Scientific aLICator LIC Cloning and Expression Kit 4 (N-terminal His-tag/WELQut) (#K1281) available from Thermo Scientific.Definition of Activity Unit: Each unit is defined as the amount of enzyme required to cleave ≥ 99% of 100 μg of a control protein in 16 h at 20°C.
• Enzyme activity is assayed in 100 μL 100 mM Tris-HCl (pH 8.0)
• Hazardous: No
• Molecular Weight: 22 kDa monomer
• Source:Bacillus subtiliscells with a cloned gene of SplB protease from Staphylococcus aureus
• Storage Buffer: Enzyme is supplied in 10 mM Na_2HPO_4; 1.8 mM KH_2PO_4, pH 7.3; 140 mM NaCl; 2.7 mM KCl, 50% glycerol
• Storage Condition:-20°C
• -20°C
