WELQut Protease is a highly specific serine protease cleaving outside the WELQX recognition motif to remove N-terminal protein fusion tags.
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.
- 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
- Removal of N-terminal fusion tags from recombinant protein preparations.
† 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)
|Molecular Weight||22 kDa monomer|
|Source||Bacillus subtilis cells with a cloned gene of SplB protease from Staphylococcus aureus|
|Storage Buffer||Enzyme is supplied in 10 mM Na2HPO4; 1.8 mM KH2PO4, pH 7.3; 140 mM NaCl; 2.7 mM KCl, 50% glycerol|
|Storage Condition||-20 C|
|Storage Condition:||-20 C|
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