Welqut Protease
Escherichia Coli.
Greater than 97.0% as determined by SDS-PAGE.
Description
Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 22kDa. The Welqut Protease is purified by proprietary chromatographic techniques.
Product Specs
The WELQut Protease, derived from Staphylococcus aureus, is a highly specific recombinant serine protease. It demonstrates exceptional precision in identifying and cleaving recombinant proteins possessing a specific recognition sequence: Trp, Glu, Leu, Gln, followed by any amino acid (X). Notably, the cleavage occurs externally to this recognition sequence, ensuring no extra amino acids remain attached to the target protein. This protease exhibits remarkable versatility, functioning effectively across a temperature range of 4-30°C and a pH range of 6.5-9.0, without the need for specific buffers.
The recombinant Welqut Protease is a single, non-glycosylated polypeptide chain with a molecular weight of 22kDa, composed of 204 amino acids. Its purification is achieved through proprietary chromatographic techniques.
The formulation of Welqut Protease consists of 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4, with a pH of 7.3, 140 mM NaCl, and 2.7 mM KCl.
SDS-PAGE analysis indicates a purity exceeding 97.0%.
One unit of enzyme activity is defined as the amount required to cleave 99% or more of 100 micrograms of a control protein within 16 hours at a temperature of 20°C. The enzyme activity assay is conducted in a volume of 100 microliters of 100 mM Tris-HCl buffer at pH 8.0.
Escherichia Coli.
Product Science Overview
The protease recognizes an engineered recognition sequence, W-E-L-Q↓X, where X can be any amino acid . This sequence is typically added to recombinant proteins to allow for precise cleavage. The enzyme cleaves outside the recognition sequence without leaving additional amino acids bound to the target protein, ensuring that the integrity of the target protein is maintained .
Welqut Protease is active over a broad temperature range (4°C to 30°C) and pH range (6.5 to 9.0), making it versatile for various experimental conditions . It does not require specific buffers, which simplifies its use in different applications . The enzyme is stable when stored at 4°C for short-term use and at -20°C for long-term storage, with the addition of a carrier protein recommended to enhance stability .
Welqut Protease is primarily used for the removal of N-terminal fusion tags from recombinant protein preparations . Its high specificity and ability to cleave without leaving additional residues make it ideal for on-column proteolysis reactions . The built-in His-tag allows for easy removal of the protease from reaction mixtures, further enhancing its utility in protein purification processes .
- High Specificity: The enzyme is highly specific to its recognition sequence and does not generate non-specific product bands, even after prolonged incubation or when used in excess .
- Ease of Use: The protease can be easily removed from reaction mixtures using its built-in His-tag, simplifying downstream processing .
- Versatility: Active across a wide range of temperatures and pH levels, Welqut Protease does not require specific buffers, making it adaptable to various experimental conditions .
