Escherichia Coli.
Sterile filtered colorless solution.
Greater than 97% as determined by SDS-PAGE.
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 210 amino acids and having a molecular mass of 22kDa. The Welqut Protease is fused to a 6 amino acid His tag at C-terminus and is purified by proprietary chromatographic techniques.
WELQut Protease, a recombinant serine protease derived from Staphylococcus aureus, exhibits exceptional specificity. This protease precisely targets and cleaves recombinant proteins containing a specific recognition sequence: Trp, Glu, Leu, Gln, followed by any amino acid (X). Notably, WELQut Protease cleaves externally to the recognition sequence, leaving no extraneous amino acids attached to the target protein. Its versatility is evident in its tolerance to a wide temperature range (4-30°C) and pH range (6.5-9.0), eliminating the need for specific buffers.
Welqut Protease Recombinant is a single-chain polypeptide, devoid of any glycosylation. It comprises 210 amino acids, culminating in a molecular weight of 22kDa. A 6-amino acid His tag is fused to the C-terminus of the protease to facilitate purification, which is achieved through proprietary chromatographic techniques.
The product is a sterile, colorless solution that has been filtered for sterility.
The formulation of Welqut Protease consists of 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4 (pH 7.3), 140 mM NaCl, and 2.7 mM KCl.
For optimal storage, keep the product at 4°C if the entire vial will be used within 2-4 weeks. For extended storage, freezing at -20°C is recommended. To further enhance long-term stability, the addition of a carrier protein such as 0.1% HSA or BSA is advised. Repeated freeze-thaw cycles should be avoided.
SDS-PAGE analysis confirms that the purity of the protease is greater than 97%.
One unit of enzyme activity is defined as the amount required to cleave at least 99% of 100 micrograms of a control protein within 16 hours at 20°C. Enzyme activity is measured in a 100-microliter reaction volume containing 100 mM Tris-HCl (pH 8.0).
Escherichia Coli.