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HRV 3C Protease, 3C, HRV-3C
HRV-3C Protease Cleavage Enzyme, GST Tag, His Tag is a recombinant form of human rhinovirus (HRV) type 14 3C protease with GST Tag & His Tag produced in Escherichia coli cells at ACRObiosystems. The SDS-PAGE purity of the protein is greater than 90%.
The high specificity of HRV-3C Protease Cleavage Enzyme, GST Tag makes it an ideal tool for cleaving fusion proteins at definite cleavage sites. The fusion protein can be purified and cleaved by HRV-3C Protease Cleavage Enzyme, GST Tag, His Tag to obtain the target protein.
>1 Units/µg. One unit will cleave >95% of 100 µg control fusion protein in 50 mM Tris-HCl, 150 mM NaCl, pH 7.5 at 4°C for 16 h.
The enzyme recognizes the cleavage site: Leu-Glu-Val-Leu-Phe-Gln-↓-Gly-Pro.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, 1 mM EDTA, 0.05% Tween20. Contact us for customized product format or formulation.
See Certificate of Analysis for details of reconstitution instruction and specific concentration.
500 mM Tris-HCl, pH7.0, 1.5 M NaCl, 10 mM EDTA, 10 mM dithiothreitol. Chill to 5°C prior to use.
Store at -20°C after reconstituted. Avoid repeated freeze-thaw cycles.
Protease Recombinant is fusion protein of GST and human rhinovirus (HRV) type 14 3C protease.Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as It has been demonstrated that the enzyme exhibits highest activity around neutral pH at temperature ranging from 22 to 37°C, even retaining robust activity at 4°C. Thus, cleavage can be performed at low temperature to enhance the stability of the target protein. The catalytic activity is insensitive to organic solvents (up to 10%); however, it can be strongly stimulated by high concentration of anions such as sulfate.