HRV-3C Protease,3C Protease
HRV-3C Protease Cleavage Enzyme, GST Tag is a recombinant form of human rhinovirus (HRV) type 14 3C protease produced in Escherichia coli cells at ACRObiosystems.
Predicted N-terminus: Met
Request for sequence
This protein carries a GST tag at the N-terminus
The protein has a calculated MW of 46.0 kDa. The protein migrates as 44-46 kDa under reducing (R) condition (SDS-PAGE).
The enzyme recognizes the cleavage site: Leu-Glu-Val-Leu-Phe-Gln-↓-Gly-Pro.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris,150 mM NaCl,1 mM EDTA,0.05% Tween20,1 mM DTT,PH8.0.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
HRV-3C Protease Cleavage Enzyme, GST Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
>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℃ for 16 h (QC tested).
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℃, even retaining robust activity at 4℃. 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.