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Your Position: Home > Protein > 3C (HRV) > 3CC-N3133

HRV-3C Protease Cleavage Enzyme Protein, GST Tag (active enzyme)

  • Synonym
    HRV-3C Protease,3C Protease
  • Source
    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
  • Molecular Characterization

    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).

  • Application
    The enzyme recognizes the cleavage site: Leu-Glu-Val-Leu-Phe-Gln-↓-Gly-Pro.
  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    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.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    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:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
3C (HRV) SDS-PAGE

HRV-3C Protease Cleavage Enzyme, GST Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

Bioactivity

>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).

  • Background
    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.
  • Clinical and Translational Updates
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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