PreScission protease is a cysteine protease derived from human rhinovirus – HRV3C Protease. rPP is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. It specifically recognizes the amino acid sequences which include the core site of Leu-Phe-Gln-Gly-Pro and cleaves between the Gln and Gly residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the super structures of the fusion protein. rPP works most effective at 4°C and can digest substrates at room temperature as well.
Source
Escherichia coli.
Molecular Weight
PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of sequences which include the core amino acid sequence Leu-Phe-Gln/Gly-Pro cleaving between the Gln and Gly residues. 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 well.
Biological Activity
Appearance
Sterile colorless liquid.
Formulation
50 mM Tris-HCl, pH 7.0 (at 25°C), 150 mM NaCl, 1 mM EDTA, 1 mM dithiothreitol. Chill to 5 °C prior to use.
Endotoxin
Reconstitution
Stability and Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.- 3 months, -20 to -70 °C under sterile conditions after opening.
References
1. Werner G, Rosenwirth B, Bauer E, et al. 1986. J Virol, 57: 1084-93.2. Libby RT, Cosman D, Cooney MK, et al. 1988. Biochemistry, 27: 6262-8.3. Aschauer B, Werner G, McCray J, et al. 1991. Virology, 184: 587-94.4. Leong LE, Walker PA, Porter AG. 1993. J Biol Chem, 268: 25735-9.