PreScission Protease (PSP)
PreScission Protease (PSP) is a recombinant fusion enzyme consisting of human rhinovirus type 14 (HRV14) 3C protease fused to glutathione S-transferase (GST), expressed using an E. coli expression system. This enzyme selectively recognizes an octapeptide sequence (Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro) and catalyzes peptide bond cleavage specifically between the glutamine (Gln) and glycine (Gly) residues. Reaction conditions involve incubation at 4°C in buffer systems optimized for protease activity. PreScission Protease (PSP) is a valuable tool in the field of protein purification, used to cleave recombinant proteins expressed as fusion proteins with this sequence between the vector domain and the target protein.
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Components |
K1101-100U |
K1101-200U |
K1101-500U |
Storage |
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PreScission Protease |
100 U |
200 U |
500 U |
-80°C |
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10X Cleavage Buffer |
1 mL |
2 x 1 mL |
3 x 1 mL |
-80°C |
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Shipping: dry ice Shelf life: 2 years |
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Note: It is recommended to aliquot upon first use to avoid repeated freeze-thaw cycles: store aliquots at -20°C for a validity period of 6 months.
Sterile colorless liquid
Used at low temperatures (4°C)
Specifically recognize the short peptide Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro at low temperature (4°C) and digest between gln and gly amino acid residues
