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PreScission Protease

PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro (LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro 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.
¥800
Z02799-100

Source E. coli
Biological Activity 1.4U/μl. One unit is defined as the amount of enzyme needed to cleave 100 μg of fusion protein in 16 hours to 90% completion at 5°C in a buffer containing 50 mM Tris-HCl, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT.
Cleavage Buffer 50mM Tris-HCl, pH7.0 (at 25°C), 150 mM NaCl, 1 mM EDTA, 1 mM dithiothreitol. Chill to 5°C prior to use.
Physical Appearance Sterile colorless liquid.
Storage & Stability Upon receiving, this product remains stable for 6 months at -20℃ or below. Avoid repeated freeze-thaw cycles.
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During cleavage reactions, it is recommended that samples be removed at various time points and analyzed by SDS-PAGE to estimate the yield, purity, and extent of digestion. The amount of PreScission Protease, temperature and length of incubation required for complete digestion of a given GST fusion partner may vary depending on the fusion partner. Optimal conditions for each fusion should be determined in pilot experiments. Digestion may be improved by adding TritonTM X-100, TweenTM 20, NonidetTM, or NP40 to a concentration of 0.01%. Concentrations of these detergents up to 1% do not inhibit PreScission Protease.
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PreScission Protease

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PreScission Protease

Lane 1: 2 μg of PreScission Protease, non-reducing (NR)
Lane 2: 2 μg of PreScission Protease, reducing (R)
≥ 90% as analyzed by SDS-PAGE »

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Synonyms PreScission Protease(PSP)
Target Background PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro (LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro 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.
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For laboratory research use only. Direct human use, including taking orally and injection and clinical use are forbidden.