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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.
$89.00
Z02799-100

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Product Introduction
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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Applications
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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Background
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.


Citations
Shantel Rios; Bibek Bhattachan; Christoph Wirblich; Anisha Chandwani; Kruthi Vavilikolanu; Jacob F. Myers; Chrysoula Kitsou; Utpal Pal; Matthias J. Schnell, et al. Rabies virus-vectored Lyme disease vaccine provides long-term protection against tick-transmitted Borrelia burgdorferi. npj Vaccines. (2025-10)
Shantel Rios; Bibek Bhattachan; Christoph Wirblich; Anisha Chandwani; Kruthi Vavilikolanu; Jacob F. Myers; Chrysoula Kitsou; Utpal Pal; Matthias J. Schnell, et al. Rabies virus-vectored Lyme disease vaccine provides long-term protection against tick-transmitted Borrelia burgdorferi. npj Vaccines. (2025-10)
Shantel Rios; Bibek Bhattachan; Christoph Wirblich; Anisha Chandwani; Kruthi Vavilikolanu; Jacob F. Myers; Chrysoula Kitsou; Utpal Pal; Matthias J. Schnell, et al. Rabies virus-vectored Lyme disease vaccine provides long-term protection against tick-transmitted Borrelia burgdorferi. npj Vaccines. (2025-10)
Shantel Rios; Bibek Bhattachan; Christoph Wirblich; Anisha Chandwani; Kruthi Vavilikolanu; Jacob F. Myers; Chrysoula Kitsou; Utpal Pal; Matthias J. Schnell, et al. Rabies virus-vectored Lyme disease vaccine provides long-term protection against tick-transmitted Borrelia burgdorferi. npj Vaccines. (2025-10)
Shantel Rios, et al. The Development of a Rabies Virus-Vectored Vaccine against , Targeting BBI39. Vaccines (Basel). (2024-01)
Mitchell A Ellison, et al. Spt6 directly interacts with Cdc73 and is required for Paf1 complex occupancy at active genes in Saccharomyces cerevisiae. Nucleic Acids Res. (2023-06)
Asrafun Nahar, et al. Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones. Cell Reports. (2022-06)
Fatma Betul Ertem, et al. Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography. STAR Protoc. (2022-01)
Fatma Betul Ertem, et al. Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography. STAR Protoc. (2022-01)
English JG, et al. VEGAS as a Platform for Facile Directed Evolution in Mammalian Cells. Cell. (2019-07)
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