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HRV-3C Protease, His Tag

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. 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. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin.Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.
$50.00
Z03092-100

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Product Introduction
Source E. coli
Species Human Rhinovirus
Purity > 95% by SDS-PAGE analyses.
Biological Activity 0.6 IU/μl.
Unit Definition One unit is defined as the amount of enzyme needed to cleave 100 μg of fusion protein in 16 hours to 90% completion at 4°C in a buffer containing 50mM Tris-HCl, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT.
Molecular Weight 24kDa, observed by reducing SDS-PAGE.
Formulation Sterile liquid solution contains 50 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, 50% Glycerol, pH 7.5.
Storage & Stability HRV-3C Protease, His Tag remains stable for 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles.
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HRV-3C Protease, His Tag

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HRV-3C Protease, His Tag

Lane 1: 2 μg of 3C protease, His, Human, reducing (R)
Lane 2: 2 μg of 3C protease, His, Human, non-reducing (NR)
> 95% as analyzed by SDS-PAGE »

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Background
Synonyms rPSP, PSP, HRV 3C Protease
Target Background Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHisfusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-PheGln/GlyPro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.
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For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.


Citations
Melissa S Traver , et al. The Structure of the Arabidopsis PEX4-PEX22 Peroxin Complex—Insights Into Ubiquitination at the Peroxisomal Membrane. Front Cell Dev Biol. (2022-02)
Fu L, et al. Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease. Nature Communications. (2020-09)
Wacker Daniel, et al. Crystal Structure of an LSD-Bound Human Serotonin Receptor. Cell. (2017)
Zheng Yi, et al. Structure of CC Chemokine Receptor 5 with a Potent Chemokine Antagonist Reveals Mechanisms of Chemokine Recognition and Molecular Mimicry by HIV. Immunity. (2017)