3C Protease Protein, HRV, Recombinant (His)

Catalog No. TMPS-00049

Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins.

rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography.

The recombinant enzyme consists of 217 amino acids, has a molecular mass of approximately 24 kDa, and is produced through proprietary purification methods. It is fully biologically active.

3C Protease Protein, HRV, Recombinant (His)

Catalog No. TMPS-00049

Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins.<br/><br/>rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography.<br/><br/>The recombinant enzyme consists of 217 amino acids, has a molecular mass of approximately 24 kDa, and is produced through proprietary purification methods. It is fully biologically active.

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Product Information

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 50 mM Tris-HCl, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT.
Description	Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins. rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography. The recombinant enzyme consists of 217 amino acids, has a molecular mass of approximately 24 kDa, and is produced through proprietary purification methods. It is fully biologically active.
Species	Human Rhinovirus
Tag	His
Synonyms	rPSP,PSP,HRV 3C Protease
Protein Purity	> 95% as determined by SDS-PAGE
Molecular Weight	24 kDa (Reducing conditions)
Formulation	Sterile liquid solution contains 50 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, 50% Glycerol, pH 7.5.
Stability & Storage	Recombinant PreScission Protease (rPSP) remains stable up to 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles.
Shipping	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background	Recombinant PreScission Protease (rPSP) is a highly purified, restriction-grade 6×His-tagged protease derived from human rhinovirus 3C (HRV 3C). It specifically cleaves at the recognition sequence Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP), with the cleavage occurring between the Gln and Gly residues. This protease is commonly used to remove affinity tags from fusion proteins. rPSP functions optimally at 30 °C, but retains activity at temperatures as low as 4 °C. Cleavage efficiency may vary with different fusion proteins, so optimization of enzyme amount, incubation time, and temperature is recommended. The His-tag allows easy removal of the protease after digestion using Ni²⁺ affinity chromatography.

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