3C Protease Protein, HRV, Recombinant (His)

Catalog No. TMPS-00049 Copy Product Info

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.

3C Protease Protein, HRV, Recombinant (His)

Catalog No. TMPS-00049

Copy Product Info

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)

Pack Size	Price	USA Stock	Global Stock
100 U	$85	7-10 days	7-10 days
250 U	$170	7-10 days	7-10 days
500 U	$297	7-10 days	7-10 days

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For research use only—not for human use. No sales to individuals. Use as intended only.

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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	Proteins are shipped with blue 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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