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3C Protease Protein, HRV, Recombinant (His)

3C Protease Protein, HRV, Recombinant (His)
产品编号 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)

3C Protease Protein, HRV, Recombinant (His)

3C Protease Protein, HRV, Recombinant (His)
产品编号 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.
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产品信息

生物活性
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.
产品描述
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.
种属
Human Rhinovirus
标签His
别名
rPSP,PSP,HRV 3C Protease
蛋白纯度
> 95% as determined by SDS-PAGE
分子量24 kDa (Reducing conditions)
缓冲液Sterile liquid solution contains 50 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, 50% Glycerol, pH 7.5.
存储
Recombinant PreScission Protease (rPSP) remains stable up to 1 year at -20°C from date of receipt. Please avoid freeze-thaw cycles.
运输方式In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
研究背景
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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