NUPTEC Inc. Ltd.

Product Details

Professional Manufaturer of Resins for Protein Purification

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SUMO protease (histidine tag)
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  • SUMO protease (histidine tag)

Catalog No:

NRPA31S

Product Name:

SUMO protease (histidine tag)


SUMO protease (Small Ubiquitin-like MOdifiers Protease 1), also known as Ulp(Ubl-specific protease ), is a highly active cysteine protease found in Saccharomyces cerevisiae, which can specifically recognize the tertiary structure of ubiquitin-like protein (SUMO protein), rather than the amino acid sequence, and specific cleavage occurs. SUMO protein is often used as a fusion tag, which can effectively improve the solubility, stability and expression of the target protein in the prokaryotic expression system (or eukaryotic expression system). SUMO tag fusion protein can be cleaved by SUMO protease after expression and purification. SUMO protease cleaves after two consecutive glycine sequences (-Gly-Gly) at the C- terminal of SUMO tag. Reasonable design can make the N-terminal of the cleaved target protein free of any excess amino acids. SUMO protease (histidine tag) A histidine tag is added to the N-terminal of the amino acid sequence of SUMO protease. It is a high-purity SUMO protease obtained by fusion expression in E. coli and purified by a variety of chromatographic methods. The optimal reaction temperature of the enzyme is 30 ℃, but under certain reaction conditions (4-30 ℃, pH7.5-9, etc.), it can maintain efficient cleavage activity, and the fusion of histidine tag is convenient for the target protein to be cleaved and removed by metal chelate Affinity chromatograph.

Product features and technical indicators

Product Name

SUMO protease (histidine tag)(SUMO Protease , His-tag; SUMO-P(His))

Catalog No.

NRPA31

Specifications

1mg,10mg,100mg,500mg

Product form

Solution form, 5mM PB, 2mM DTT, pH 8.0, 50% glycerol

molecular weight

27.8 kDa

isoelectric point

6.34

specific activity

≥120,000u/mg

absorption coefficient

UV absorption method, extinction coefficient E(0.1% at 280 nm) = 1.026

Source

Escherichia coli

Purity

≥ 95%(SDS-PAGE detection)

Save condition

-20 ℃ preservation

Conditions of transport Low temperature transportation of dry ice
Validity Period 3 years
Activity Definition In a buffer system (20mM Tris-HCl) at pH 8.0, the reaction was carried out at 30 ° C. for 1h to cleave 90% of 4 μg of substrate protein, and the amount of enzyme required was 1U.