Products from BPS Bioscience require a minimum order value above 400€
Applications: Useful for removal of SUMO-tags from recombinant SUMO fusion proteins
Background: SUMO Protease 2, a highly active and robust recombinant protease, cleaves hSUMO3 from recombinant fusion proteins. Unlike thrombin, EK, or TEV protease, which recognize short, linear sequences, SUMO Protease 2 recognizes the tertiary structure of huSUMO3. As a result, SUMO Protease 2 will not cleave within the fused protein of interest.
Description: Human SENP2 recombinant protein, with N-terminal His-tag, expressed in E. coli.
Format: Aqueous buffer solution
Formulation: 50 mM HEPES, pH 7.5, 150 mM NaCl, 10% glycerol
Purity: ≥95% by SDS-PAGE and RP-HPLC
Storage Stability: Store at or below -80°C. Stable as supplied for up to 1 year when stored dessicated at -80°C.
Supplied As: 10U/µl in aqueous buffer
Tags: N-terminal His-tag
Uniprot: Q9HC62
Unit Definition: 1 Unit of SUMO Protease 2 cleaves >90% of 100 µg SUMO Protease 2 Control Protein in 1 hour (37°C)
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. MarblestoneJG, et al. (2006). "Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO," Protein Science, 15:182-9.
2. Butt TR, Edavettal SC, Hall JP, Mattern MR (2005). "SUMO fusion technology for difficult-to-express proteins," Protein Expr Purif., 43(1):1-9.
3. Zuo X, et al. (2005). "Enhanced expression and purification of membrane proteins by SUMO fusion in Escherichia coli.," J. Struct. Funct. Gen., 6:103-11.
4. Malakhov MP, et al. (2004). "SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins," J. Struct. Funct.Gen., 5:75-86.
English
Deutsch
