SUMO Protease

Description:
SUMO (Small Ubiquitin-like MOdifiers) Protease is a highly purified Ulp1 from a E. coli expression system, which carries the yeast Ulp1. It recognizes the tertiary structure of SUMO and cleaves SUMO from recombinant fusion proteins. The SUMO protease has a N-terminal His-tag and can be removed by Ni-NTA agarose.

Application:
- Removal of fusion tags from recombinant proteins
- Highly dynamic and precise cleavage capabilities
- Purification of proteins and peptides

Supplied with:
10X high salt and 10X no salt SUMO buffers

10× SUMO Protease Buffer (Salt plus)
500 mM Tris-HCl，pH 8.0
2% Igepal（NP-40）
1.5 M NaCl
10 mM DTT

10× SUMO Protease Buffer (Salt free)
500 mM Tris-HCl，pH 8.0
2% Igepal（NP-40）
10 mM DTT

Source: E. coli
M.W.: 26 kDa
Purity: ≥95%
Label: His-tag
Activity: >10⁵ Unit/mg

Quality Control:
SUMO Protease has greater than 95% purity with no non-specific protease contamination. It is functionally tested for the absence of any non-specific protease activity.

Unit Definition:
One unit of SUMO Protease is defined as the amount of enzyme needed to cleave 85% of 2µg of substrate protein at 30°C in one hour.

Recommended Storage Condition: -80°C

Figures:

Figure 1, Coomassie staining of SUMO Protease in different elution fractions.

Figure 2, RP-HPLC Chromatogram of SUMO Protease.