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.
Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion.
Human Trypsin 1, encoded by the PRSS1 gene, is also known as cationic trypsinogen. It contains a signal peptide (residues 1‑15), a pro region (residues 16‑23), and a mature chain (residues 24‑247).
25,000 U, 100 U/μl
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