SUMO protease, also known as Ulp, is a protease
that specifically removes small ubiquitin-related modifier (SUMO) in any recombinant SUMO fusion protein. Different
from other tag removal proteases such as enterokinase (EK) and TEV which
recognize a specific amino acid sequence and cut at a specific cleavage site,
SUMO protease recognizes the SUMO tertiary structure and cleave it, more
specifically and leaving no residual amino acids. |
Source |
Recombinant SUMO Protease expressed in E.coli |
Species |
Saccharomyces
cerevisiae |
Tag |
His Tag |
Molecular Weight |
Predicted MW: 27 kDa |
Purity |
≥ 95% as analyzed by
SDS-PAGE |
Endotoxin Level |
< 0.2 EU/μg of
protein by gel clotting method |
Biological Activity |
10 U/μl Unit definition: One unit of SUMO Protease cleaves ≥ 85% of 2 μg control substrate in 1 h at 30℃ |
Storage Buffer | 25 mM Tris-HCl, 0.1% Igepal (NP-40), 250 mM NaCl, 0.5 mM DTT, 50% (v/v) glycerol, pH 8.0 |
Storage & Stability |
Upon receiving, the product remains stable for
up to 6 months at -20 °C. This product is stable for up to 1 week at 37 °C.
Avoid repeated freeze-thaw cycles by making single-use aliquots before the
solution is stored at -20 °C. |
»
Lane 1: 2 μg of SUMO Protease Animal-Free, His, non-reducing (NR)
Lane 2: 2 μg of SUMO Protease Animal-Free, His, reducing (R)
> 95% as analyzed by SDS-PAGE
»
For
laboratory research or manufacture use only. Direct human use, including taking
orally and injection and clinical use are forbidden.