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Lyophilized from sterile 20mM Tris, 500mM NaCl, 20% glycerol, 1mM DTT, pH 8.0, 5 % trehalose and 5 % mannitol.
Bio-activity
Measured by the hydrolysis of UbiquitinAMC. The specific activity is>140 pmoles/min/μg.
Molecular Mass
Recombinant Human UCHL1 consisting of 229 amino acids and migRates as an 25.6 kDa band in SDS-PAGE under reducing conditions as predicted.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 92 % by SDS-PAGE.
Storage
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C). Avoid repeated freeze/thaw cycles.
Reconstitution
Reconstitute in sterile distilled water to a concentration of 0.1-1.0 mg/mL.
Warning
For research use only!
Background
Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity.
Tag
His
Species
Human
Source
E. coli
BACKGROUND
Background
Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity.
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