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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Mouse / IgG2b, kappa|
|Immunogen||Recombinant human protein purified from E.coli (GST-UCHL3)|
|Storage buffer||HEPES with 0.15M NaCl, 0.01% BSA, 50% glycerol|
|Contains||0.03% sodium azide|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay Dependent|
|Western Blot (WB)||0.5 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
A suggested positive control for this product is SK-N-MC cells.
The two ubiquitin C-terminal hydrolase (UCH) enzymes, UCHL1 and UCHL3, deubiquitinate ubiquitin-protein conjugates and control the cellular balance of ubiquitin. UCHL1 and UCHL3 are both small proteins of ~220 amino acids that share more than 40% amino acid sequence identity. UCHL3 is universally expressed in all tissues, while UCHL1 is expressed exclusively in neuronal tissue, testis and ovary. The activity of UCHL3 is more than 200 fold higher than UCHL1 when a fluorogenic ubiquitin substrate is used. UCHL1 associates with monoubiquitin and UCHL3 binds to Nedd8, ubiquitin-like protein. UCHL1 and UCHL3 play a role in the regulation of neuronal development and spermatogenesis. UCHL1 is involved in the pathogenesis of Parkinson's disease (PD) and Alzheimer's disease (AD). Down-regulation and extensive oxidative modification of UCHL1 have been observed in the brains of AD patients as well as PD patients.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
testicular tissue protein Li 221; ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase); ubiquitin carboxyl-terminal hydrolase isozyme L3; ubiquitin thioesterase L3; ubiquitin thiolesterase; UCH-L3
RGD1561196; UCH-L3; UCHL3