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 ~220aa that share more than 40% aa 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. 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.
Applications:
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution:
Western Blot: 1:2000
Optimal dilutions to be determined by the researcher.
Positive Control:
SK-N-MC cells
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.