Human UCH-L1/PGP9.5 Alexa Fluor® 594-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: UCH-L1/PGP9.5

UCH-L1 (ubiquitin carboxyterminal hydrolase isozyme 1; also PGP9.5) is a 24-27 kDa member of the peptidase C12 family of enzymes. It shows restricted expression, being found in neurons and oocytes. UCH-L1 has dual enzymatic activity. As a monomer, it is a ubiquitin hydrolase that removes ubiquitin from modified proteins; as a homodimer, it acts as a ligase that creates ubiquitin dimers. In neurons, UCH-L1’s most important role appears to be that of generating free ubiquitin. Human UCH-L1 is 223 amino acids (aa) in length. It is O-glycosylated, ubiquitinated, and farnesylated; when farnesylated, it becomes associated with cell membranes. Three potential splice forms are reported. One shows a two aa substitution for aa 12-15, a second contains an alternative start site at Met82, and a third shows the same start site coupled with a deletion of aa 138-153. Full-length human UCH-L1 shares 95% aa identity with mouse UCH-L1.       

Product Datasheets

Related Research Areas

• Deubiquitinating Enzymes (DUBs)
• Neuronal Markers
• Parkinson's Disease Related Molecules
• Search Ubiquitin-related Enzymes
• Ubiquitin-related Molecules in the Akt Pathway