Anti-UCHL1 (Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1, UCH-L1, Neuron Cytoplasmic Protein 9.5

UCH-L1 is a 24-27kD 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 223aa 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 aa12-15, a second contains an alternative start site at Met82, and a third shows the same start site coupled with a deletion of aa138-153. Full-length human UCH-L1 shares 95% aa identity with mouse UCH-L1. Applications: Suitable for use in Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested. Recommended Dilution: Western Blot: 2ug/ml, Immunohistochemistry: 8-25ug/ml, Immunoprecipitation: 25ug/ml, Optimal dilutions to be determined by the researcher. Storage and Stability: Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.