Simple Plex Human UCH-L1 Cartridge New

Simple Plex Human UCH-L1 Cartridge Summary

*The Sample Volume represented is based on the amount of sample incorporated into the reaction after taking into account the assay’s minimum required dilution for a given matrix. Serial dilution may be necessary to achieve some of the final sample volumes represented.

Product Summary

Precision

Cell Culture Supernates, Serum, EDTA Plasma, Heparin Plasma, Cerebrospinal Fluid

Recovery

Linearity

Product Datasheets

Preparation and Storage

Background: UCH-L1/PGP9.5

Ubiquitin Carboxyl-terminal Esterase L1 (UCH-L1), also known as PGP9.5, is a deubiquitinating enzyme with a predicted molecular weight of 25 kDa. The human protein shares 95% amino acid sequence identity with its mouse and rat orthologs. UCH-L1 is expressed abundantly in neurons, accounting for 1-2% of total soluble proteins in the brain. It localizes primarily to the cytoplasm, but a subpopulation has been shown to be transiently nuclear. UCH-L1 contains two catalytic residues, Cys90 and His161, which are required for isopeptide bond cleavage at the C-terminal glycine residue of Ubiquitin. The levels of free Ubiquitin appear to be partially regulated by UCH-L1 through the hydrolysis of small Ubiquitin chains and the stabilization of monomeric Ubiquitin. Mice lacking functional UCH-L1 show neuronal dysfunction and neurodegeneration, and mutations in this enzyme have been linked to Parkinson's disease, suggesting that it is important for proper central nervous system function. UCH-L1 also likely plays a complex role in cancer. It has been reported to function as an oncogene in lymphoma, colorectal cancer, and nonsmall cell lung carcinoma. In contrast, it is thought to function as a tumor suppressor protein in nasopharyngeal and breast cancers.

Related Research Areas

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