Ubiquitin carboxyl-terminal hydrolase L1 (UCH –L1) is one of the most abundant proteins in the brain and represents 1-2% of total soluble brain proteins.  UCH-L1 activity is thought to cleave polymeric ubiquitin to monomers and to hydrolyze bonds between ubiquitin-protein conjugatges to regenerate ubiquitin monomers.   In many degenerative diseases, ubiquitin has been identified as a component of several inclusion bodies and certain of these are associated with UCH-L1 activity.  One such inclusion is the Lewy body of Parkinson’s disease.  Since a polymorphism has been detected in the UCH-L1 gene, it is suspected to have a role is some forms of Parkinson’s disease.

A goat antiserum to a synthetic peptide that corresponds to amino acids 46-63 of the N-terminus of the human UCH-L1 is currently available. This antiserum has been shown to be immunoreactive with the unconjugated immunizing peptide by ELISA. It also labels a 27 kD protein in western blots.  This antibody should be a valuable tool for scientists working to understand the role of UCH-L1 in Parkinson’s disease.

This antiserum was produced using proprietary methodology whereby the peptide is attached to a carrier that elicits minimal immunoreactivity so that the antiserum has a higher degree of specificity for the peptide.  Since there is no overwhelming production of interfering antibodies to the carrier, this antiserum can routinely be used without further purification.  Pseud-Immune™ control immune serum (Cat no. GPA018E) from a mock immunized animal is available to be used in conjunction with this antibody as well as the immunizing peptide (Cat no. HSP016N) which can be used to neutralize immunoreactivity.

Manufacturing Reference:    

Southwest Immunology, Inc., unpublished results.