Synphilin-1 is a cytoplasmic protein that is enriched in the neurophil of normal human brain.  Although the exact function of synphilin-1 is unknown, it may possibly have a role as a cytoskeletal protein based on the presence of ankyrin-like repeats and an ATP, GTP-binding domain. It has been shown to be novel is its ability to associate in vivo with a-synuclein to form cytoplasmic eosinophilic inclusions.  Additionally, it has been observed to be present in Lewy bodies of Parkinson disease, which are composed of a-synuclein.  Because synphilin-1 is not found in protein aggregates of Alzheimer’s disease, it appears to be specific for a-synuclein-containing lesions.  Synphilin-1 may facilitate the aggregation of a-synuclein into Lewy bodies.

A goat antiserum to a synthetic peptide that corresponds to amino acids 829-847 of the C-terminus of the human synphilin-1 is currently available. This antiserum has been shown to be immunoreactive with the unconjugated immunizing peptide by ELISA. It also labels Lewy bodies in Parkinson’s disease using formalin-fixed, paraffin-embedded sections and it labels a 90 kD in western blots.  This antibody should be a valuable tool for scientists working to understand the role of synphilin-1 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. 

Manufacturing Reference:

Southwest Immunology, Inc., unpublished results.