Cysteine String Protein ELISA Kits

Cysteine string protein (CSP) is a member of the DnaJ/Hsp40 family of co-chaperones that localises to neuronal synaptic vesicles. Its name derives from the possession of a string of 12Ð15 cysteine residues, palmitoylation of which is required for targeting to post-Golgi membranes. The DnaJ domain of CSP enables it to bind client proteins and recruit Hsc70 chaperones, thereby contributing to the maintenance of protein folding in the presynaptic compartment. Are evolutionary highly conserved members of the Hsp40 protein family and are localized to synaptic vesicles and secretory granules. Mutation of CSP in flies, worms and mice reduces lifespan and causes synaptic dysfunction and neurodegeneration. Present on a wide range of types of secretory vesicles in neuronal and non-neuronal tissues. They contain a Dna-J domain and a characteristic string of palmitoylated cysteine residues that is responsible for membrane targeting. Mammals contain three CSP genes (CSP_, CSP_, and CSP_), with CSP_ being the only CSP isoform in brain.

Recent studies have revealed that the neurodegenerative disease, adult onset neuronal ceroid lipofuscinosis, is caused by mutations in the human CSP_-encoding DNAJC5 gene. Contains a conserved J domain. CSP has a characteristic HPD motif in the J-domain that is required in this family of proteins to allow them to bind to Hsc70/Hsp70 and act in concert with Hsc70/Hsp70 in the refolding or disaggregation of client proteins. CSP_ have revealed that CSP_ prevents presynaptic degeneration. CSP_ chaperones key proteins of the synaptic vesicle cycle that become nonfunctional under use-dependent stress. Biochemical analysis of CSP demonstrated that it could indeed bind to and activate the ATPase activity of Hsc70.