Anti-TCP1 epsilon/CCT5 Antibody Picoband® Fluoro488 Conjugated

CCT5 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC) . This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Mutations in this gene cause hereditary sensory and autonomic neuropathy with spastic paraplegia (HSNSP) . Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 13.

E. coli-derived human CCT5 recombinant protein (Position: L443-K535) . Human CCT5 shares 95.7% amino acid (aa) sequence identity with both mouse and rat CCT5.

Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta. .

Actin Assembly, Actin, etc., Chaperones, Cytoskeleton, Cytoskeleton/ECM, Microfilaments, Microtubules, Protein Trafficking, Signal Transduction, Tubulin

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. .

1. Bouhouche, A., Benomar, A., Bouslam, N., Chkili, T., Yahyaoui, M. Mutation in the epsilon subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441-443, 2006. 2. Liou, A. K. F., Willison, K. R. Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes. EMBO J. 16: 4311-4316, 1997.