TCP1 alpha Antibody – Polyclonal

The protein encoded by this gene 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. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found. [provided by RefSeq, Jun 2010]

CCTA: 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. Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Belongs to the TCP-1 chaperonin family.

Protein type: Chaperone; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 6q25.3-q26

Cellular Component: acrosome; centrosome; chaperonin-containing T-complex; cytosol; Golgi apparatus; microtubule; myelin sheath; nuclear heterochromatin; pericentriolar material

Molecular Function: ATP binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding

Biological Process: binding of sperm to zona pellucida; positive regulation of telomerase activity; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization; tubulin folding