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].
custom-made
TCP1
Origin: Human
Host: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
TCP1
Origin: Mouse
Host: HEK-293 Cells
Recombinant
> 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
custom-made
TCP1
Origin: Mouse
Host: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
SDS, ELISA, WB
custom-made
TCP1
Origin: Human
Host: Cell-free protein synthesis (CFPS)
Recombinant
approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
SDS, ELISA, WB
Latest Publications for our TCP1 alpha/CCTA Proteins
Hirai, Maeda, Omori, Yamamoto, Kokeguchi, Takashiba: "Serum antibody response to group II chaperonin from Methanobrevibacter oralis and human chaperonin CCT." in: Pathogens and disease, Vol. 68, Issue 1, pp. 12-9, (2013) (PubMed).