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The protein encoded by CCT2 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). Additionally we are shipping CCT2 Antibodies (89) and CCT2 Kits (10) and many more products for this protein.
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Chaperonin containing T-complex polypeptide beta subunit is the only subunit message to be reduced in wounded mucosa versus unwounded control, and this reduction was confirmed at the protein level.
CCT-beta mRNA remains unchanged in both fetal and adult wound tissues.
A role for the TRiC (show MARVELD2 Proteins) subunits TCP1 (show TCP1 Proteins) and CCT2, and potentially the entire TRiC (show MARVELD2 Proteins) complex, in breast cancer.
Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma.
PDCD5 (show PDCD5 Proteins) bound the apical domain of the CCTbeta (show PCYT1B Proteins) subunit, projecting above the folding cavity without entering it. Like PDCD5 (show PDCD5 Proteins), beta-tubulin (show TUBB Proteins) also interacts with the CCTbeta (show PCYT1B Proteins) apical domain, but a second site is found at the sensor loop deep within the folding cavity.
Destruction of the beta-tubulin:CCT-beta complex provokes Hsp90 (show HSP90 Proteins)-dependent protein ubiquitination and degradation.
PB2 associates with CCT2 as a monomer and the CCT binding site is located in a central region of the PB2 protein.
The chaperonin (show HSPD1 Proteins) CCT (show FLVCR2 Proteins) is identified as a novel physiological substrate for p90 (show CANX Proteins) ribosomal S6 kinase (show RPS6KB1 Proteins) (RSK (show RPS6KA1 Proteins)) and p70 ribosomal S6 kinase (S6K (show RPS6KB1 Proteins)).
role of chaperonin-containing t-complex polypeptide 1 beta (CCT2) in the regulation of mesangial cell contraction, proliferation, and migration with filamentous/globular-(F/G-) actin (show ACTB Proteins) ratio under high glucose induction
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. Two transcript variants encoding different isoforms have been found for this gene.
T-complex protein 1 subunit beta
, chaperonin containing TCP1, subunit 2 (beta)
, T-complex protein 1 subunit beta-like
, subunit 2
, chaperonin-containing T-complex polypeptide beta subunit
, t-complex protein 1 subunit beta-like
, T-complex protein 1, beta subunit
, chaperonin containing t-complex polypeptide 1, beta subunit
, chaperonin containing t-complex polypeptide 1, subunit 2
, chaperonin subunit 2 (beta)