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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).
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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.
the novel LCA (zeige CLTA Proteine) mutations in CCTbeta (zeige PCYT1B Proteine) and the impact of chaperon disability by these mutations in cellular biology.
A role for the TRiC (zeige MARVELD2 Proteine) subunits TCP1 (zeige TCP1 Proteine) and CCT2, and potentially the entire TRiC (zeige MARVELD2 Proteine) complex, in breast cancer.
Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma.
PDCD5 (zeige PDCD5 Proteine) bound the apical domain of the CCTbeta (zeige PCYT1B Proteine) subunit, projecting above the folding cavity without entering it. Like PDCD5 (zeige PDCD5 Proteine), beta-tubulin (zeige TUBB Proteine) also interacts with the CCTbeta (zeige PCYT1B Proteine) 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 (zeige HSP90 Proteine)-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 (zeige HSPD1 Proteine) CCT (zeige FLVCR2 Proteine) is identified as a novel physiological substrate for p90 (zeige CANX Proteine) ribosomal S6 kinase (zeige RPS6KB1 Proteine) (RSK (zeige RPS6KA1 Proteine)) and p70 ribosomal S6 kinase (S6K (zeige RPS6KB1 Proteine)).
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 (zeige ACTB Proteine) 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)