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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). Zusätzlich bieten wir Ihnen CCT2 Antikörper (102) und CCT2 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
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The retinal pathology observed in the homozygous cct2-L394H-7del mutants resembles the retinal pathology of human leber congenital amaurosis (LCA) patients.
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 mutations in CCTbeta and the impact of chaperon disability by these mutations in cellular biology.
A role for the TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, in breast cancer.
Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma.
PDCD5 bound the apical domain of the CCTbeta subunit, projecting above the folding cavity without entering it. Like PDCD5, beta-tubulin also interacts with the CCTbeta 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-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 CCT is identified as a novel physiological substrate for p90 ribosomal S6 kinase (RSK) and p70 ribosomal S6 kinase (S6K).
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 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)