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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 Proteins (5) and CCT2 Kits (4) and many more products for this protein.
Showing 10 out of 70 products:
Human Monoclonal CCT2 Primary Antibody for IF, WB - ABIN394185
Fislová, Thomas, Graef, Fodor: Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT. in Journal of virology 2010
Show all 5 references for ABIN394185
Cow (Bovine) Monoclonal CCT2 Primary Antibody for WB - ABIN119784
Satish, Johnson, Abdulally, Post, Ehrlich, Kathju: Cloning and expression of rabbit CCT subunits eta and beta in healing cutaneous wounds. in Cell stress & chaperones 2010
Show all 3 references for ABIN119784
Human Monoclonal CCT2 Primary Antibody for ELISA, WB - ABIN969009
Abe, Yoon, Kubota, Mendoza, Gygi, Blenis: p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling. in The Journal of biological chemistry 2009
Show all 2 references for ABIN969009
Human Monoclonal CCT2 Primary Antibody for EIA, WB - ABIN1109211
Goudreault, DAmbrosio, Kean, Mullin, Larsen, Sanchez, Chaudhry, Chen, Sicheri, Nesvizhskii, Aebersold, Raught, Gingras: A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. in Molecular & cellular proteomics : MCP 2009
Show all 2 references for ABIN1109211
Human Monoclonal CCT2 Primary Antibody for IF, ELISA - ABIN564615
Seo, Baye, Schulz, Beck, Zhang, Slusarski, Sheffield: BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. in Proceedings of the National Academy of Sciences of the United States of America 2010
Show all 2 references for ABIN564615
Frog Monoclonal CCT2 Primary Antibody for IHC (p), WB - ABIN264513
Kubota, Yokota, Yanagi, Yura: Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits. in European journal of biochemistry / FEBS 1999
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 Antibodies) subunits TCP1 (show TCP1 Antibodies) and CCT2, and potentially the entire TRiC (show MARVELD2 Antibodies) complex, in breast cancer.
Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma.
PDCD5 (show PDCD5 Antibodies) bound the apical domain of the CCTbeta (show PCYT1B Antibodies) subunit, projecting above the folding cavity without entering it. Like PDCD5 (show PDCD5 Antibodies), beta-tubulin (show TUBB Antibodies) also interacts with the CCTbeta (show PCYT1B Antibodies) 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 Antibodies)-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 Antibodies) CCT (show FLVCR2 Antibodies) is identified as a novel physiological substrate for p90 (show CANX Antibodies) ribosomal S6 kinase (show RPS6KB1 Antibodies) (RSK (show RPS6KA1 Antibodies)) and p70 ribosomal S6 kinase (S6K (show RPS6KB1 Antibodies)).
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 Antibodies) 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)