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The protein encoded by CCT5 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 CCT5 Proteine (4) und CCT5 Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 77 products:
Human Monoclonal CCT5 Primary Antibody für IF, IHC (p) - ABIN564973
Inoue, Aizaki, Hara, Matsuda, Ando, Shimoji, Murakami, Masaki, Shoji, Homma, Matsuura, Miyamura, Wakita, Suzuki: Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein. in Virology 2011
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Cow (Bovine) Monoclonal CCT5 Primary Antibody für GS, IP - ABIN2477953
Donohue, Miller: Adenocarcinoma of the prostate: biopsy to whole mount. Denver VA experience. in The Urologic clinics of North America 1991
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CCT5 complex caps (zeige CAPS Antikörper) mutant mHTT fibrils at their tips and encapsulates mHTT oligomers, providing a structural description of the inhibition of mHTTQ46-Ex1 (zeige FRMD6 Antikörper) by CCT5 complex and a shared mechanism of mHTT inhibition between TRiC (zeige MARVELD2 Antikörper) chaperonin (zeige HSPD1 Antikörper) and the CCT5 complex
H147R CCT5 was not as efficient in chaperoning these substrates as wild type CCT5.
Both CCT4 (zeige CCT4 Antikörper) and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin (zeige HSPD1 Antikörper) reactions without other partner subunits.
introduction of the truncated human CCT epsilon subunit (zeige CHRNE Antikörper) into yeast cells
A missense mutation within the CCT5 gene is associated with autosomal recessive mutilating sensory neuropathy with spastic paraplegia.
mRNA expression of CCT5, RGS3 (zeige RGS3 Antikörper), and YKT6 (zeige YKT6 Antikörper) was significantly up-regulated in p53 (zeige TP53 Antikörper)-mutated tumors and associated with a low response rate to docetaxel.
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 have been observed but have not been thoroughly characterized. In addition, three pseudogenes of this gene have been identified.
chaperonin containing TCP1, subunit 5 (epsilon)
, T-complex protein 1 subunit epsilon
, T-complex protein 1 subunit epsilon-like
, t-complex protein 1 subunit epsilon-like
, T-complex protein 1, epsilon subunit
, chaperonin subunit 5 (epsilon)
, TCP-1 epsilon
, chaperonin containing TCP1, subunit 5 (epsilon) a