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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). De plus, nous expédions CCT5 Protéines (4) et CCT5 Kits (1) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 84 products:
Human Monoclonal CCT5 Primary Antibody pour 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. dans Virology 2011
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Cow (Bovine) Monoclonal CCT5 Primary Antibody pour GS, IP - ABIN2477953
Donohue, Miller: Adenocarcinoma of the prostate: biopsy to whole mount. Denver VA experience. dans The Urologic clinics of North America 1991
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CCT5 complex caps (Montrer CAPS Anticorps) mutant mHTT fibrils at their tips and encapsulates mHTT oligomers, providing a structural description of the inhibition of mHTTQ46-Ex1 (Montrer FRMD6 Anticorps) by CCT5 complex and a shared mechanism of mHTT inhibition between TRiC (Montrer MARVELD2 Anticorps) chaperonin (Montrer HSPD1 Anticorps) and the CCT5 complex
H147R CCT5 was not as efficient in chaperoning these substrates as wild type CCT5.
Both CCT4 (Montrer CCT4 Anticorps) and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin (Montrer HSPD1 Anticorps) reactions without other partner subunits.
introduction of the truncated human CCT epsilon subunit (Montrer CHRNE Anticorps) 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 (Montrer RGS3 Anticorps), and YKT6 (Montrer YKT6 Anticorps) was significantly up-regulated in p53 (Montrer TP53 Anticorps)-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.
T-complex protein 1 subunit epsilon
, T-complex protein 1, epsilon subunit
, chaperonin subunit 5 (epsilon)
, TCP-1 epsilon
, chaperonin containing TCP1, subunit 5 (epsilon)
, chaperonin containing TCP1, subunit 5 (epsilon) a
, T-complex protein 1 subunit epsilon-like
, t-complex protein 1 subunit epsilon-like