Recombinant Human TCP1 epsilon/CCT5 protein (GST tag N-Terminus)
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Recombinant Human TCP1 epsilon/CCT5 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 541 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
CCTE, KIAA0098, CCT5, T-complex protein 1 subunit epsilon, TCP-1-epsilon, CCT-epsilon, Chaperonin containing T-complex polypeptide 1 subunit 5
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TCP1 epsilon/CCT5 protein (GST tag N-Terminus) (AB132283)
12.5% SDS-PAGE stained with Coomassie Blue showing ab132283.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CCT5 is part of the cytosolic chaperonin complex called the TRiC (TCP1 Ring Complex) which is essential for the folding of actin and tubulin. This complex ensures that cytoskeletal proteins achieve their correct tertiary structures necessary for maintaining cellular architecture and function. Additionally this complex prevents the misfolding and aggregation of proteins a process that helps maintain cellular homeostasis and prevent cellular stress.
Pathways
CCT5 plays a significant role in the cytoskeleton modeling and protein homeostasis pathways. In the cytoskeleton pathway CCT5's interaction with actin and tubulin is vital ensuring these proteins attain functional conformation. In the protein homeostasis pathway CCT5 assists in degrading misfolded proteins working closely with other components like heat shock proteins (HSPs) to manage cellular protein load effectively. This interaction highlights its importance in preventing the accumulation of damaged proteins.
Specifications
Form
Liquid
General info
Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed : 25467444, PubMed : 36493755, PubMed : 35449234, PubMed : 37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed : 25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed : 20080638).
Sequence similarities
Belongs to the TCP-1 chaperonin family.
Post-translational modifications
Ubiquitinated by the DCX(DCAF12) complex specifically recognizes the diglutamate (Glu-Glu) at the C-terminus, leading to its degradation.
Target data
Product promise
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