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| Cat.No | ACP23021 | Target Name | CCT5 |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Expression Range | 2-541 | Protein Length | Full Length of Mature Protein |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P48643 |
|---|
Uniprot Id
P48643
Target Species
Human
Target Name
CCT5
Target Full Name
T-complex protein 1 subunit epsilon
Target Function
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. 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. The TRiC complex plays a role in the folding of actin and tubulin.
Target Involvement
Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP)
Target Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Target Protein Families
TCP-1 chaperonin family
Target Synonyms
CCT 5; CCT epsilon ; CCT-epsilon; CCT5; CCTE; CCTepsilon; Chaperonin containing T-complex polypeptide 1; subunit 5; Chaperonin containing TCP 1 epsilon; Chaperonin containing TCP 1 subunit 5; Chaperonin containing TCP 1 subunit 5 epsilon; Chaperonin containing TCP1 epsilon; Chaperonin containing TCP1 subunit 5; Chaperonin containing TCP1 subunit 5 epsilon; KIAA0098; T complex protein 1 epsilon subunit; T complex protein 1 subunit epsilon; T-complex protein 1 subunit epsilon; TCP 1 epsilon; TCP-1-epsilon; TCP1epsilon; TCPE; TCPE_HUMAN
Target Background
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. Mutations in this gene cause hereditary sensory and autonomic neuropathy with spastic paraplegia (HSNSP). Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 13.
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