Recombinant Human T-complex protein 1 subunit epsilon (CCT5)

Code CSB-YP004862HU
MSDS
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Source Yeast
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Code CSB-EP004862HU
MSDS
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Source E.coli
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Code CSB-EP004862HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP004862HU
MSDS
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Source Baculovirus
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Code CSB-MP004862HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
CCT5
Uniprot No.
Alternative Names
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
Species
Homo sapiens (Human)
Expression Region
2-541
Target Protein Sequence
ASMGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMM VDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAE QLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSC HRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPK KVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAI CQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQE ISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYG GGAAEISCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQ VKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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.
Gene References into Functions
  1. CCT5 complex caps mutant mHTT fibrils at their tips and encapsulates mHTT oligomers, providing a structural description of the inhibition of mHTTQ46-Ex1 by CCT5 complex and a shared mechanism of mHTT inhibition between TRiC chaperonin and the CCT5 complex PMID: 25995452
  2. H147R CCT5 was not as efficient in chaperoning these substrates as wild type CCT5. PMID: 25124038
  3. introduction of the truncated human CCT epsilon subunit into yeast cells PMID: 22232265
  4. A missense mutation within the CCT5 gene is associated with autosomal recessive mutilating sensory neuropathy with spastic paraplegia. PMID: 16399879
Involvement in disease
Neuropathy, hereditary sensory, with spastic paraplegia, autosomal recessive (HSNSP)
Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families
TCP-1 chaperonin family
Database Links

HGNC: 1618

OMIM: 256840

KEGG: hsa:22948

STRING: 9606.ENSP00000280326

UniGene: Hs.1600

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