Recombinant Human T-complex protein 1 subunit alpha (TCP1)

Code CSB-YP023320HU
MSDS
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Source Yeast
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Code CSB-EP023320HU
MSDS
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Source E.coli
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Code CSB-EP023320HU-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-BP023320HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP023320HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
TCP1
Uniprot No.
Alternative Names
AI528772; c-cpn; CCT alpha; CCT; CCT-alpha; CCT1; Ccta; CCTalpha; D6S230E; MGC133746; p63; T complex 1; T complex protein 1 alpha subunit; T complex protein 1; T-complex homolog TCP1; T-complex protein 1 subunit alpha; T-complex protein 1 subunit alpha B; Tailless complex polypeptide 1; Tailless complex polypeptide 1A; Tailless complex polypeptide 1B; TCP 1 alpha; Tcp-1; TCP-1-alpha; TCP1; TCPA_HUMAN; Tp63; TRic
Species
Homo sapiens (Human)
Expression Region
1-556
Target Protein Sequence
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND
Protein Length
Full length 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. Chaperonin CCT interferes with fibre assembly by interaction of its CCTzeta and CCTgamma subunits with the A53T central hydrophobic region. This interaction is specific to NAC conformation, as it is produced once soluble alpha-synuclein A53T oligomers form and blocks the reaction before fibres begin to grow. PMID: 28102321
  2. chaperonin-containing TCP-1 complex required for lysosomal functioning and autophagosome degradation PMID: 27929117
  3. Result suggest the positive correlation between purinergic receptor P2X 7 (P2X7R) and T-complex protein 1 (TCP-1) in lymphoma patients. PMID: 26556873
  4. Data suggest that biosynthesis and folding of leukemogenic fusion oncoprotein AML1-ETO/RUNX1-RUNX1T1 is facilitated by interaction with the chaperonin TRiC/CCT1/TCP1 and HSP70 (heat shock protein 70). PMID: 26706127
  5. Changes for CRMP2, TCP1epsilon, TPM2 and 14-3-3gamma were confirmed in experimental tumors and in a series of 28 human SI-NETs. PMID: 25224486
  6. A role for the TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, in breast cancer. PMID: 25704758
  7. CCT8 might be an oncogene and participate in HCC cell proliferation. PMID: 24862099
  8. identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain PMID: 24846140
  9. Data suggest that specific molecular mediators involved in glucocerebrosidase maturation and degradation, and abnormal interaction with TCP1 and c-Cbl, could be responsible for phenotypic variation among patients with the same genotypes. PMID: 21098288
  10. the membrane binding domain of CTP:phosphocholine cytidylyltransferase has a role in alveolar type II cells PMID: 19684306
  11. Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1. PMID: 11771755
  12. TRiC chaperonin binds to HIF prolyl hydroxylase PHD3 PMID: 15251459
  13. the strong inhibitory action of PhLP(S) on Gbetagamma signaling is the result of a previously unrecognized mechanism of Gbetagamma-regulation, inhibition of Gbetagamma-folding by interference with TCP-1alpha PMID: 15745879
  14. Data show that Plk1 associates with chaperonin-containing TCP1 complex (CCT) both in vitro and in vivo. PMID: 15923617
  15. The specific and directed rearrangement of the beta-actin structure, seen in the natural beta-actin-TRiC system, is vital for guiding beta-actin to the native state. PMID: 17939680
  16. a paper describing a pathway in which this gene product functions PMID: 1630491

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Subcellular Location
Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families
TCP-1 chaperonin family
Database Links

HGNC: 11655

OMIM: 186980

KEGG: hsa:6950

STRING: 9606.ENSP00000317334

UniGene: Hs.363137

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