Recombinant Human T-complex protein 1 subunit beta (CCT2)

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Code CSB-EP004856HU
MSDS
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
CCT2
Uniprot No.
Research Area
Signal Transduction
Alternative Names
99D8.1; CCT 2; CCT beta; CCT-beta; CCT2; CCTB; Chaperonin containing t complex polypeptide 1 beta subunit; Chaperonin containing t complex polypeptide 1 subunit 2; Chaperonin containing TCP1 subunit 2; Chaperonin containing TCP1 subunit 2 (beta); CTP:phosphocholine cytidylyltransferase 2; Epididymis secretory sperm binding protein Li 100n; HEL S 100n; MGC142074; MGC142076; MGC94480; PRO1633; T complex protein 1 beta subunit; T complex protein 1 subunit beta; T-complex protein 1 subunit beta; TCP 1 beta; TCP-1-beta; TCPB_HUMAN
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
2-535aa
Target Protein Sequence
ASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
70.3 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or 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
Tris-based buffer,50% glycerol
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
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Amino acids 2-535 form the expressed segment for recombinant Human CCT2. The expected molecular weight for the CCT2 protein is calculated to be 73.4 kDa. The CCT2 protein was expressed in e.coli. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of CCT2, making it easier to detect and purify the CCT2 recombinant protein in the later stages of expression and purification.

T-complex protein 1 subunit beta (CCT2) is a crucial molecular chaperone in cells, primarily involved in the process of protein folding. Research on CCT2 plays a vital role in our understanding of protein folding and maintaining structural integrity within cells. In cancer research, the expression of CCT2 is associated with various types of tumors, particularly playing a significant role in the proliferation and invasion of tumor cells. Scientists aim to uncover the molecular mechanisms of CCT2 in cancer development, hoping to provide new targets for cancer treatment. Additionally, CCT2 is linked to research on neurological disorders. Its function in neurons may be related to the occurrence of neurodegenerative diseases. Scientists are working to gain a deeper understanding of the role of CCT2 in the nervous system, aiming to provide new clues for the treatment of related diseases.

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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. the novel LCA mutations in CCTbeta and the impact of chaperon disability by these mutations in cellular biology. PMID: 27645772
  2. A role for the TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, in breast cancer. PMID: 25704758
  3. Increased expression of CCT2 is associated with tumor progression and the clinical behavior of gallbladder carcinoma. PMID: 23782473
  4. PDCD5 bound the apical domain of the CCTbeta subunit, projecting above the folding cavity without entering it. Like PDCD5, beta-tubulin also interacts with the CCTbeta apical domain, but a second site is found at the sensor loop deep within the folding cavity. PMID: 24375412
  5. PB2 associates with CCT2 as a monomer and the CCT binding site is located in a central region of the PB2 protein. PMID: 20573828
  6. The chaperonin CCT is identified as a novel physiological substrate for p90 ribosomal S6 kinase (RSK) and p70 ribosomal S6 kinase (S6K). PMID: 19332537

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Subcellular Location
Cytoplasm.
Protein Families
TCP-1 chaperonin family
Database Links

HGNC: 1615

OMIM: 605139

KEGG: hsa:10576

STRING: 9606.ENSP00000299300

UniGene: Hs.189772

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