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

Code CSB-BP004856HU
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Source Baculovirus
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Code CSB-EP004856HU-B
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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-MP004856HU
Size Pls inquire
Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
CCT2
Uniprot No.
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)
Expression Region
2-535
Target Protein Sequence
ASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
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. 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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