catalog number :
MBS961285
products type :
Recombinant Protein
products full name :
Recombinant Human T-complex protein 1 subunit beta
products short name :
T-complex protein 1 subunit beta
products name syn :
CCT-beta
other names :
T-complex protein 1 subunit beta isoform 2; T-complex protein 1 subunit beta; T-complex protein 1 subunit beta; chaperonin containing TCP1 subunit 2; CCT-beta
products gene name :
CCT2
other gene names :
CCT2; CCT2; CCTB; 99D8.1; PRO1633; CCT-beta; HEL-S-100n; TCP-1-beta; 99D8.1; CCTB; TCP-1-beta
uniprot entry name :
TCPB_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
2-535
sequence :
ASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVK
STLGPKGMDKILLSSGRDASLMVTNDGATILKNIGVDNP
AAKVLVDMSRVQDDEVGDGTTSVTVLAAELLREAESLIA
KKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQ
DLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNL
EAIHIIKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENA
KILIANTGMDTDKIKIFGSRV
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Signal Transduction
products description :
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin.
products references :
Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT.Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.Mol. Cell. Biol. 18:7584-7589(1998)
ncbi acc num :
NP_001185771.1
ncbi gb acc num :
NM_001198842.1
ncbi mol weight :
73.36kD
ncbi pathways :
Assembly Of The Primary Cilium Pathway (1268846); Association Of TriC/CCT With Target Proteins During Biosynthesis Pathway (1268699); BBSome-mediated Cargo-targeting To Cilium Pathway (1268850); Cargo Trafficking To The Periciliary Membrane Pathway (1268848); Chaperonin-mediated Protein Folding Pathway (1268694); Cooperation Of Prefoldin And TriC/CCT In Actin And Tubulin Folding Pathway (1268695); Folding Of Actin By CCT/TriC Pathway (1268698); Formation Of Tubulin Folding Intermediates By CCT/TriC Pathway (1268697); Metabolism Of Proteins Pathway (1268677); Organelle Biogenesis And Maintenance Pathway (1268838)
ncbi summary :
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. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
uniprot summary :
CCT-beta: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Belongs to the TCP-1 chaperonin family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Chaperone. Chromosomal Location of Human Ortholog: 12q15. Cellular Component: chaperonin-containing T-complex; cytoplasm; cytosol; microtubule; myelin sheath. Molecular Function: ATP binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding. Biological Process: 'de novo' posttranslational protein folding; binding of sperm to zona pellucida; cellular protein metabolic process; chaperone cofactor-independent protein folding; chaperone-mediated protein complex assembly; positive regulation of telomerase activity; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization