|Other Names||T-complex protein 1 subunit delta, TCP-1-delta, CCT-delta, Stimulator of TAR RNA-binding, CCT4, CCTD, SRB|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cytoplasm. Melanosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
The chaperonin containing TCP1 (MIM 186980) complex (CCT),also called the TCP1 ring complex, consists of 2 back-to-backrings, each containing 8 unique but homologous subunits, such asCCT4. CCT assists the folding of newly translated polypeptidesubstrates through multiple rounds of ATP-driven release andrebinding of partially folded intermediate forms. Substrates of CCTinclude the cytoskeletal proteins actin (see MIM 102560) andtubulin (see MIM 191130), as well as alpha-transducin (MIM 139330)(Won et al., 1998 [PubMed 9819444]).
Mukherjee, K., et al. BMC Evol. Biol. 10, 64 (2010) :Zebol, J.R., et al. Int. J. Biochem. Cell Biol. 41(4):822-827(2009)Chi, A., et al. J. Proteome Res. 5(11):3135-3144(2006)Hillier, L.W., et al. Nature 434(7034):724-731(2005)Imai, Y., et al. J. Biol. Chem. 278(51):51901-51910(2003)
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