|Other Accession||P80313, Q5ZJK8, Q2NKZ1, NP_006420.1|
|Other Names||T-complex protein 1 subunit eta, TCP-1-eta, CCT-eta, HIV-1 Nef-interacting protein, CCT7, CCTH, NIP7-1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 79-92 of HUMAN CCT7|
|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. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes 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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6.
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)
Guo, D., et al. Biochem. Biophys. Res. Commun. 337(4):1308-1318(2005)
Hanafy, K.A., et al. J. Biol. Chem. 279(45):46946-46953(2004)
Imai, Y., et al. J. Biol. Chem. 278(51):51901-51910(2003)
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