|Other Names||Tubulin-specific chaperone E, Tubulin-folding cofactor E, TBCE|
|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||Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network.|
|Cellular Location||Cytoplasm. Cytoplasm, cytoskeleton|
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Provided below are standard protocols that you may find useful for product applications.
Cofactor E is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state.
Biernacki, M.A., et al. Cancer Res. 70(3):906-915(2010) Padidela, R., et al. J. Clin. Endocrinol. Metab. 94(8):2686-2691(2009) Lindgren, C.M., et al. PLoS Genet. 5 (6), E1000508 (2009) Jin, S., et al. Development 136(9):1571-1581(2009) Diaz, G.A., et al. Genomics 54(1):13-18(1998) Parvari, R., et al. Am. J. Hum. Genet. 63(1):163-169(1998)
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