|Other Names||Hamartin, Tuberous sclerosis 1 protein, TSC1, KIAA0243, TSC|
|Target/Specificity||The synthetic peptide sequence is selected from aa 592-605 of HUMAN TSC1|
|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||In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling (PubMed:12271141, PubMed:28215400). Seems not to be required for TSC2 GAP activity towards RHEB (PubMed:15340059). Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling (By similarity). Acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155).|
|Cellular Location||Cytoplasm. Membrane; Peripheral membrane protein. Note=At steady state found in association with membranes.|
|Tissue Location||Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney. Also expressed in embryonic kidney cells|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a growth inhibitory protein thought to play a role in the stabilization of tuberin. Mutations in this gene have been associated with tuberous sclerosis. Alternative splicing results in multiple transcript variants.
Hoogeveen-Westerveld, M., et al. Biochim. Biophys. Acta 1802(9):774-781(2010)
Mehta, M.S., et al. Breast Cancer Res. Treat. (2010) In press :
Mieulet, V., et al. Trends Mol Med 16(7):329-335(2010)
Liu, C.Y., et al. Carcinogenesis 31(7):1259-1263(2010)
Guo, L., et al. Acta Biochim. Biophys. Sin. (Shanghai) 42(4):266-273(2010)
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