|Application ||WB, IHC-P|
|Dilution||IHC-P (5 µg/ml), WB (4 µg/ml),|
|Other Names||Hamartin, Tuberous sclerosis 1 protein, TSC1, KIAA0243, TSC|
|Target/Specificity||15 amino acid peptide from the carboxy terminus of human TSC1|
|Reconstitution & Storage||Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted.|
|Precautions||Hamartin / TSC1 Antibody (C-Terminus) is for research use only and 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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In complex with TSC2, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Seems not to be required for TSC2 GAP activity towards RHEB. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling.
van Slegtenhorst M.A.,et al.Science 277:805-808(1997).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Humphray S.J.,et al.Nature 429:369-374(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Nagase T.,et al.DNA Res. 3:321-329(1996).
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