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Phospho-TSC1(Y297) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q92574
Other Accession NP_000359.1
Additional Information
Gene ID 7248
Other Names Hamartin, Tuberous sclerosis 1 protein, TSC1, KIAA0243, TSC
Target/Specificity The synthetic peptide sequence is selected from aa 290-304 of HUMAN TSC1
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name TSC1 {ECO:0000303|PubMed:9242607, ECO:0000312|HGNC:HGNC:12362}
Function Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12906785, PubMed:12271141, PubMed:28215400, PubMed:15340059, PubMed:24529379). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400). The TSC- TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self- aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also 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 Lysosome membrane; Peripheral membrane protein. Cytoplasm, cytosol Note=Recruited to lysosomal membranes in a RHEB-dependent process in absence of nutrients (PubMed:24529379). In response to nutrients, the complex dissociates from lysosomal membranes and relocalizes to the cytosol (PubMed:24529379).
Tissue Location Highly expressed in skeletal muscle, followed by heart, brain, placenta, pancreas, lung, liver and kidney (PubMed:9242607). Also expressed in embryonic kidney cells (PubMed:9242607).
Research Areas
Citations (0)
citation

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Background

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.

References

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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$ 277.78
Cat# BP3895a
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