Phospho-TSC1(T390) Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| DB, E |
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Primary Accession | Q92574 |
Other Accession | NP_000359.1 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 129767 Da |
Gene ID | 7248 |
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Other Names | Hamartin, Tuberous sclerosis 1 protein, TSC1, KIAA0243, TSC |
Target/Specificity | This TSC1 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding T390 of human TSC1. |
Dilution | DB~~1:500 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Phospho-TSC1(T390) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TSC1 {ECO:0000303|PubMed:9242607, ECO:0000312|HGNC:HGNC:12362} |
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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:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). 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, PubMed:33215753). 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). |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
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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