| Host: |
Rabbit |
| Applications: |
WB/IHC/IF/ELISA |
| Reactivity: |
Human/Mouse/Rat |
| Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Rabbit polyclonal antibody anti-Phospho-Tuberin-Tyr1571 (1537-1586 aa) is suitable for use in Western Blot, Immunohistochemistry, Immunofluorescence and ELISA research applications. |
| Clonality: |
Polyclonal |
| Conjugation: |
Unconjugated |
| Isotype: |
IgG |
| Formulation: |
Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide. |
| Purification: |
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. |
| Concentration: |
1 mg/mL |
| Dilution Range: |
WB 1:500-1:2000IHC 1:100-1:300ELISA 1:5000IF 1:50-200 |
| Storage Instruction: |
Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
| Gene Symbol: |
TSC2 |
| Gene ID: |
7249 |
| Uniprot ID: |
TSC2_HUMAN |
| Immunogen Region: |
1537-1586 aa |
| Specificity: |
Phospho-Tuberin (Y1571) Polyclonal Antibody detects endogenous levels of Tuberin protein only when phosphorylated at Y1571. |
| Immunogen: |
The antiserum was produced against synthesized peptide derived from the human TSC2 around the phosphorylation site of Tyr1571 at the amino acid range 1537-1586 |
| Post Translational Modifications | Phosphorylation at Ser-939 and Thr-1462 by PKB/AKT1 in response to insulin signaling and growth factor stimulation inhibits the ability of the TSC-TBC complex to suppress mTORC1 signaling: phosphorylation promotes dissociation of the TSC-TBC complex from lysosomal membranes, leading to activation of mTORC1 by RHEB. Phosphorylation at Ser-1387, Ser-1418 or Ser-1420 does not affect interaction with TSC1. Phosphorylation by AMPK activates it and leads to negative regulation of the mTORC1 complex. Phosphorylated at Ser-1798 by RPS6KA1.phosphorylation inhibits TSC2 ability to suppress mTORC1 signaling. Phosphorylated by DAPK1. Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase complex, leading to its subsequent degradation. Ubiquitinated by MYCBP2 independently of its phosphorylation status leading to subsequent degradation.association with TSC1 protects from ubiquitination. |
| Function | 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. Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. 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. The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1. Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling. Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5. |
| Protein Name | TuberinTuberous Sclerosis 2 Protein |
| Database Links | Reactome: R-HSA-1632852Reactome: R-HSA-165181Reactome: R-HSA-198323Reactome: R-HSA-380972Reactome: R-HSA-5628897Reactome: R-HSA-5674400Reactome: R-HSA-8854214 |
| Cellular Localisation | Lysosome MembranePeripheral Membrane ProteinCytoplasmCytosolRecruited To Lysosomal Membranes In A Rheb-Dependent Process In Absence Of NutrientsIn Response To Insulin Signaling And Phosphorylation By Pkb/Akt1The Complex Dissociates From Lysosomal Membranes And Relocalizes To The Cytosol |
| Alternative Antibody Names | Anti-Tuberin antibodyAnti-Tuberous Sclerosis 2 Protein antibodyAnti-TSC2 antibodyAnti-TSC4 antibody |
Information sourced from Uniprot.org
12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance
