Anti-Human Hamartin Antibody Pair

Product Description: TSC complex subunit 1 (TSC1), also known as hamartin, is a tumor suppressor protein that plays a crucial role in regulating cell growth and proliferation. TSC1 forms a multi-protein complex with TSC2 (tuberin) and TBC1D7, creating an elongated, scorpion-like structure where TSC1's coiled-coil backbone runs along the TSC2 dimer, breaking its symmetry and facilitating complex assembly. This complex acts as a GTPase-activating protein (GAP) for the small GTPase Rheb, thereby negatively regulating the mammalian target of rapamycin complex 1 (mTORC1), a central controller of anabolic cell growth. TSC1 also functions as a co-chaperone for Hsp90, inhibiting its ATPase activity and stabilizing client proteins, including TSC2, by preventing their ubiquitination and proteasomal degradation. Mutations in TSC1 disrupt these regulatory functions, leading to diseases such as tuberous sclerosis complex-a genetic disorder characterized by benign tumor growth in multiple organs-and lymphangioleiomyomatosis. Protein 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) [The Uniprot Consortium]