Anti-Hamartin TSC1 Antibody

Primary Antibodies

Boster Bio Anti-Hamartin TSC1 Antibody (Catalog # A00365). Tested in ELISA, WB, ICC, IF applications. This antibody reacts with Human, Mouse, Rat.

Tuberous sclerosis complex (TSC) is an autosomal dominant tumor syndrome caused by mutations in either of the TSC1 or TSC2 tumor suppressor genes. The products of these genes form a protein complex that indirectly decreases the signaling of the mammalian Target of Rapamycin (TOR), an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. TOR activity is stimulated by Rheb, a member of the Ras superfamily of G-proteins, when the GTP/GDP ratio bound to Rheb is high. Immunoprecipitated TSC1/TSC2 has been shown to stimulate Rheb GTPase activity in vitro, suggesting that the TSC1/TSC2 decreases the ability of Rheb to stimulate TOR activity. This is supported by experiments showing overexpression of TSC1 and TSC2 results in a significant decrease in the GTP/GDP ratio bound to Rheb and the inhibition of cell growth. A shorter 40 kDa isoform of TSC1 has been shown to exist but its function is unknown.

Polyclonal

TSC1 Antibody is supplied in PBS containing 0.02% sodium azide.

TSC1 antibody was raised against a 15 amino acid synthetic peptide from the middle region of human TSC1. The immunogen is located within amino acids 220 - 270 of TSC1.

TSC1 Antibody is affinity chromatography purified via peptide column.

Tuberous sclerosis 1

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).

Highly expressed in skeletal muscle, followed
by heart, brain, placenta, pancreas, lung, liver and kidney. Also
expressed in embryonic kidney cells.