SIRT1 (1F3) Antibody

SIRT1 (NAD-dependent deacetylase sirtuin-1) has been found to associate with the tumor suppressor protein p53. SIRT1 binds and deacetylates p53 with specificity for its C-terminal Lys382 residue in response to the upregulation of promyelocytic leukemia protein (PML) nuclear bodies or oncogenic Ras. The deacetylation of p53 SIRT1 has been shown to negatively regulate p53-mediated transcription,Porcinereventing cellular senescence and apoptosis induced by DNA damage and stress. SIRT1 has the closest homology to the yeast Sir2p and is widely e, Xenopus/Amphibian,pressed in fetal and adult tissues, with high e, Xenopus/Amphibian,pression in heart, brain, skeletal muscle and low e, Xenopus/Amphibian,pression in lung and placenta. SIRT1 regulates the p53-dependent DNA damage response pathway by binding to and deacetylating p53, specifically at Lysine 382.