Human Sirtuin 1/SIRT1 Antibody

SIRT1 (SIR2-like protein 1; also NAD-dependent protein deacetylase sirtuin-1 and hSIR2) is a class I member of the sirtuin family of enzymes. Although its predicted MW is 81 kDa, it runs anomalously at 110-120 kDa in SDS-PAGE. It is a widely expressed nuclear protein that participates in the deacetylation of multiple proteins, including p300, p53, LKB1 and histone H1. Functionally, this has the effect of promoting heterochromatin formation, cell survival and resistance to oxidative stress. Metabolically, SIRT1 induces insulin secretion, inhibits glycolysis and suppresses fatty acid synthesis. Human SIRT1 is 747 amino acids (aa) in length. It possesses two NLS's (aa 32-39 and 223-230), an NES (aa 138-145), and a sertuin-type deacetylase domain (aa 241-495) that contains an NAD and Zn binding motif. There are at least 12 utilized Ser/Thr phosphorylation sites, plus two nitrosylated Cys and one acetylated Ala. There are also four potential isoform variants. One is 95 kDa in size and shows a deletion of aa 454-639, a second is 17 kDa in size and contains a 16 aa substitution for aa 149-747, and a third contains an alternative start site at Met296. SIRT1 is also known to undergo proteolysis by cathepsin B at Val533Ser534, generating a fourth, C-terminally truncated 75 kDa isoform. Full-length SIRT1 is suggested to form trimers, while the 17 kDa isoform appears to form dimers. Over aa 2-747, human and mouse SIRT1 share 86% aa sequence identity.