SIRT1 Rabbit Recombinant mAb

SIRT1 Antibody detects endogenous levels of total SIRT1.

The sirtuin family represents a unique set of enzymes that respond directly to the energy state of the cell in regulating its intrinsic enzymatic functions. SIRT1 is most conserved to its ancestral yeast Sir2, in both protein structure and function, and acts solely as a deacetylase, similar to SIRT2, while SIRT4 and SIRT6 do not have strong deacetylase activity. SIRT1 has been comprehensively studied in higher organisms, and the focus has been on the substrates of SIRT1 deacetylation. Besides the ability of SIRT1 to deacetylate H1, H3, and H4, SIRT1 is also found to deacetylate a critical master regulator in p53, suggesting a role in tumor suppression. Since the initial discovery of SIRT1 deacetylation of p53, many diverse protein substrates have been identified, including FOXO3a, PGC-1α, and PPARγ. These SIRT1 substrates have linked the metabolic state of the cell to various diseases, including cancer, diabetes, and neurodegenerative diseases.