SIRT1 HUMAN RECOMBINANT EXPRESSED IN E. COLI N-TERMINAL HISTIDINE TAGGED >=90% (SDS-PAGE) BUFFERED AQUEOUS GLYCEROL SOLUTION

General description

SIRT1 (sirtuin 1) belongs to the silent information regulator (SIR) family and is a class of HDAC (histone deacetylase). It is expressed in various tissues including brain, liver, pancreas, adipose tissue, and skeletal muscle. SIRT1 is also known as the longevity gene.

Application

Human SIRT1 (sirtuin1) has been used in in vitro acetylation and deacetylation assays. It has also been used to study its effects on homeostasis of human nucleus pulposus cells.

Biochem/physiol Actions

SIRT1 (sirtuin 1) functions as a regulator of various metabolic pathways, and influences the pathophysiology of several metabolic diseases. It is a regulator of protein deacetylation, and is a candidate therapeutic target in non-alcoholic fatty liver disease (NAFLD), amyotrophic lateral sclerosis (ALS), kidney disease, and pulmonary disease. It also participates in tumorigenesis, and whether it functions as an oncogene or as a tumor suppressor depends upon the tumor type. In pancreatic ductal adenocarcinoma (PDAC) its elevated expression is linked with poor prognosis, and in non-small-cell lung cancer (NSCLC) it suppresses the expression of tumor suppressor p27. It is also thought to function as a suppressor of cardiovascular disorders, such as myocardial infarction, or neurodegenerative diseases, such as Alzheimer′s disease (AD) or Parkinson′s disorder (PD).

Sirtuins are a family of NAD⁺ dependent deacetylases that remove an acetyl group from the e-amino group of lysine residues. The proteins within this family are named after the first protein discovered, from yeast, called Sir2 (Silent Information Regulator 2). The proteins are conserved from bacteria to higher eukaryotes. In humans, there are seven Sir2 family members (SIRT1 to SITR7). SIRT1 plays a pivotal role in the regulation of cellular differentiation, metabolism, cell cycle, apoptosis and regulation of p53. Several targets for SIRT1 were identified among them Lys³⁸² of p53. Using RNA interference, additional targets were identified. It was demonstrated that reduced levels of human SIRT1 led to increased acetylation of Histone H4-Lys¹⁶, H4-Lys²⁰, and Histone H3-Lys⁹ as well as histone H1-Lys²⁶.

Physical form

Solution containing 50 mM Tris, pH 7.4, 100 mM NaCl, 1 mM DTT, protease inhibitors (Product code P8340) 1:200, and 10% glycerol (w/v).