PPARa Ligand-binding Domain (human, recombinant)

Peroxisome proliferator-activated receptor ? (PPAR?) is a member of the nuclear receptor family of ligand-activated transcription factors that regulates a variety of metabolic functions and inflammation.{49726} It contains an N-terminal domain that is subject to phosphorylation, a DNA-binding domain, and a C-terminal ligand-binding domain.{49727} PPAR? is highly expressed in tissues with high fatty acid oxidation rates, including the liver, heart, skeletal muscle, brown adipose tissue, and kidney, as well as in macrophages and T cells.{49728,49727} It is activated by a variety of endogenous ligands such as fatty acids, eicosanoids, and endocannabinoids, as well as synthetic agents, including fenofibrate (Item No. 10005368) and gemfibrozil (Item No. 14835).{49729} Upon activation, PPAR? heterodimerizes with the retinoid X receptor (RXR) and binds to PPAR response elements in PPAR? target genes, recruiting RNA polymerase II and initiating gene transcription.{49726} PPAR? transcriptionally regulates a variety of genes involved in several cellular processes, including lipid and hormone transport, peroxisomal and mitochondrial ?-oxidation, amino acid metabolism, and inflammation.{49726,49727} Genome-wide deletion of Ppara protects mice from high-fat diet-induced hyperinsulinemia and insulin resistance.{49730} Ppara SNPs have been found in individuals with a variety of cardiovascular conditions, including hypertension, atherosclerosis, coronary artery disease, left ventricular hypertrophy, or myocardial infarction.{49726} Formulations containing PPAR? agonists have been used in the treatment of hyperlipidemia. Cayman's PPAR? Ligand-binding Domain protein can be used for Western blot (WB) applications.