Peroxisome proliferator-activated receptor α (PPARα) is a member of the nuclear receptor family of ligand-activated transcription factors that regulates a variety of metabolic functions and inflammation. It contains an N-terminal domain that is subject to phosphorylation, a DNA-binding domain, and a C-terminal ligand-binding domain. PPARα 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. It is activated by a variety of endogenous ligands such as fatty acids, eicosanoids, and endocannabinoids, as well as synthetic agents, including fenofibrate and gemfibrozil . Upon activation, PPARα heterodimerizes with the retinoid X receptor (RXR) and binds to PPAR response elements in PPARα target genes, recruiting RNA polymerase II and initiating gene transcription. PPARα transcriptionally regulates a variety of genes involved in several cellular processes, including lipid and hormone transport, peroxisomal and mitochondrial β-oxidation, amino acid metabolism, and inflammation. Genome-wide deletion of Ppara protects mice from high-fat diet-induced hyperinsulinemia and insulin resistance. 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. Formulations containing PPARα agonists have been used in the treatment of hyperlipidemia. Cayman''s PPARα Ligand-binding Domain protein can be used for Western blot (WB) applications.
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