His-tagged full length PPAR beta(cat# p1049-01, 10ug)
His-tagged ligand binding domain of PPAR beta (p1064-01, 10ug)
GST tagged ligand binding domain of PPAR beta (p4035-01, 10ug).
There is evidence that a group of closely related nuclear receptors, called peroxisome proliferator-activated receptors (PPARs), may be involved in chronic diseases such as diabetes, obesity, artherosclerosis and cancer. The PPARs were first cloned as the nuclear receptors that mediate the effects of synthetic compounds called peroxisome proliferators on gene transcription. It soon became clear that eicosanoids and fatty acids can also regulate gene transcription through PPARs. They bind a specific element in the promoter region of target genes only as a heterodimer with the receptor for 9- cis retinoic acid, RXR (retinoid X receptor). Binding of the ligand of either receptor can activate the complex, but binding of both ligands simultaneously is more potent (1). Three PPAR isotypes have been identified: α, β (also called NUC1) and γ. PPARα is expressed most in brown adipose tissue and liver, then kidney, heart and skeletal muscle. PPARβ is found in many tissues but the highest expression is in the gut, kidney and heart. PPARγ is mainly expressed in adipose tissue, and to a lesser extent in colon, the immune system and the retina (2). PPARβ has received little attention, probably because of the lack of a connection with important clinical manifestations. However, recently PPARβ has been linked to colon cancer (3), among other functions. PPAR regulates the expression of acyl-CoA synthetase 2 in the brain, linking PPARβ to basic lipid metabolism (4). Moreover, it probably participates in embryo implantation and decidualization (5).
Recombinant His-tagged PPARβ, His tagged and GST-tagged ligand binding domain of PPAR beta were expressed and purified from E. coli system.
PPARβ has been applied in DNA and protein-protein interactions assays. Purified protein is greater than 95% homogeneous and based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein. 20 units are sufficient for a gel-mobility shift assay and 100 units are sufficient for a protein-protein interaction assay. 0.5 mg/ml (in 1X dilution buffer A) 1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA
References: 1. Desvergene et al., (1999) Endocr. Rev. 20, 649-688 2. Kersten (2000) Nature 405, 421-424 3. He et al., (1999) Cell 99, 335-345 4. Basu-Modak et al., (1999) J. Biol. Chem. 274, 35881-35888 5. Lim et al., (1999) genes Dev. 13, 1561-1574
DISCLAIMER
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
