PPARA
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
The purified recombinant protein has an amino terminal polyhistidine tag and is greater than 95 % homogeneous and contains no detectable protease, DNase and RNase activity.
PI
Recombinant PPARα is isolated from an E. coli strain that carries the coding sequence of the human PPARα under the control of a T7 promoter (accession number NM 005036). The purified recombinant protein has an amino terminal polyhistidine tag and is greater than 95 % homogeneous and contains no detectable protease, DNase and RNase activity.
Pureté
The purified recombinant protein has an amino terminal polyhistidine tag and is greater than 95 % homogeneous and contains no detectable protease, DNase and RNase activity.
Crystallography grade
PPARA
Origine: Humain
Hôte: Tobacco (Nicotiana tabacum)
Recombinant
>80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA
Indications d'application
Recombinant PPARα is suitable for DNA and protein-protein interaction assays. 20 ng is sufficient for gelshift assays and 100 ng is sufficient for protein-protein interaction studies. The molecular weight of the protein is ~52 kDa. NOTE: The presence of Poly [d(I-C)] in buffers may affect protein functionality and should be avoided.
Peroxisome Proliferator-Activated Receptors (PPARs) are nuclear receptors involved in lipid transport and metabolism. As such, their roles in chronic diseases such as diabetes, obesity, atherosclerosis and cancer are heavily investigated. Transcriptional activity of PPARs is regulated by fatty acid binding. Three PPAR isotypes have been identified: α, δ and Y. PPARγ stimulates lipolysis of circulating triglycerides and the subsequent uptake of fatty acids into adipose cells. PPARs bind to peroxisome proliferator response elements (PPREs) as heterodimers with the retinoid X receptor (RXR).