A portion of amino acids 399-427 from the human protein was used as the immunogen for this SREBP2 antibody.
SREBPs, including SREBP-1a, SREBP-1c, and SREBP-2, constitute a family of basic helix-loop-helix (bHLH) transcription factors that play a critical role in lipid homeostasis by regulating genes involved in cholesterol and fatty acid metabolism. Each SREBP consists of three domains, including an amino-terminal transcription factor domain of ~480 amino acids, a middle hydrophobic region of ~80 amino acids containing two hydrophobic transmembrane segments, and a carboxy-terminal regulatory domain of ~590 amino acids. SREBP-2 regulates cholesterol synthesis by activating the transcription of genes for HMG-CoA reductase and other enzymes of the cholesterol synthetic pathway. SREBP-2 is ubiquitously detected in various tissues. Under basal conditions SREBP is bound to ER membranes as a glycosylated precursor protein. Upon cholesterol depletion, the protein is cleaved to its active forms (about 50-68 kDa) and translocated into the nucleus to stimulate transcription of genes involved in the uptake and synthesis of cholesterol.
