SREBP-2 Blocking Peptide

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • signaling signalling controls peptides proteins diseases antibodies antisera antiserum WB western blots blotting ICC immunocytochemistry atherosclerosis 1a 1c basic helix-loop-helix bHLH transcription factors lipids homeostasis regulating genes cholesterols fatty acids metabolisms domains amino-terminals hydrophobic regions transmembranes segments carboxy regluates synthesis genes HMG-CoA reductases enzymes synthetics pathways tissues basal ER endoplasmic reticulum membranes glycosylateds nucleus cells livers brown fats testis HepG2 human fibroblasts
• Product Overview:
  To be used in conjunction with Cayman’s SREBP-2 polyclonal antibody (Catalog No. 10007663) to block protein-antibody complex formation during immunochemical analysis of SREBP-2 protein. · 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.{13853} 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.{13853} SREBP-2 regulates cholesterol synthesis by activating the transcription of genes for HMG-CoA reductase and other enzymes of the cholesterol synthetic pathway.{13851} SREBP-2 is ubiquitously detected in various tissues.{12882} 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.{13148} Cayman’s SREBP-2 polyclonal antibody detects both precursor and active forms of the protein in tissues and cells such as liver, brown fat, testis, HepG2 cells, and human fibroblast. The apparent molecular weight on SDS-PAGE may be higher than the calculated molecular weight (about 126 kDa) due to glycosylation of the protein.{13852}