[G05] Goat Anti-Human Apolipoprotein E Sepharose™ 4B Gel50A-G1 Resin-1ml
|Concentration:||≥ 5 mg/ml|
Polyclonal goat antibody human apo E coupled with CNBr-activated Sepharose 4B™.
75 mM PBS, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, 0.1mM PMSF, pH 7.3.
Specifically binds to human apo E.
Affinity purification column.
2-8ºC store in buffer with 0.5 mM EDTA and 0.02% NaN3, 0.1 mM PMSF. DO NOT FREEZE!
*Sepharose is a trademark of GE Healthcare Life Sciences, Sweden.
** These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.
Apo E contains 299 amino acid residues. It is a 34-37 kDa glycosylated protein (Rall et al., 1983).
Apo E is involved with triglyceride, phospholipid, cholesteryl ester, and cholesterol transport in and out of cells and is a ligand for LDL receptors. Apo E has also been implicated in immune and nerve degeneration. It has been found to suppress lymphocyte proliferation. Late-onset familial and sporadic Alzheimer disease patients have been found to have a higher occurrence of one of the three common Apo E isoforms, Apo E4. The Apo E4 isoform has been detected in senile plaques and neurofibrillary tangles of Alzheimer disease patients. Apo E4 is associated with rapid chylomicron-remnant clearance and increased total cholesterol levels.
Rall, S C, K H Weisgraber, T L Innerarity, T P Bersot, R W Mahley, and C B Blum. "Identification of a New Structural Variant of Human Apolipoprotein E, E2(Lys146 Leads to Gln), in a Type III Hyperlipoproteinemic Subject with the E3/2 Phenotype." Journal of Clinical Investigation 72.4 (1983): 1288-297.
|[G05]||2018||Morton, Allyson M.; Koch, Manja; Mendivil, Carlos O.; Furtado, Jeremy D.; Tjønneland, Anne; Overvad, Kim et al. (2018): Apolipoproteins E and CIII interact to regulate HDL metabolism and coronary heart disease risk. In JCI insight 3 (4). DOI: 10.1172/jci.insight.98045.|
|[G05]||2010||Mendivil, Carlos O.; Zheng, Chunyu; Furtado, Jeremy; Lel, Julian; Sacks, Frank M. (2010): Metabolism of very-low-density lipoprotein and low-density lipoprotein containing apolipoprotein C-III and not other small apolipoproteins. In Arterioscler Thromb Vasc Biol. 30 (2), pp. 239–245. DOI: 10.1161/ATVBAHA.109.197830.|
|[G05]||2010||Zheng, Chunyu; Khoo, Christina; Furtado, Jeremy; Sacks, Frank M. (2010): Apolipoprotein C-III and the Metabolic Basis for Hypertriglyceridemia and the Dense Low-Density Lipoprotein Phenotype. In Circulation 121 (15), pp. 1722–1734. DOI: 10.1161/CIRCULATIONAHA.109.875807.|
|[G05]||2007||Zheng, Chunyu; Khoo, Christina; Ikewaki, Katsunori; Sacks, Frank M. (2007): Rapid turnover of apolipoprotein C-III-containing triglyceride-rich lipoproteins contributing to the formation of LDL subfractions. In J. Lipid Res. 48 (5), pp. 1190–1203. DOI: 10.1194/jlr.P600011-JLR200.|
|[G05]||2006||Kawakami, Akio; Aikawa, Masanori; Libby, Peter; Alcaide, Pilar; Luscinskas, Francis W.; Sacks, Frank M. (2006): Apolipoprotein CIII in apolipoprotein B lipoproteins enhances the adhesion of human monocytic cells to endothelial cells. In Circulation 113 (5), pp. 691–700. DOI: 10.1161/CIRCULATIONAHA.105.591743.|
|[G05]||2005||van den Elzen, Peter; Garg, Salil; León, Luis; Brigl, Manfred; Leadbetter, Elizabeth A.; Gumperz, Jenny E. et al. (2005): Apolipoprotein-mediated pathways of lipid antigen presentation. In Nature 437 (7060), pp. 906–910. DOI: 10.1038/nature04001.|