[H05] HRP-conjugated Sheep Anti-Human Apolipoprotein AII12H-S1a
|Concentration:||1 mg/ml (OD 1.35 / 280 nm)|
|Antigen:||Human Apolipoprotein AII|
|Form:||Freeze dried powder|
|Buffer:||50 mM PBS, 0.1 M NaCl, and 0.01% Thiomersal, pH 7.4.|
|Specificity||Specifically binds to human apo AII. Dilution for immunoblot and ELISA range: 1,000 to 8,000.|
|Use:||The antibody can be used for detection of apo AII in plasma and lipoproteins, immunoassays, immunoblots, enzyme conjugation, or biotinylation.|
|Storage:||-20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.|
|Form:||Freeze dried powder|
|Stabilizer:||10 mg / ml Bovine Serum Albumin.|
Freeze-dried product should be stored refrigerated until opened. After opening, restore to suggested ml volume with distilled water. If it is not completely clear after standing for 1-2 hours at room temperature, centrifuge the product. It is stable for several weeks at 4°C as an undiluted liquid. Do not use for more than one day after dilution. For extended storage after reconstitution, we suggest aliquot to avoid repeated freezing and thawing; or the addition of an equal volume of glycerol to make a final glycerol concentration of 50%, followed by storage at -20°C. The concentration of protein and buffer salts will decrease to one-half of the original after the addition of glycerol.
*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.
Apo AII comprises 25% of HDL. It exists in human plasma as a dimer of 2 identical chains of 77 amino acid residues, joined by disulfide. The molecular weight is reported to be 8.7 kDa for a single chain (Brewer et al., 1972).
Studies on mouse reported that apo AII may be proatherogenic (Warden et al., 1993); however, case-control study in the large European Prospective Investigation demonstrated that plasma Apo AII concentrations were strongly inversely correlated with CHD events (Birjmohun et al., 2007).
Birjmohun, R. S., G. M. Dallinga-Thie, J. A. Kuivenhoven, E. S.g. Stroes, J. D. Otvos, N. J. Wareham, R. Luben, J. J.p. Kastelein, K.-T. Khaw, and S. M. Boekholdt. "Apolipoprotein A-II Is Inversely Associated With Risk of Future Coronary Artery Disease." Circulation 116 (2007): 2029-035.
Brewer, H. B., S. E. Lux, R. Ronan, and K. M. John. "Amino Acid Sequence of Human ApoLp-Gln-II (apoA-II), an Apolipoprotein Isolated from the High-Density Lipoprotein Complex." Proceedings of the National Academy of Sciences 69.5 (1972): 1304-308.
Warden, C., C. Hedrick, J. Qiao, L. Castellani, and A. Lusis. "Atherosclerosis in Transgenic Mice Overexpressing Apolipoprotein A-II." Science 261 (1993): 469-72.
|[H04][H05]||2009||Gillard, Baiba K.; Lin, Hu-Yu Alice; Massey, John B.; Pownall, Henry J. (2009): Apolipoproteins A-I, A-II and E are independently distributed among intracellular and newly secreted HDL of human hepatoma cells. In Biochimica et Biophysica Acta 1791 (12), pp. 1125–1132. DOI: 10.1016/j.bbalip.2009.07.004.|
|[H04][H05]||2009||Rosales, Corina; Gillard, Baiba K.; Courtney, Harry S.; Blanco-Vaca, Francisco; Pownall, Henry J. (2009): Apolipoprotein Modulation of Streptococcal Serum Opacity Factor Activity against Human Plasma High-Density Lipoproteins. In Biochemistry 48 (33), pp. 8070–8076. DOI: 10.1021/bi901087z.|