[P11] Human Apolipoprotein CI (Apo CI)31P-102
|Concentration:||1 mg / ml, determined by the Lowry method|
|Source:||From fresh human plasma that has tested negative for Hepatitis C, HIV-I and HIV-II antibodies as well as Hepatitis surface antigens.|
|Purification:||After series ultracentrifugations, Very Low Density Lipoprotein (VLDL) is isolated from human plasma. Apo CI is purified from delipidated VLDL, followed by gel-filtration and DEAE-Sepharcyl chromatography.|
|Purity:||≥ 98% by SDS-PAGE|
|Buffer:||In 75 mM Sodium Phosphate, 75 m M NaCl, 0.02 % NaN3, 1 mM EDTA, p H 7.4.|
|Storage:||-20°C for long-term storage, 4°C for short- term storage. Aliquot to avoid repeated freezing and thawing.|
*The products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.
ApoCI contains 57 amino acid residues and the m.w. is 6.6 kDa (Jackson et al., 1974).
ApoCI has been found to activate LCAT (Liu and Subbaiah 1993). Apo CI is an inhibitor of lipoprotein binding to the LDL receptor, LDL receptor-related protein, and VLDL receptor. Apo CI is also an inhibitor of the plasma cholesteryl ester transfer protein and of fatty acid uptake into tissues (Shachter, 2001). This inhibition role can potentially regulate several lipase enzymes (Poensgen, 1990, Conde-Knape et al., 2002; Berbee et al., 2005.)
Berbee J.F., C.C. van der Hoogt, D. Sundararaman, L.M. Havekes, and P.C. Rensen. “Severe hypertriglyceridemia in human APOC1 transgenic mice is caused by apoC-I-induced inhibition of LPL.” J. Lipid. Res. 46 (2005) 297-306.
Conde-Knape K., A. Bensadoun, J.H. Sobel. J.S. Cohn, and N.S. Shachter. “Overexpression of apoC-I in apoE-null mice: severe hypertriglyceridemia due to inhibition of hepatic lipase” J. Lipid Res. 43 (2002): 2136-2145.
Jackson R.L., J. T. Sparrow, H. N. Baker, J.D. Morrisett, O. D. Taunton, and A. M. Jr. Gotto. “The primary structure of apolipoprotein-serine.” J. Biol. Chem. 249.16 (1974): 5308-13.
Liu, M. and P.V. Subbaiah. “Activation of plasma lysolecithin acyltransferase reaction by apolipoproteins A-I, C-I and E.” Biochim. Biophys. Acta. 1168 (1993): 144-152.
Poensgen, J., “Apolipoprotein C-1 inhibits the hydrolysis by phospholipase A2 of phospholipids in liposomes and cell membranes” Biochim. Biophys. Acta. 1042 (1990): 188-192.
Shachter, Neil S., “Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism” Current Opinion in Lipidology 12(3): 297-304.
|[P11][P12]||2017||Toth, Christopher A.; Kuklenyik, Zsuzsanna; Jones, Jeffrey I.; Parks, Bryan A.; Gardner, Michael S.; Schieltz, David M. et al. (2017): On-column trypsin digestion coupled with LC-MS/MS for quantification of apolipoproteins. In Journal of proteomics 150, pp. 258–267. DOI: 10.1016/j.jprot.2016.09.011.|
|[P11][P12]||2015||Trenchevska, Olgica; Schaab, Matthew R.; Nelson, Randall W.; Nedelkov, Dobrin (2015): Development of multiplex mass spectrometric immunoassay for detection and quantification of apolipoproteins C-I, C-II, C-III and their proteoforms. In Methods (San Diego, Calif.) 81, pp. 86–92. DOI: 10.1016/j.ymeth.2015.02.020.|
|[P11][P12]||2011||Borges, Chad R.; Oran, Paul E.; Buddi, Sai; Jarvis, Jason W.; Schaab, Matthew R.; Rehder, Douglas S. et al. (2011): Building multidimensional biomarker views of type 2 diabetes on the basis of protein microheterogeneity. In Clinical chemistry 57 (5), pp. 719–728. DOI: 10.1373/clinchem.2010.156976.|
|[P11][P12]||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.|