Host Species:	Goat
Concentration:	1 mg/ml (OD 1.35 / 280 nm)
Antigen:	Human Apolipoprotein CI
Purification:	Affinity purified
Buffer:	75 mM Sodium Phosphate, 75 mM NaCl, 0.5 mM EDTA, 0.02% NaN3, pH 7.2
Specificity	Specifically binds to human apo CI. Dilution for immunoblot and ELISA range: 1,000 to 20,000.
Use:	The antibody can be used for detection of apo CI 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.

 

*These products are for research or manufacturing use only, not for use in human therapeutic or diagnostic applications.

 

Importance

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.

 

Citations

 

[A08][A09]	2017	Bus, Pascal; Pierneef, Louise; Bor, Rosalie; Wolterbeek, Ron; van Es, Leendert A.; Rensen, Patrick Cn et al. (2017): Apolipoprotein C-I plays a role in the pathogenesis of glomerulosclerosis. In J. Pathol 241 (5), pp. 589–599. DOI: 10.1002/path.4859.
[A08][A09]	2017	Wassef, Hanny; Bissonnette, Simon; Dufour, Robert; Davignon, Jean; Faraj, May (2017): Enrichment of Triglyceride-Rich Lipoproteins with Apolipoprotein C-I Is Positively Associated with Their Delayed Plasma Clearance Independently of Other Transferable Apolipoproteins in Postmenopausal Overweight and Obese Women. In J. Nutr. 147 (5), pp. 754–762. DOI: 10.3945/jn.116.242750.
[A08][A09]	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.
[A08][A09]	2015	Yassine, Hussein N.; Trenchevska, Olgica; Ramrakhiani, Ambika; Parekh, Aarushi; Koska, Juraj; Walker, Ryan W. et al. (2015): The Association of Human Apolipoprotein C-III Sialylation Proteoforms with Plasma Triglycerides. In PLoS ONE 10 (12), e0144138. DOI: 10.1371/journal.pone.0144138.
[A08][A09]	2014	Zvintzou, Evangelia; Skroubis, George; Chroni, Angelika; Petropoulou, Peristera-Ioanna; Gkolfinopoulou, Christina; Sakellaropoulos, George et al. (2014): Effects of bariatric surgery on HDL structure and functionality: results from a prospective trial. In Journal of Clinical Lipidology 8 (4), pp. 408–417. DOI: 10.1016/j.jacl.2014.05.001.
[A08][A09]	2013	Takinami, Yoshihiko; Yoshimatsu, Shinya; Uchiumi, Takaoki; Toyosaki-Maeda, Tomoko; Morita, Atsushi; Ishihara, Takeshi et al. (2013): Identification of Potential Prognostic Markers for Knee Osteoarthritis by Serum Proteomic Analysis. In BiomarkInsights 8, BMI.S11966. DOI: 10.4137/BMI.S11966.
[A08][A09]	2012	Cudaback, Eiron; Li, Xianwu; Yang, Yue; Yoo, Thomas; Montine, Kathleen S.; Craft, Suzanne et al. (2012): Apolipoprotein C-I is an APOE genotype-dependent suppressor of glial activation. In Journal of Neuroinflammation 9, p. 192. DOI: 10.1186/1742-2094-9-192.
[A08][A09]	2012	Wassef, Hanny; Salem, Huda; Bissonnette, Simon; Baass, Alexis; Dufour, Robert; Davignon, Jean; Faraj, May (2012): White Adipose Tissue Apolipoprotein C-I Secretion in Relation to Delayed Plasma Clearance of Dietary Fat in Humans. In Arterioscler Thromb Vasc Biol. 32 (11), pp. 2785–2793. DOI: 10.1161/ATVBAHA.112.300306.
[A08][A09]	2010	Lahiry, Piya; Cao, Henian; Ban, Matthew R.; Pollex, Rebecca L.; Mamakeesick, Mary; Zinman, Bernard et al. (2010): APOC1 T45S polymorphism is associated with reduced obesity indices and lower plasma concentrations of leptin and apolipoprotein C-I in aboriginal Canadians. In J. Lipid Res. 51 (4), pp. 843–848. DOI: 10.1194/jlr.P002014.
[A08][A09]	2009	Barlage, Stefan; Gnewuch, Carsten; Liebisch, Gerhard; Wolf, Zsuzsanna; Audebert, Franz-Xaver; Glück, Thomas et al. (2009): Changes in HDL-associated apolipoproteins relate to mortality in human sepsis and correlate to monocyte and platelet activation. In Intensive Care Medicine 35 (11), pp. 1877–1885. DOI: 10.1007/s00134-009-1609-y.
[A08][A09]	2008	Abildayeva, Karlygash; Berbée, Jimmy F. P.; Blokland, Arjan; Jansen, Paula J.; Hoek, Frans J.; Meijer, Onno et al. (2008): Human apolipoprotein C-I expression in mice impairs learning and memory functions. In J. Lipid Res. 49 (4), pp. 856–869. DOI: 10.1194/jlr.M700518-JLR200.
[A08][A09]	2008	Berbée, Jimmy F. P.; Mooijaart, Simon P.; Craen, Anton J. M. de; Havekes, Louis M.; van Heemst, Diana; Rensen, Patrick C. N.; Westendorp, Rudi G. J. (2008): Plasma apolipoprotein CI protects against mortality from infection in old age. In The Journals of Gerontology. Series A, Biological sciences and medical sciences 63 (2), pp. 122–126. DOI: 10.1093/gerona/63.2.122.
[A08][A09]	2008	Christoffersen, Christina; Jauhiainen, Matti; Moser, Markus; Porse, Bo; Ehnholm, Christian; Boesl, Michael et al. (2008): Effect of Apolipoprotein M on High Density Lipoprotein Metabolism and Atherosclerosis in Low Density Lipoprotein Receptor Knock-out Mice. In J. Biol. Chem. 283 (4), pp. 1839–1847. DOI: 10.1074/jbc.M704576200.
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[A08][A09]	2007	Westerterp, Marit; Berbée, Jimmy F. P.; Delsing, Dianne J. M.; Jong, Miek C.; Gijbels, Marion J. J.; Dahlmans, Vivian E. H. et al. (2007): Apolipoprotein C-I binds free fatty acids and reduces their intracellular esterification. In J. Lipid Res. 48 (6), pp. 1353–1361. DOI: 10.1194/jlr.M700024-JLR200.
[A08][A09]	2006	Göbel, Thomas; Vorderwülbecke, Sonja; Hauck, Katarzyna; Fey, Holger; Häussinger, Dieter; Erhardt, Andreas (2006): New multi protein patterns differentiate liver fibrosis stages and hepatocellular carcinoma in chronic hepatitis C serum samples. In World Journal of Gastroenterology 12 (47), pp. 7604–7612. DOI: 10.3748/wjg.v12.i47.7604.
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[A08][A09]	2006	Westerterp, Marit; Haan, Willeke de; Berbée, Jimmy F. P.; Havekes, Louis M.; Rensen, Patrick C. N. (2006): Endogenous apoC-I increases hyperlipidemia in apoE-knockout mice by stimulating VLDL production and inhibiting LPL. In J. Lipid Res. 47 (6), pp. 1203–1211. DOI: 10.1194/jlr.M500434-JLR200.
[A08][A09]	2005	Berbée, Jimmy F. P.; van der Hoogt, Caroline C.; Sundararaman, Deepa; Havekes, Louis M.; Rensen, Patrick C. N. (2005): Severe hypertriglyceridemia in human APOC1 transgenic mice is caused by apoC-I-induced inhibition of LPL. In J. Lipid Res. 46 (2), pp. 297–306. DOI: 10.1194/jlr.M400301-JLR200.
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academy biomed[A05]绵羊抗人类载脂蛋白AII多克隆抗体12A-S1a学院生物医学公司$ 155.00$ 155.00目录号数量1寄主物种： 羊浓度： 1毫克/毫升（OD 1.35 / 280 nm）抗原： 人类载脂蛋白AII纯化： 亲和纯化缓冲： 75 mM磷酸钠，75 mM NaCl，0.5 mM EDTA，0.02％NaN3，pH 7.2特异性 与人载脂蛋白AII特异性结合。免疫印迹和ELISA的稀释范围：1,000至80,000。用： 该抗体可用于检测血浆和脂蛋白中的载脂蛋白AII，免疫测定，免疫印迹，酶结合或生物素化。存储： -20°C长期保存，4°C短期保存。等分试样，以避免反复冻结和解冻。 *这些产品仅用于研究或制造用途，不能用于人体治疗或诊断应用。 重要性Apo AII占HDL的25％。它在人血浆中以77条氨基酸残基的2条相同链的二聚体形式存在，并通过二硫键连接。据报道，单链的分子量为8.7kDa（Brewer等，1972）。对小鼠的研究报道，apoAII可能具有促动脉粥样硬化作用（Warden等，1993）。然而，一项大型的欧洲前瞻性研究中的病例对照研究表明，血浆Apo AII浓度与冠心病事件密切相关（Birjmohun等，2007）。Birjmohun，RS，GM Dallinga-Thie，JA Kuivenhoven，ESg Stroes，JD Otvos，NJ Wareham，R.Luben，JJp Kastelein，K.-T. Khaw和SM Boekholdt。“载脂蛋白A-II与未来冠状动脉疾病的风险成反比。” 循环116（2007）：2029-035。Brewer，HB，SE Lux，R.Ronan和KM John。“人ApoLp-Gln-II（apoA-II），一种从高密度脂蛋白复合物中分离的载脂蛋白的氨基酸序列。” 美国国家科学院院刊69.5（1972）：1304-308。Warden，C.，C.Hedrick，J.Qiao，L.Castellani和A.Lusis。“过表达载脂蛋白A-II的转基因小鼠中的动脉粥样硬化。” 科学261（1993）：469-72。