[H07] HRP-conjugated Goat Anti-Human Apolipoprotein CI - AcademyBiomed

[H07] HRP-conjugated Goat Anti-Human Apolipoprotein CI


Academy Bio-Medical Company, Inc.

  • $331.00

Host Species: Goat
Concentration: 1 mg/ml (OD 1.35 / 280 nm)
Antigen: Human Apolipoprotein CI
Purification: Affinity purified
Buffer: 50 mM PBS, 0.1 M NaCl, and 0.01% Thiomersal, pH 7.4.
Specificity Specifically binds to human apo CI. Dilution for immunoblot and ELISA range: 1,000 to 4,000.
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.
Form: Freeze dried powder
Stabilizer: 10 mg / ml Bovine Serum Albumin.


and Storage:

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.



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.



[H07] 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.
[H07] 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.
[H07] 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.
[H07] 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.
[H07] 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.
[H07] 2005 Bouchard, Catherine; Dubuc, Geneviève; Davignon, Jean; Bernier, Lise; Cohn, Jeffrey S. (2005): Post-transcriptional regulation of apoC-I synthesis and secretion in human HepG2 cells. In Atherosclerosis 178 (2), pp. 257–264. DOI: 10.1016/j.atherosclerosis.2004.09.014.
[H07] 2004 Wassef, Hanny; Bernier, Lise; Davignon, Jean; Cohn, Jeffrey S. (2004): Synthesis and secretion of apoC-I and apoE during maturation of human SW872 liposarcoma cells. In J. Nutr. 134 (11), pp. 2935–2941. DOI: 10.1093/jn/134.11.2935.

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