apoC-III Antibody (8H7): sc-293227

apoC-III Antibody (8H7) is a mouse monoclonal IgG2a kappa light chain antibody that detects apoC-III protein of human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). anti-apoC-III antibody (8H7) is available as the non-conjugated format. apoC-III protein plays a crucial role in lipid metabolism, particularly in regulating triglyceride-rich lipoproteins. apoC-III protein is primarily synthesized in the liver and inhibits lipoprotein lipase and hepatic lipase, enzymes essential for triglyceride breakdown in the bloodstream. By delaying lipoprotein catabolism, apoC-III protein contributes to elevated triglyceride levels, a significant risk factor for cardiovascular diseases. Understanding apoC-III protein function is vital for developing therapeutic strategies aimed at managing dyslipidemia and reducing heart disease risk. apoC-III gene is located on chromosome 11q23, and expression is tightly regulated, making apoC-III protein an important target for research in lipid metabolism and cardiovascular health.

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apoC-III Antibody (8H7) References:

1. Insights into apolipoprotein C metabolism from transgenic and gene-targeted mice.  |  Jong, MC. and Havekes, LM. 2000. Int J Tissue React. 22: 59-66. PMID: 10937355
2. Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene cluster in murine and human macrophages. A critical role for nuclear liver X receptors alpha and beta.  |  Mak, PA., et al. 2002. J Biol Chem. 277: 31900-8. PMID: 12032151
3. Human apoC-IV: isolation, characterization, and immunochemical quantification in plasma and plasma lipoproteins.  |  Kotite, L., et al. 2003. J Lipid Res. 44: 1387-94. PMID: 12700345
4. Targeting ApoC-III to Reduce Coronary Disease Risk.  |  Khetarpal, SA., et al. 2016. Curr Atheroscler Rep. 18: 54. PMID: 27443326
5. Targeting apoC-III and ANGPTL3 in the treatment of hypertriglyceridemia.  |  Nurmohamed, NS., et al. 2020. Expert Rev Cardiovasc Ther. 18: 355-361. PMID: 32511037
6. The Roles of ApoC-III on the Metabolism of Triglyceride-Rich Lipoproteins in Humans.  |  Borén, J., et al. 2020. Front Endocrinol (Lausanne). 11: 474. PMID: 32849270
7. Inhibition of Angiopoietin-Like Protein 3 or 3/8 Complex and ApoC-III in Severe Hypertriglyceridemia.  |  Larouche, M., et al. 2023. Curr Atheroscler Rep. 25: 1101-1111. PMID: 38095804
8. Hypertriglyceridemia associated with deficiency of apolipoprotein C-II.  |  Breckenridge, WC., et al. 1978. N Engl J Med. 298: 1265-73. PMID: 565877
9. Identification and characterization of a new human gene (APOC4) in the apolipoprotein E, C-I, and C-II gene locus.  |  Allan, CM., et al. 1995. Genomics. 28: 291-300. PMID: 8530039
10. Identification, characterization, cloning, and expression of apolipoprotein C-IV, a novel sialoglycoprotein of rabbit plasma lipoproteins.  |  Zhang, LH., et al. 1996. J Biol Chem. 271: 1776-83. PMID: 8576182
11. Expression of a novel human apolipoprotein (apoC-IV) causes hypertriglyceridemia in transgenic mice.  |  Allan, CM. and Taylor, JM. 1996. J Lipid Res. 37: 1510-8. PMID: 8827523
12. In vivo footprinting analysis of the hepatic control region of the human apolipoprotein E/C-I/C-IV/C-II gene locus.  |  Dang, Q. and Taylor, J. 1996. J Biol Chem. 271: 28667-76. PMID: 8910501