[S11] Goat Anti-Human Apolipoprotein CII Antiserum

Importance

Apo CII contains 78 amino acid residues. The m.w. is 8.5 kDa (Jackson et al., 1977).

The lipid-binding domain of Apo CII is localized to a region in the N-terminal with a strongly amphipathic nature (Macphee et al., 1999). Apo CII is also one of the key components of the metabolism of total triacylglycerol-rich lipoproteins by activating lipoprotein lipase that hydrolyzes fatty acids from triacylglycerols in chylomicrons (Kei et al., 2012).

Jackson, R. L., h. N. Baker, E. B. Gilliam, and A. M. Jr. Gotto. “Primary structure of very low density apolipoprotein C-II of human plasma.” Proc Natl. Acad. Sci. USA 74.5 (1977): 1942-5.

Kei, Anastazia A., Theodosios D. Filippatos, Vasilios Tsimihodimos, and Moses S. Elisaf. "A Review of the Role of Apolipoprotein C-II in Lipoprotein Metabolism and Cardiovascular Disease." Metabolism 61.7 (2012): 906-21.

Macphee, Cait E., Geoffrey J. Howlett, William H. Sawyer, and Andrew H. A. Clayton. "Helix−Helix Association of a Lipid-Bound Amphipathic α-Helix Derived from Apolipoprotein C-II." Biochemistry 38.33 (1999): 10878-0884.