Reagent | Apolipoprotein C-II (Apo C-II)
In Association with Hypertriglyceridemia
Benefits of the Randox Apo C-II Assay
The immunoturbidimetric method limits interference from Bilirubin, Haemoglobin, Intralipid® and Triglycerides, producing more accurate results.
A correlation coefficient of r=1.00 was displayed when the Randox apo C-II assay was compared to commercially available methods.
Excellent measuring range
The Randox apo C-II assay has a measuring range of 1.48 – 9.70mg/dl for the comfortable detection of clinically important results.
The Randox apo C-II assay is available in a liquid ready-to-use format for convenience and ease-of-use.
Dedicated calibrator and controls available
Randox offer dedicated apolipoprotein calibrator and controls for a complete testing package.
Applications available detailing instrument-specific settings for the convenient use of the Randox apo C-II assay on a variety of clinical chemistry analysers.
Apo C – II is a 79-amino acid protein synthesised in the liver and is the co-factor for lipid transport in the bloodstream 1. Apo C – II is a surface constituent of lipoproteins and the C – terminal helix activates lipoprotein lipase (LPL) 2. The active peptide of apo C – II corresponds to residues 44 – 79 and has been identified to reverse the symptoms of genetic apo C – II deficiency. Moreover, LPL is also a key enzyme in the regulation of triglyceride levels 3.
Both an excess and deficiency of apo C – II is associated with hypertriglyceridemia and reduced LPL activity. Elevated levels of apo C-II is associated with excess triglyceride – rich particles and altercations in the distribution of HDL particles, increasing the risk of CVD 4. Whilst extremely rare, a deficiency in apo C-II results in excess fasting hypertriglyceridemia and chylomicronemia. Hypertriglyceridemia can cause eruptive xanthomas, pancreatitis, hepatosplenomegaly and lipemia retinalis. Biologically and clinically, apo C – II deficiency closely mimics LPL deficiency. Synonyms for apo C-II deficiency include: C – II an apolipoproteinemia and hyperlipoproteinemia type Ib 5.
 Zdunek J, Martinez GV, Schleucher J, Lycksell PO, Yin Y, et al. Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for Increased Mobility of the Helix Involved in the Activation of Lipoprotein Lipase. Biochemistry 2003; 42(7): 1872-1889.
 Storjohann R, Rozek A, Sparrow JT, Cushley RJ. Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine. Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids 2000; 1486(2-3): 253-264.
 Kei AA, Filippatos TD, Tsimihodimos V, Elisaf MS. A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease. Metabolism: Clinical and Experimental 2012; 61(7): 906-921.
 Meyers NL, Larsson M, Olivecrona G, Small DM. A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II*. Journal of Biological Chemistry 2015; 290(29): 18029-18044.
 Hoffmann MM, März W. Apo C-II Deficiency. Encyclopedia of Molecular Mechanisms of Disease 2009; 132(133): https://link.springer.com/referenceworkentry/10.1007%2F978-3-540-29676-8_137 (accessed 6 November 2019).