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Rockland produces highly specific antibodies to apolipoproteins. Apolipoproteins are amphipathic molecules, having both hydrophobic and hydrophilic regions, and are therefore able to interact with both water and lipids. They are an integral part of lipoprotein particles and are important in stabilizing their structures. They also act as ligands for specific cellular receptors and mediate lipoprotein metabolism. These two characteristics make the apolipoproteins responsible for binding and transporting lipids through the lymphatic and circulatory systems and are therefore crucial to the study of any fat and cholesterol related conditions and illnesses. Accordingly, antibodies specific for each apolipoprotein should be considered important research and diagnostic tools. 

Structural representation of apolipoprotein e3 
Structural representation of apolipoprotein e3 (apoe3).






Lipoprotein particles fall into four main categories based on their size and density. The categories include high density lipoprotein (HDL), low density lipoprotein (LDL), very low density lipoprotein (VLDL), and chylomicrons (see structure below), each carrying a different combination of apolipoproteins. HDL carries apo-A-I and A-II, LDL carries apo-B, while VLDL and chylomicrons carry a combination of all apolipoproteins.


Lipoprotein Structure

Chemical structure of cholesterol

Chemical structure of cholesterol



The molecular weights of the apolipoproteins vary as shown in the following list:




Molecular weight


















Our understanding of the functions of each apolipoptrotein varies:

APO A-I is the primary protein component of HDL. It promotes transport of fat and cholesterol from the peripheral tissues to the liver for degradation and excretion. It plays a role in the body’s natural ability to regulate excess cholesterol. HDL is often called good cholesterol and has long been monitored in patients. Reduced or deficient levels of HDL have been correlated with an increase in the risk for coronary artery disease, myocardial infarction, and peripheral vascular disease. It may be that APO A-I measurements are an even more accurate indicator of disease than HDL measurements.


To detect human APO A-I use APOLIPOPROTEIN A-I Antibody

To detect mouse APO A-I use APOLIPOPROTEIN A-I Antibody




APO A-II is the second most abundant protein in HDL in plasma, and may be important in the formation and stabilization of HDL.

To detect human APO A-II use APOLIPOPROTEIN A-II Antibody





APO B is the primary protein in LDL, and like A-I, it plays a role in lipid transport and metabolism by transporting and storing cholesterol in peripheral tissues. APO B may be responsible for regulating the rate of cholesterol synthesis. LDL is often called bad cholesterol, and like HDL, it is monitored. In contrast to A-I, increased levels of APO B appear to correlate with an increase in the risk and frequency of coronary artery disease and other cholesterol-related conditions. Monitoring APO B may be more important than monitoring LDL.

To detect human APO B use APOLIPOPROTEIN B Antibody





APO C-I, found in human plasma, plays an integral role in the prevention and reduction of human atherosclerosis. The purpose of APO C-I appears to be to regulate or inhibit cholesteryl ester transfer protein (CETP), the plasma protein responsible for mediating the exchange of esterified cholesterol and triglycerides back and forth between the low and high density lipoproteins.  APO C-I, one of the most positively charged proteins in the human body, most likely prevents CETP activity by modifying the electrostatic charge of HDL.  This results in more cholesteryl esters remaining in the more beneficial HDL over other, more atherogenic lipoproteins, making this protein important to the study and prevention of all atherosclerosis-related diseases including coronary heart disease, carotid artery disease, peripheral artery disease, and chronic kidney disease.

To detect human APO C-I use APOLIPOPROTEIN C-I Antibody




APO C-II, found in the plasma, is a component of chylomicrons and VLDLs.  It activates the lipoprotein lipase enzyme in the capillary vessels, which hydrolyzes the triglycerides in these lipoproteins and releases them as free fatty acids to be collected in the muscles and adipose tissues.  Deficiencies in this protein have been shown to cause severely elevated levels of triglyceride-rich lipoproteins and cholesterol, and associated health problems such as recurrent pancreatitis, enlarged liver and spleen (hepatosplenomegaly), and xanthomatosis.  Replacement therapy using recombinant APO C-II has been studied as a possible treatment for these conditions.

To detect human APO C-II use APOLIPOPROTEIN C-II Antibody






APO C-III, a relatively small protein found on the surface of most lipoproteins, alternatively inhibits the lipoprotein lipase enzyme, while also inhibiting the hepatic lipase enzyme and the uptake of triglyceride-rich particles by hepatic receptors. Increased levels of APO C-III will cause an excess of triglycerides (hypertriglyceridemia) and associated conditions such as pancreatitis, hepatosplenomegaly, and xanthomatosis. Excess APO C-III has also been associated with insulin resistance and atherosclerosis.

To detect human APO C-III use APOLIPOPROTEIN C-III Antibody




APO E is synthesized in several areas of the body, and possesses multiple functions. It is primarily synthesized in the liver, where it functions in the transport of triglycerides to the liver for metabolism. It is also produced in small amounts in the intestines, spleen, lungs, adrenals, ovaries, kidneys, and muscles. A large amount of APO E is also produced in the brain, and serves to transport cholesterol to neurons. Until recently, APO E was studied largely only for its role in cholesterol metabolism, but it has now begun to be studied for its tangential roles in other areas such as immune regulation, cognition, and Alzheimer’s disease research. 

To detect human APO E use APOLIPOPROTEIN E Antibody




APO J, also called clusterin, has been associated with a variety of activities, most of them having to do with programmed cell death (apoptosis) and its inhibition, as well as the clearance and recycling of these dead cells.  It has also been associated with phagocyte recruitment, aggregation induction, complement attack prevention, membrane remodelling, lipid transport, and hormone transport.  It is known to bind and form complexes with immoglobulins, lipids, bacteria, leptin, heparin, amyloids, and other entities.

To detect human APO J use APOLIPOPROTEIN J Antibody



The Rockland Advantage: Anti-Apolipoprotein Antibodies

Rockland purifies apolipoprotein antibodies from hyper-immune serum by immunoaffinity chromatography followed by extensive cross adsorption to remove unwanted reactivity and generate precise specificities.  Less than 1% cross-reactivity is typically seen when assayed by ELISA against a panel of human and mouse apolipoproteins and related serum proteins.  


Reference Rockland Bucket


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