Apolipoprotein H (ApoH) is a plasma glycoprotein of about 50 kDa, which circulates in blood either free or bound to lipoproteins (chylomicrons, LDL, VLDL and HDL). It was first isolated from plasma lipoproteins in 1961 by H. E. Schultze, who names it Beta2-glycoprotein 1 (B2GP1) since he finds it in the beta2-globulin fraction. Other synonyms include Activated protein C-binding protein, APC inhibitor and Anticardiolipin cofactor.

The main role of ApoH is not yet established in vivo. Studies conducted in vitro have shown that the ApoH protein is able to bind to negatively charged molecules and structures, including anionic phospholipids, heparin and apoptotic cells. 

The ApoH protein also participates in the inflammation acute phase and binds to infectious agents. ApoH-Technologies works precisely on this feature to propose tools to bind, concentrate and purify infectious micro-organisms.

The ApoH protein is available in solution, purified from human albumin. After its purification, it is activated and stabilized by patented methods and industrial know-how. It can then be used in solution or immobilized on a solid backing adapted to the detection method. Hence, ApoH is easy to integrate standard detection methods:

by adding a rapid sample pretreatment step to concentrate infectious agents on magnetic beads;

by replacing an active molecule, such as capture antibody, in ELISA sandwich tests.