Concanavalin A (ConA)

Concanavalin A is a lectin protein originally extracted from the jack-bean Canavalia ensiformis. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal alpha-mannosyl groups. It was the first lectin to be available on a commercial basis and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities. It is also used to purify macromolecules in lectin affinity chromatography. Concanavalin A is also a lymphocyte mitogen. It is also widely believed to be involved in the interaction between alpha-mannosyl oligosaccharides on the surface of the HIV virus and the human T cell lymphocyte, used by the HIV virus to enter the T cell.It has also been shown as a stimulator of several matrix metalloproteinases (MMPs).