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Concanavalin A is a lectin protein originally extracted from the jack-bean Canavalia ensiformis. It binds specifically to certain structures found in various sugars, namely internal and nonreducing terminal alpha-mannosyl groups. It is used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities. It is also used in lectin affinity chromatography.
Concanavalin A is also a lymphocyte mitogen.
It has also been shown as a stimulator of several matrix metalloproteinases (MMPs).[1]
See also
References
- ^ Author(s): YU, M; SATO, H; SEIKI, M; THOMPSON, EW Title: COMPLEX REGULATION OF MEMBRANE-TYPE MATRIX METALLOPROTEINASE EXPRESSION AND MATRIX METALLOPROTEINASE-2 ACTIVATION BY CONCANAVALIN A IN MDA-MB-231 HUMAN BREAST-CANCER CELLS Source: CANCER RESEARCH, 55 (15): 3272-3277 AUG 1 1995 ISSN: 0008-5472
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