Cona

Concanavalin A (ConA) is a plant lectin extracted from the seeds of the jack bean, Canavalia ensiformis. It binds specific carbohydrate structures, particularly α-D-mannosyl and α-D-glucosyl residues, on glycoproteins and other glycoconjugates. The binding is calcium- and manganese-dependent and occurs most strongly with certain terminal mannose and glucose moieties.

ConA is a homotetramer, with carbohydrate-binding sites formed at subunit interfaces. Its activity requires bound divalent cations and can be influenced by pH and temperature. The protein’s affinity and specificity for sugars make it a widely used tool in carbohydrate biology and biochemistry.

In laboratory use, ConA is employed for glycoprotein purification via affinity chromatography (often on ConA–agarose or ConA–Sepharose matrices). It also serves as a mitogen for T lymphocytes, stimulating their proliferation in vitro, which supports studies of immune function and cell signaling. ConA-binding assays are used to analyze glycosylation patterns, and the lectin can aid in detecting carbohydrate motifs in various glycoproteins.

Safety and handling: ConA is a potent research reagent and can be toxic if ingested or misused. It should be handled with appropriate laboratory safety practices, including personal protective equipment and proper waste disposal. It is intended for laboratory use and is not suitable for dietary or therapeutic applications.

See also: Lectins, glycoproteins, affinity chromatography, T-cell mitogens.