Concanavalin A from Canavalia ensiformis (Jack bean)

agarose conjugate, Type VI, saline suspension


Quality Level


Type VI


saline suspension

extent of labeling

15-30 mg concanavalin A protein per mL


cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment


matrix spacer

1 atom


5-15 mg/mL binding capacity (yeast mannan)(in 0.01 M phosphate buffered saline, pH 6.8, containing 1 mM each CaCl2, MgCl2 and MnCl2)


agarose conjugate

storage temp.


Looking for similar products? Visit Product Comparison Guide

General description

Concanavalin A (Con A), isolated from Jack beans (Canavalia ensiformis), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site. Con A can be isolated by affinity chromatography with dextrans.


Concanavalin A (Con A) has been used for enzyme immobilization.
Used for the purification of glycoproteins containing mannose

Biochem/physiol Actions

Concanavalin A (Con A) is a T cell mitogen that can activate the lymphocytes.
Con A can induce tumor cell death through autophagy.
Con A is not blood group specific but has an affinity for terminal α-D-mannosyl and α-D-glucosyl residues. Ca2+ and Mn2+ ions are required for activity. Con A dissociates into dimers at pH 5.6 or below. Between pH 5.8 and pH 7.0, Con A exists as a tetramer; above pH 7.0 higher aggregates are formed. Con A exhibits mitogenic activity which is dependent on its degree of aggregation. Succinylation results in an active dimeric form which remains a dimer above pH 5.6.

Physical form

Suspension in 1.0 M NaCl + 0.1 M potassium phosphate, pH 6.0, with 1 mM CaCl2, 1 mM MgCl2 and 1 mM MnCl2 containing preservative

Analysis Note

Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, containing Ca2+ and Mn2+ of a 1 mg per mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hr incubation at 25 °C.


12 - Non Combustible Liquids

WGK Germany


Certificate of Analysis

Certificate of Origin

R Lotan et al.
Biochemistry, 16(9), 1787-1794 (1977-05-03)
The effects of several commonly used detergents on the saccharide-binding activities of lectins were investigated using lectin-mediated agglutination of formalin-fixed erythrocytes and affinity chromatography of glycoproteins on columns of lectins immobilized on polyacrylic hydrazide-Sepharose. In the hemagglutination assays, Ricinus communis...
A Kobata et al.
Journal of chromatography, 597(1-2), 111-122 (1992-04-24)
Elucidation of the binding specificity of a concanavalin A-Sepharose column led to the possibility of the affinity chromatography of oligosaccharides and glycopeptides with the use of immobilized lectin columns. Subsequent addition of immobilized erythroagglutinating phytohaemagglutinin, Aleuria aurantia lectin, Datura stramonium...
Concanavalin A for in vivo glucose sensing: a biotoxicity review
Ballerstadt R, et al.
Biosensors And Bioelectronics, 22(2), 275-284 (2006)
Richard C and Geoffrey S
Immunology (2009)
Development of a biosensor specific for cysteine sulfoxides
Keusgen M, et al.
Biosensors And Bioelectronics, 18, 805-812 (2003)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service