Concanavalin A (Con A), Agarose bound, 10 ml, is an agarose-conjugated form of Con A. This lectin recognizes alpha-linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins and exists as a tetramer of four identical subunits at neutral and alkaline pH. Below pH 5.6, Con A dissociates into active dimers of 52 kDa. Covalent attachment of Con A to the agarose beads (using a hydrophilic spacer arm) preserves lectin activity and minimizes conformational changes that might result in non-specific or hydrophobic interactions. This also ensures that conjugated proteins are not leached off the beads by Tris or other routinely used buffers. Agarose-conjugated Con A is supplied as a 1:1 suspension in buffer and comprises a matrix of heat-stable, crosslinked 4% agarose beads that is stable in solutions at pH 3–11 as well as many organic solvents. Because no residual charge is present after conjugation, non-specific binding to the matrix is minimized.