Con A recognizes α-linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins. At neutral and alkaline pH, Con A exists as a tetramer of four identical subunits; below pH 5.6, Con A dissociates into active dimers of 52 kDa. Acetylation, succinylation, or other derivatizations can also produce stable forms with dimeric structures. (See succinylated Con A). Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds.
Con A requires calcium or manganese ions at each of its four saccharide binding sites. Although these divalent metal ions are bound tightly to the polypeptide structure, buffers which can bind calcium (such as phosphate) generally should be avoided in diluting Con A, since a gradual loss in activity may occur.
Rhodamine labeled Con A has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated fluorochromes. The excitation maximum is at 550 nm and the emission maximum is at 575 nm.
Accompanying each fluorescent lectin is an analysis data sheet summarizing the results of our quality control tests and providing pertinent information on the product. All of these reagents are supplied as solutions perserved with sodium azide.
Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside