Maackia amurensis Lectin (MAA/MAL I) - Pure

Product Description
Leukoagglutinating lectin (MAL I) is isolated from Amur seeds, Maackia amurensis, and is a glycoprotein composed of 287 amino acid residues. This lectin has a molecular weight of 130,000 Da and is a dimer of two subunits. MAL I has an isoelectric point of pH 4.7 and a carbohydrate specificity for GalBeta4GlcNAc.

Maackia amurensis lectin I has non-specific blood group specificity and therefore agglutinates all types of human erythrocytes. MAL I requires three intact sugar units for binding and does not interact when Beta1,4-linkage is replaced with Beta1,3-linkage, nor when the “reducing sugar” of trisaccharide is recycled. Repeating sequence of N-acetyllactosamine is not required but does show to enhance the binding of MAL I to a series of glycolipids. Either N-acetyl or N-glycoyl groups may be substituted without reduction in binding. MAL I elutes a concentration of 0.2 M of lactose.

This product comes in a lyophilized powder form and is stored at -20 C. Reconstitute with sterile buffer. No metal ions are required for binding.

Applications:
Detect Neu5Acα2,3GalBeta1,4GlcNA residues in several animal tissues
Useful in subcellular localization of specific sialyltransferases

References

• Knibbs, R., et al. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. (1991) 266:83-88.
• Yamamoto, K., et al. Sialic acid-binding motif of Maackia amurensis lectins. J Biochem. (1997) 121:756-761.