Iris hybrid Lectin (IRA) - Pure

Iris hybrid agglutinin (IRA) is isolated from dutch iris bulbs. IRA is a heterodimer that consists of two peptide chains, 27,000 and 34,000, linked by disulfide bonds. It has an isoelectric point between pH 7.2 and pH 7.4. This lectin agglutinates both native and trypsin-treated rabbit erythrocytes, not human erythrocytes, with specificity for blood group O and also agglutinates A and B erythrocytes. IRA is N-acetylgalactosamine specific and elutes with sugar GalNAcα1-3Galβ-O. GalNAc α1-3[L-Fuc α 2] Gal and GalNAc α1-3GalNAc are noninhibitory which suggests the importance of a free equatorial hydroxyl group at the C-2 position of the penultimate galactose for lectin binding. Either acetamido group or a fucosyl group at this position appears to cause steric hindrance, thus abolishing binding to the lectin.   Specifications:   Abreviation: IRA Material Source: Dutch iris Preferred Sugar Specificity: N-Acetylgalactosamine Inhibiting or Eluting Sugar: N-Acetylgalactosamine Divalent Ions: None Required Mitogenic Activity: No Lyophilized or Liquid: Lyophilized Storage Temperature: -20C Hazardous Shipping: Non-hazardous Application Agglutination studies, ELISA assays   References Halvarsson, M., et al. Isolation and characterization of an N-acetyl-D-galactosamine-binding lectin from Dutch iris bulbs which recognizes the blood group A disaccharide (GalNAc alpha 1-3Gal). J Biol Chem. (1994) 269(10):7666-73.