WGA is not blood group specific but has an affinity for Nacetyl--D-glucosaminyl residues and N-acetyl--Dglucosamine oligomers. WGA contains no protein-bound carbohydrate. Detects glycoproteins containing (14)-Nacetyl-D-glucosamine when used with appropriate peroxidase substrate. Wheat germ agglutinin (WGA) At low pH (below pH 3), this lectin is a monomer (17 kDa by sedimentation velocity). However, it is a dimer (35 kDa by sedimentation velocity) at neutral to slightly acidic pH. By SDS-PAGE analysis, the monomers migrate as 18 kDa proteins. The absorption maximum (lmax) for the native dimer is 272 nm with a molar extinction coefficient (EM) of 1.09 x 10 5 . The pI varies by lectin isoform (isolectins I, IIa, III - pI = 8.7).

Purified WGA was coupled to HRP using proprietary methods.

The inhibition of agglutination activity by di Nacetylglucosamine (GlcNAc)2 on this wheat germ lectin is reported to be aproximately 600 times greater than that of Nacetylglucosamine (GlcNAc). Tri-N-acetylglucosamine (GlcNAc)3 is reported to be about 3000 times more inhibitory than GlcNAc.6 This product is labeled with horseradish peroxidase. The peroxidase label allows use of this lectin in blotting procedures for the identification of sugar side-chains on proteins.