Succinylated wheat germ agglutinin (Succ-WGA) is affinity purified from native wheat germ agglutinin (WGA). It is dimeric at pH 5 and dissociates below pH 4.5. Succ-WGA agglutinates rabbit erythrocytes at a minimum concentration of approximately 2 µg/ml and can agglutinate human erythrocytes from blood groups A, B, and O. Its solubility is about 100 times greater than that of unmodified Lectin at neutral pH. Unlike native WGA, Succ-WGA does not bind sialic acid residues but retains specificity for N-acetylglucosamine. The use of conjugates from both native and succinylated WGA allows differentiation between sialylated glycoconjugates and other N-acetylglucosamine structures.

Recommended Usage: Recommended dilutions of 0.5 - 10 μg/ml in 1XPBS. 2 – 10 μg/ml of Succ – WGA will agglutinate rabbit/porcine erythrocytes.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunohistochemistry, Immunocytochemistry, Bioconjugations, Blotting, ELISA, Cell typing, Glycoprotein purification, Glycobiology.

References

1.Robert Bloch and Max M. Burger. purification of wheat germ agglutinin using affinity chromatography on chitin. biochemical and biophysical research communications, March1974, Vol. 58, No. 1.
2.Allen AK, Neuberger A, Sharon N. The purification, composition and specificity of wheat-germ agglutinin. Biochem J. 1973 Jan;131(1):155-62.
3.Wright CS. Crystal structure of a wheat germ agglutinin/glycophorin- sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding. J Biol Chem. 1992 Jul 15;267(20):14345-52.
4.Schwefel D, Maierhofer C, Beck JG, Seeberger S, Diederichs K, Möller HM, Welte W, Wittmann V. Structural basis of multivalent binding to wheat germ agglutinin. J Am Chem Soc. 2010 Jun 30;132(25):8704-19.