N-Acetyl-D-Glucosamine (GlcNAc) Separopore® 4B-CL

Applications:

N-Acetyl-glucosamine-Separopore® 4B-CL is used to purify wheat germ (Triticum vulgaris) lectin, other lectins, and certain other carbohydrate-binding proteins. The purification results in specificity and prolonged biological activity of the protein depending on the applied conditions. N-acetyl-galactosamine is attached to Separopore® through hydroxyl groups.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References

Characterization and purification of the discoidin domain-containing protein retinoschisin and its interaction with galactose. Biochemistry. (2008) 47: 9098-106.
Molecular cloning and characterization of novel ficolins from Xenopus laevis. Immunogenetics. (2003) 55: 29-37.
The myrosinase-binding protein from Brassica napus seeds possesses lectin activity and has a highly similar vegetatively expressed wound-inducible counterpart. Eur J Biochem. (1997) 250: 680-8.
Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain. J Biol Chem. (1993) 268: 18560-6.
Identification of the macrophage mannose receptor as a 175-kDa membrane protein. Proc Natl Acad Sci U S A. (1986) 83: 2501-5.
Two distinct UDP-galactose: 2-acetamido-2-deoxy-D-glucose 4 beta-galactosyltransferases in porcine trachea. J Biol Chem. (1984) 259: 8045-7.
Characterization of UDP-galactose:2-acetamido-2-deoxy-D-glucose 3 beta-galactosyltransferase from pig trachea. J Biol Chem. (1983) 258: 9893-8.
The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites. Eur J Biochem. (1979) 93: 453-60.
Affinity chromatography of soluble galactosyltransferases using an easily synthesized N-acetylglucosamine-agarose bead. Experientia. (1976) 32: 690-1.
Purification of native and synthetic lysozyme with tri-(N-acetylglucosamine)-agarose. Methods Enzymol. (1974) 34: 639-45.