Maackia amurensis Lectin (MAA/MAL I) - Pure
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 and is a dimer of two subunits. MAL I has an isoelectric point of pH 4.7 and a carbohydrate specificity for Gal‚àö√º4GlcNAc. This lectin elutes with the sugar lactose.
MAL 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 ‚àö√º1,4-linkage is replaced with ‚àö√º1,3-linkage, nor when the ‚Äö√†√∂¢‚Äö√Ñ√∂‚àö√°Æº‚Äö√†√∂‚àö√¢‚Äö√Ñ√∂‚àö√ë‚Äö√†¬¥‚Äö√†√∂‚àö√¢®‚àö¬Æreducing sugar'‚àöœÄ of trisaccharide is reduced. Repeating sequence of N-acetyllactosamine is not required but does enhance the binding of MAL I to a series of glycolipids. Either N-acetyl or N-glycosyl groups may be substituted without reduction in binding.
This product comes in a lyophilized form and is stored at -20ºC. Reconstitute with sterile buffer. No metal ions are required for binding.
|Molecular Weight||:||130 kDa|
|Shelf Life||:||2 years|
Technical DocumentationSafety Data Sheet (SDS)
Certificates of Analysis (COA)