计算溶液所需的质量、体积或浓度。
Phaseolus vulgaris lectin (PHA-E) is isolated from red kidney beans and purified by affinity chromatography and ion-exchange chromatography. It is a tetrameric protein with a molecular weight of 128 kDa. The lectin recognizes and binds specifically to terminal galactose, N-acetylglucosamine and mannose residues of complex glycans on mammalian glycoproteins. Because of its strong erythrocyte agglutinating activity, it is also known as Erythroagglutinin (PHA-E). PHA-E is not blood group specific. Less than 5 μg/ml agglutinates human erythrocytes of type O and agglutination can be inhibited by certain oligosaccharides. PHA-E lectin is supplied as a white lyophilized powder from a buffer containing from 50 mM NH4HCO3. The purity of the lectin in determined by SDS-PAGE, which generate one single band at 34 kDa. Erythrocyte agglutination studies;Model system of how proteins recognize carbohydrates● Ultrapure quality ● Sμgar specificity: complex oligosaccharides ● Strong erythroagglutinin activity ● Lyophilized powderRed kidney beans
Phaseolus vulgaris lectin (PHA-E) is isolated from red kidney beans and purified by affinity chromatography and ion-exchange chromatography. It is a tetrameric protein with a molecular weight of 128 kDa. The lectin recognizes and binds specifically to terminal galactose, N-acetylglucosamine and mannose residues of complex glycans on mammalian glycoproteins. Because of its strong erythrocyte agglutinating activity, it is also known as Erythroagglutinin (PHA-E). PHA-E is not blood group specific. Less than 5 μg/ml agglutinates human erythrocytes of type O and agglutination can be inhibited by certain oligosaccharides. PHA-E lectin is supplied as a white lyophilized powder from a buffer containing from 50 mM NH4HCO3. The purity of the lectin in determined by SDS-PAGE, which generate one single band at 34 kDa.
● Ultrapure quality
● Sugar specificity: complex oligosaccharides
● Strong erythroagglutinin activity
● Lyophilized powder
Erythrocyte agglutination studies;Model system of how proteins recognize carbohydrates