Succinylated Wheat Germ Agglutinin (Fluorescein)

Succinylated Wheat Germ Agglutinin (Fluorescein) (100 μg, 1 mg/mL, 0.5 mg/mL, 60 μg/mL; 1.5 h) is an acidic protein with an isoelectric point (pI) of 4.0. Its solubility under neutral pH conditions is 100-fold higher than that of unmodified wheat germ agglutinin. It maintains a stable dimeric state even at a pH as low as 4.8, and possesses completely identical light absorption properties to unmodified wheat germ agglutinin (HY-NP091)^[1].
Succinylated Wheat Germ Agglutinin (Fluorescein) retains the ability to bind to ligands containing N-acetylglucosamine^[1].
Succinylated Wheat Germ Agglutinin (Fluorescein) (2-500 μg/mL, 2.5 mM, 0.03 mM, 50 mM; 1 h) retains agglutinating activity against rabbit red blood cells, mouse thymocytes, mouse splenocytes, and A⁺ human red blood cells even at the lowest concentration of 2 μg/mL (rabbit- and mouse-derived cells) or 10 μg/mL (type A-positive human red blood cells), but fails to agglutinate horse red blood cells even at a concentration as high as 500 μg/mL^[1].
Succinylated Wheat Germ Agglutinin (Fluorescein) exhibits almost identical fluorescence and phosphorescence responses to N-acetylglucosamine oligosaccharides as unmodified wheat germ agglutinin^[1].
Succinylated Wheat Germ Agglutinin (Fluorescein) binds to both untreated and neuraminidase-treated BHK 21 C 13 cells; it binds to rat splenic lymphocytes non-cooperatively; and it binds to rat splenic lymphocytes with high affinity^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.