Griffonia simplicifolia lectin (GSL I+II) is affinity puritied from a woody climbing shrub native to Africa. It consists of both lectins GSL I+II. GSL I+II shows specificity for blood group B greater than blood group A1.
This lectin interacts with pulmonary microvascular endothelial cells, but does not readily interact with pulmonary arterial endothelial cells. This binding pattern has been successfully utilized to enrich cell populations in vitro that possess functional behaviors characteristic of those seen in vivo.
Alkaline phosphatase (AP) is conjugated to Griffonia simplicifolia Lectin (GSL I+II) to show the binding of GSL I+II in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.