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.
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Griffonia simplicifolia Lectin (GSL I+II) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.