Sambucus nigra Lectin (SNA/EBL I) is an isolectin isolated from elderberry bark and purified by affinity chromatography. SNA I belongs to the group of type 2 ribosome-inactivating proteins and is composed of an A-chain with enzymatic activity and a B-chain with carbohydrate-binding activity. It has specificity for α2,6-linked sialic acid residues, and elutes with the sugar lactose. SNA I can induce apoptosis through the caspase-dependent pathway at low concentrations. This effect depends on the carbohydrate binding of the B-chain and is independent from the catalytic activity of the A-chain.
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 Sambucus nigra Lectin (SNA/EBL I) 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.