Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia)

Agglutination activity is expressed in μg/mL and is determined from serial dilutions of a 1 mg/mL solution using phosphate buffered saline, pH 6.8, containing, for each lectin, calcium, magnesium, and manganese at different concentrations. This activity is the lowest concentration to agglutinate a 2% suspension of appropriate erythrocytes after 1 hr incubation at 25 °C.

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used for microglia detection in murine astrocytes culture by staining the culture with lectin BS1-B4. It has also been used in the preparation of staining solution to incubate the tissue sections.

BS-I has a major affinity for terminal α-D-galactosyl residues with a secondary affinity for terminal N-acetyl-α-D-galactosaminyl residues.

Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling, because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism.

Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and possesses carbohydrate binding sites on the surface.

BS-I is a tetrameric lectin consisting of two types of subunits designated A and B. There are five BS-I isolectins with different subunit composition: BSI-B₄, BSI-AB₃, BSI-A₂B₂, BSI-A₃B and BSI-A₄. BSI-B₄ is blood group B specific and has an exclusive affinity for terminal α-D-galactosyl residues, whereas BSI-A₄ has blood group A specificity and has a major affinity for terminal N-acetyl-α-D-galactosaminyl residues.

Package size based on protein content by Lowry.