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.
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.
BS-I has a major affinity for terminal a-D-galactosyl residues with a secondary affinity for terminal N-acetyl-a-D-galactosaminyl residues.
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 ß-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.
0.2, 1 mg in serum bottle