Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia)

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has A and B subunits, which recognizes αGalNAc and αGal-end groups respectively. Lectins are extracted from the seeds of the legume shrub Griffonia simplicifolia, which are carbohydrate binding proteins.

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has been used for immunohistochemistry and immunofluorescence staining.

Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) agglutinates human blood group A and B cells. It is specific for αGalNAc- and αGal. It acts as a reagent for the detection of this αGal epitope in biological materials. Lectin from Bandeiraea simplicifolia is used as a marker for xenoreactive antigen (αGal1−3Gal) and cancer. Lectin plays an important role in fertilization, embryogenesis, inflammation, metastasis and host-parasite recognition.

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

Contains citrate buffer salts and calcium chloride

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.

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.