Lotus tetragonolobus Lectin (LTL) - Pure

Product Description
Pure lectin LTL is isolated from lotus seeds, Lotus tetragonolobus, and is composed of 240 amino acid residues. LTL is a glycoprotein with a molecular weight of 107,000 and consists of four subunits. This lectin has different isoelectric points of pH 7.3, 7.6, 7.9, 8.2 and a carbohydrate specificity toward α-fucose. A fucose-Sepharose affinity column that is washed with PBS buffer (pH 7.3) elutes a concentration of 0.1M of fucose in PBS.

Lotus tetragonolobus is a fucose-binding anti-H(O) lectin. Reports show that a minimum hemagglutinating dose of 3.3 µg/ml of the purified lectin against neuraminidase-treated human O erythrocytes, 26.4 µg/ml against B erythrocytes, and 105.6 µg/ml against A erythrocytes, this lectin was most inhibited by L-fucose.

Studies have also found a correlation with the degree of expression of fucose-binding proteins (FBP) binding sites and survival patients with invasive bladder cancer. Transitional cell carcinoma of the human urinary bladder tend to metastasize when it strongly expresses binding sites for LTL.

This product comes in a lyophilized powder form and is stored at -20 C. Calcium and manganese are required for binding.

Applications:
Glycobiology
Immobilized LTL effective in isolating glycans containing Lewis x determinant antigen
Immobilized LTL useful in analyzing specific fucosylation of glycoconjugates

References

• Konami, Y., et al. The primary structure of the Lotus tetragonolobus seed lectin. FEBS. (1990) 268(1):281-286.
• Shirahama, T., et al. The binding site for fucose-binding proteins of Lotus tetragonolobus is a prognostic marker for transitional cell carcinoma of the human urinary bladder. Cancer. (1993) 72(4):1329-34.
• Yamamoto, K., et al. Carbohydrate-binding peptides from several anti-H(O) lectins. J Biochem. (1992) 111(4):436-9.