Musa paradisiaca Lectin (BanLec) - Pure

The glucose/mannose-specific lectin (BanLec) was isolated from plantains, Musa paradisiaca. BanLec is a dimeric protein that consists of two identical 15 kDa subunits, composed of 141 amino acid residues, and has an isoelectric point of pH 7.3. Based on its crystal structure, this lectin exhibits some uncommon binding properties, as it recognizes 1,3-sugar units at the reducing termini and the internal α-1,3-linked glucosyl residues. Studies have also shown that BanLec has two primary carbohydrate binding sites per subunit. BanLec is known to be a potential immunomodulatory molecule and has been demonstrated to inhibit HIV-1 by binding directly to gp120 (HIV-1 envelope protein) and being able to block HIV-1 cellular entry. It has a potential anti-viral microbicide that could be used to prevent sexual transmission of HIV-1. BanLec exhibits a strong mitogenic activity towards murine T-cells. It is a stable glycoprotein that agglutinates rabbit erythrocytes.

Recommended Usage: Recommended dilutions of 0.5 – 10 μg / ml in 1XPBS. 1 – 10 μg / ml of BanLec Lectin can agglutinate neuraminidase treated human erythrocytes.

Storage Instruction: To prevent degradation and avoid repeated freeze-thaw cycles, aliquot your product into small, single-use volumes and store them at -20°C

Application

Immunohistochemistry, Immunocytochemistry, Cell typing, Blotting, Bioconjugations, Antiviral activity, Glycobiology.

References

1.Willy J. Peumans et al. Fruit specific Lectin from banana $ plantain. Planta (2000) 211: 546-554.
2.Liu, X., et al. The lectin from Musa paradisiaca binds with the capsid protein of tobacco mosaic virus and prevents viral infection. Biotechnol Biotechnol Equip. (2014) 28(3):408-416.
3.Singh, S., et al. Banana Lectin: A Brief Review. Molecules. (2014) 19:18817-18827.