Musa paradisiaca Lectin (BanLec) - Pure

Product Description
A glucose/mannose-specific lectin (BanLec) was isolated from banana, 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 demonstrated to inhibit HIV-1 by binding directly to gp120 (HIV-1 envelope protein) and being able to block HIV-1 cellular entry. BanLec is a potential anti-viral microbicide that could be used to prevent sexual transmission of HIV-1.

BanLec has an activity dependent on metal ions and exhibits a strong mitogenic activity towards murine T-cells. This lectin is a stable glycoprotein that agglutinates rabbit erythrocytes.

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

Applications:
Glycoprotein research
Immunomodulatory, antiproliferative, antiviral/antimicrobial activities, etc.

References

• 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.
• Singh, S., et al. Banana Lectin: A Brief Review. Molecules. (2014) 19:18817-18827.