Musa paradisiaca Lectin (BanLec) - Pure

Product Description

The 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 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.

Specifications:

Abbreviation: BanLec

Material Source: Banana

Preferred Sugar Specificity: Mannose

Inhibiting or Eluting Sugar: α-Methylmannoside

Divalent Ions: Zn++

Mitogenic Activity: Yes

Lyophilized or Liquid: Lyophilized

Storage Temperature: -20°C

Hazardous Shipping: Non-hazardous

Application

Glycoprotein research, Immunomodulatory, antiproliferative, antiviral/antimicrobial activities, HIV viral prevention studies

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.