Lycopersicon esculentum Lectin (LEL/LEA) - Pure

Product Description
Lycopersicon esculentum lectin/agglutinin (LEL/LEA) is isolated from tomato, Lycopersicon esculentum, and purified by affinity chromatography using known glycoprotein inhibitors of tomato lectin agglutination as affinity adsorbents. LEL has an unusually high carbohydrate content value of 50%.

Lycopersicon esculentum lectin has a molecular weight of 71,000 Da and an isoelectric point greater than pH 9. LEL has a carbohydrate specificity toward (GlcNAc) 2-4 and elutes a concentration of 0.2M of chitin hydrolysate. Presence of LEL in the juice of the tomato can be detected by observing agglutination of human erythrocytes A, B, O, or AB blood types, since this lectin is non-specific. Protease-treated erythrocytes are slightly more sensitive to agglutination by LEL. Tomato extracts capable of agglutinating untreated cells contain enough lectin to make purification useful, making it unnecessary to utilize sensitive cells.

This product comes in a lyophilized powder form and is stored at -20 C. Reconstitute with sterile buffer.

Applications:
Suitable for use in ELISA

References

• Kilpatrick, D. A comparison of tomato (Lycopersicon esculentum) lectin with its deglycosylated derivative. Biochem J. (1984) 220(3):843-7.
• Nachbar, M., et al. Tomato (Lycopersicon esculentum) lectin. Methods Enzymol. (1982) 83:363-8.