Arachis hypogaea Lectin (PNA) - Alexa Fluor 594

Arachis hypogaea agglutinin (PNA) is purified by affinity chromatography and consists of four subunits with a size of approximately 27 kDa each. This lectin has an isoelectric point between pH 5.5 and pH 6.5. It has a carbohydrate specificity for Galβ3GalNAc with an eluting sugar of galactose. Galactose and lactose are poor inhibitors while disaccharide Gal β(1->3)GalNAc and de-sialylated human erythrocyte N-substance (T-antigen which is present in many M and N blood groups) are potent inhibitors of PNA. Although extracts of Arachis hypogaea do not agglutinate untreated or trypsin-treated human erythrocytes, PNA has been known to agglutinate neuraminidase-treated human red blood cells. PNA may be used for clinical determination of T-polyagglutinability of erythrocytes and probing cell membranes of normal and malignant cells. This Lectin can be of use in characterization of tumor-specific antigens on the surface of malignant cells. It can be employed in the fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers.

Alexa Fluor 594, when bound to PNA, can show the binding pattern of this Lectin in cellular imaging and flow cytometry. The excitation wavelength required for Alexa Fluor 594 to fluoresce is high enough to avoid overlapping with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens. This product comes in a stabilized liquid form.

Recommended Usage: Recommended dilutions 0.5 -10 µg/ml in 20mM Tris-HCl pH 7.5 containing 1mM CaCl₂ and 0.5 mM MnCl_2, 50 mM NaCl. Less than 1. Less than 1 µg/ml will agglutinate neuraminidase treated human erythrocytes.

Application

Immunofluorescence, Immunohistochemistry, Cell sorting, Biomarker, Blotting, Glycobiology.

References

1.Jie Sun, Qing-li Yang*, jie Bi, Chu-shu Zhang, Li-na Yu and Feng Zhu. Purification and Identification of a Natural Lectin from the Seed of Peanut Arachis hypogaea. The Open Materials Science Journal, 2011, 5, 78-82
2.Erber, W. N., Asbahr, H., Meyer, B., Herrmann, R. P., & Davies, J. M. (1992). Peanut agglutinin (lectin from Arachis hypogaea) binding to hemopoietic cells: an immunophenotypic study using a biotin streptavidin technique. Pathology, 24(3), 173–176. https://doi.org/10.3109/00313029209063168.

3. Jones, C. J., Benbow, E. W., Knox, W. F., & Stoddart, R. W. (1988). Method for showing human spermatogenesis using Arachis hypogaea (AHA) lectin. Journal of clinical pathology, 41(9), 1017–1018. https://doi.org/10.1136/jcp.41.9.1017

4. Rambihar, C., & Kerman, K. (2010). Magnetic bead-based fluorometric detection of lectin-glycoprotein interactions. Talanta, 81(4-5), 1676–1680. https://doi.org/10.1016/j.talanta.2010.03.021