Description_x000D_ General description_x000D_ Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and possesses a carbohydrate binding sites on the surface._x000D_ Application_x000D_ Lectin from Arachis hypogaea (peanut) has been used:_x000D_ • to determine the acrosomal status (presence or absence of acrosomal matrix corresponding to intact or acrosome-reacted spermatozoa) on viable sperm cells_x000D_ • to probe cryosections of mediastinal lymph nodes (mLNs) with fluorochrome-labeled PNA and anti-B220 to detect germinal centers (GCs)_x000D_ • to visualize the cone outer segments of pre-treated retinal sections_x000D_ Packaging_x000D_ 1, 2, 5 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling. This is because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism._x000D_ PNA does not agglutinate normal human erythrocytes, but strongly agglutinates neuraminidase treated erythrocytes. PNA has potent anti-T activity similar to the anti-T antibody in human sera. The lectin can be used to distinguish between human lymphocyte subsets._x000D_ Physical form_x000D_ Contains phosphate buffer salts and NaCl