Arachis hypogaea lectin (PNA, Peanut Agglutinin)
*** for pack size 1g or more, please contact us to inquire about pricing
- Ultrapure quality
- Strong anti-T activity
- Sugar specificity: ß-D-Gal-(1-3)-D-GalNAc
- Agglutinates rabbit erythrocytes at < 0.1 µg/ml after trypsin treatment of the cells
- Lyophilized powder
Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each (1).
PNA is a carbohydrate-free protein that displays specificity towards ß-D-Gal(1-3)-D-galNAc (3). It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose (1).
Medicago’s PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa. The lectin is available in vials containing 50 mg or 10 mg lyophilized powder and the product is to be used for laboratory work only.
- Probe in histochemistry and immuno-histochemistry
- Human erythrocyte/lymphocyte studies
Directions for use
The lectin may be reconstituted with 2 ml of sterile PBS buffer, pH 7.4 before use. Spin the vial gently until full dissolution. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol.
Shipping and storage
The product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than three years from production date when stored below -20°C. After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months.
(1) The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). R Lotan, E Skutelsky, D Danon and N Sharon. JBiol. Chem Vol. 250, No. 21
(2) Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex.
Banerjee, R., Das, K., Ravishankar, R., Suguna, K., Surolia, A., Vijayan, M. (1996) J.Mol.Biol. 259: 281–96.
(3) Liener I. E., Sharon N., Goldstein I. J., (1986) The Lectins – Properties, Functions and Applications in Biology and Medicine.