Peanut agglutinin is a 110,000 molecular weight lectin composed of four identical subunits of approximately 27,000D each. PNA binds preferentially to a commonly occurring structure, galactosyl (b-1,3) N-acetylgalactosamine. This carbohydrate sequence (called the "T-antigen") is present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated glycoproteins and glycolipids. With certain exceptions, the receptor sequence for PNA is normally sialylated which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). In fact, even sialic acid which is not bound directly to the receptor sugars may inhibit binding. Although PNA appears not to require any divalent cations for activity, the presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence. Peanut Agglutinin is useful in distinguishing between normal and tumor tissues and in assessing malignancy in transitional mucosa. In addition, PNA binding has been employed as a measure of cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte subpopulations in man and experimental animals, and to measure the levels of lymphoid cell populations in many diseases. PNA has been employed in the fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers. A major cell surface receptor for Peanut Agglutinin may be asialo GM1 ganglioside. Since PNA shares specificity with the antibody to this glycolipid, PNA and the antibody can be used interchangeably in some applications. Agarose bound Peanut Agglutinin is prepared from affinity-purified lectin. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10e7 are used as the solid-phase matrix to which the lectin is covalently bound. The attachment of the lectin to the solid phase is carefully controlled in order to preserve the activity of the lectin as well as to minimize conformational changes of the bound lectin which might result in nonspecific ionic or hydrophobic interactions. The technique developed to couple lectins to agarose provides a very hydrophilic spacer arm between the protein and the matrix. This ensures maximum expression of the carbohydrate binding activity of the lectin. The linkage is very stable over a range of pH values and, unlike cyanogen bromide linkages, proteins are not leached off the gel by Tris or other routinely used buffers. In addition, residual charges generated during cyanogen bromide conjugation which can produce nonspecific binding are not present on the gel following our coupling procedure.

Small volumes of Arachis hypogaea lectin vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS656108 is a lectin targeting Arachis hypogaea. Also known as Arachis hypogaea (PNA, Peanut Agglutinin) (Agarose).