Sambucus nigra Lectin (SNA/EBL I+II) - Pure

Product Description
Sambucus nigra lectin (EBL I+II, also known as SNA) is isolated from elderberry bark. This lectin has a molecular weight of 140,000 and is composed of two ricin-related lectins. EBL I+II is a tetrameric glycoprotein with a recognition of the Neu5Ac(α2-6)Gal or GalNAc linkage in glycoconjugates.

EBL I+II is not blood group specific but it does agglutinate type A erythrocytes more strongly than either B or O cells. Trypsin treated erythrocytes react better than untreated cells. Neuraminidase treated erythrocytes will react with this lectin due to the presence of terminal galactose resides.

Simple sugars, lactose and GalNAc, are the most potent inhibitors of agglutination. Galactose is slightly less inhibitory than either lactose or GalNAc, while melibiose, raffinose, and fucose are 3-4 times less inhibitory than lactose or GalNAc. Data suggests that SNA has a broad specificity for both α- and Beta-linked galactose, as well as unrelated sugars such as fucose. It has been determined that the lectin does not bind to glycoproteins or glycolipids containing only terminal α(2,3)-linked sialic acid residues.

EBL I is composed of an A-chain with enzymatic activity and a B-chain with carbohydrate-binding activity. EBL II consists only of carbohydrate-binding B-chains. EBL I+II induces caspase-dependent apoptosis at low concentrations (nM) order, leading to typical symptoms of cell death in sensitive cells. This effect seems independent from the catalytic activity of the A-chain, but depends on the carbohydrate binding B-chain.

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

Applications:
Immobilized SNA used for affinity purification of glycoproteins
Separation and analysis of glycoconjugates
Detection of sialic acid containing glycoproteins blotted onto nitrocellulose

References