Erythrina Cristagalli Lectin (ECL, ECA) - 2 ml

Erythrina cristagallilectin consists of two different subunits of approximately 28 kDa and 26 kDa. The carbohydrate structure to which ECL binds is frequently found in membrane and serum glycoproteins of mammalian origin. Sialic acid substitution on this structure appears to prevent the lectin from binding. This specificity offers an opportunity to utilize ECL to isolate or fractionate mammalian glycoproteins.This lectin has been reported to be useful for the isolation of human natural killer (NK) cells using a negative selection panning technique (protocol available upon request or on our website). Human NK cells appear to lack accessible surface carbohydrate structures required for binding ECL and, unlike other mononuclear cells, do not adhere to ECL-coated culture dishes. Since this procedure involves a negative selection panning technique, a high recovery of viable NK cells can be obtained. The adherent cells can also be recovered by incubation in galactose or lactose.*Erythrina cristagallilectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x107daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix.This coupling method provides several advantages over the traditional cyanogen bromide procedure:Maximum carbohydrate binding activity of the coupled lectins is retainedLinkage is stable over a range of pH valuesConjugated proteins are not leached off the beads by Tris or other routinely used buffersNo residual charges are present after conjugation. This minimizes no...