Molecular Weight 54 | |
Extinction Coefficient 1.3 | |
Formulation 10 mM HEPES, 0.15 M NaCl, pH 7.5, 0.1 mM CaCl2, 0.08% sodium azide. | |
Inhibiting or Eluting Sugar Lactose | |
Unit Size 5 mg | |
Storage Instructions 2-8 °C; Store frozen for long term storage | |
Sugar Specificity Terminal type 2 LacNAc, and terminal type 2 LacdiNAc | |
Usage Summary For most applications we recommend a freshly prepared working solution of 5-20 µg/ml in the below buffer. | |
Applications Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Elispot, ELISAs, Glycobiology | |
Concentration 5 mg active conjugate/ml | |
Conjugate Biotinylated |
Erythrina Cristagalli Lectin (ECL, ECA), Biotinylated
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 agarose bound 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.
Biotinylated Erythrina cristagalli lectin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
$227.00
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Technical Information Erythrina cristagalli lectin 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 agarose bound ECL to isolate or fractionate mammalian glycoproteins. This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN ABC Reagent, Avidin D conjugate, or streptavidin derivative. Inhibiting/Eluting Sugar: 200 mM lactose |
Citations |
Product FAQs
I recently purchased a biotinylated lectin. The datasheet supplied with the lectin suggests including 0.1 mM Ca++as part of the recommended buffer to prepare a working solution. What should I specifically add, and why is this required?
From our experience we have found that some lectins require Ca++ to be present for optimal binding activity. We suggest using calcium chloride (CaCl2) to fortify working solutions and ensure a minimum level of Ca++ is met. This may be particularly pertinent if using phosphate based buffers as diluents and storage solutions.


