Erythrina cristagalli Lectin (ECL/ECA) - Separopore® 4B

Applications:

Erythrina cristagalli (coral tree) lectin is a 54 kDa glycoprotein consisting of two different subunits of approximately 28 and 26 kDa. It has a specificity toward galactose residues and appears to have the highest binding activity toward galactosyl (Beta-1,4) N-acetylglucosamine.

Erythrina cristagalli Lectin (ECL) isolated from Erythrina cristagalli (coral tree) seeds coupled with Separopore4B-CL is prepared with affinity-purified lectin. The heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2 x 10⁷ 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.

Erythrina cristagalli Lectin (ECL)-Separopore 4B-CL has been reported to be useful for the isolation of human natural killer (NK) cells using a negative selection panning technique. 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 or ECL coupled agarose beads. 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.

Technical Specifications:

• Ligand: Erythrina cristagalli
• Matrix: Separopore 4B-CL (crosslinked agarose, 4%)
• Particle size range: 52 - 165 µm
• Matrix activation: Cyanogen bromide
• Matrix attachment: Amino
• Ligand density: 3 mg ECL / ml drained gel
• Binding capacity: 2.5 mg asialofetuin /ml drained gel
• Inhibiting/Eluting Sugar: 200 mM Lactose
• Carbohydrate for Elution: .2M Lactose
• Blood Group Specificity: T-antigen
• Form: 50:50 Liquid Suspension, PBS (1x) pH 7.4 w/ 0.01% Thimerosal
• pH stability: 4 - 9
• Storage temp: 2 - 8 C DO NOT FREEZE
• Application Note: Calcium, Manganese, and Zinc are required for binding.

References:

• Lectin-binding assays for the isoforms of human erythropoietin: comparison of urinary and four recombinant erythropoietins. J Endocrinol. (1996) 150: 401-12.
• Characterization of plasminogen activator from two human renal carcinoma cell lines. J Cell Physiol. (1986) 126: 435-43.
• Purification and characterization of cathepsin D from normal human breast tissue. J Protein Chem. (1997) 16: 171-81.
• Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl Environ Microbiol. (1998) 64: 4891-6.
• Characterisation of N-glycans bound to IGFBP-3 in sera from healthy adults. Biochimie. (2010) 92: 97-101.

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