Features:

• Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×10⁷ daltons
• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Hydrophilic spacer arm is inserted between the lectin and the matrix
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• 2 mg lectin/ml gel
• Inhibiting/Eluting Sugar: 100 mM L-fucose?or?Glycoprotein Eluting Solution (ES-3100)

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This lectin is a dimer of two identical subunits of about 36 kDa each. Unlike Ulex europaeus and Lotus tetragonolobus lectins which prefer (α -1,2) linked fucose residues, Aleuria aurantia lectin binds preferentially to fucose linked (α -1,6) to N-acetylglucosamine or to fucose linked (α -1,3) to N-acetyllactosamine related structures. AAL also reversibly binds fucose attached to nucleic acids

Agarose bound* Aleuria Aurantia lectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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 retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 100 mM L-fucose

*2 mg lectin/ml gel

Agarose bound Erythrina cristagalli lectin?is prepared using 4% agarose beads.?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.

Features:

• Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×10⁷ daltons
• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Hydrophilic spacer arm is inserted between the lectin and the matrix
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• Inhibiting/Eluting Sugar: 200 mM lactose?or?Glycoprotein Eluting Solution (ES-1100)

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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.

Agarose bound* Erythrina cristagalli lectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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.

*3 mg lectin/ml gel

This coupling method provides several advantages over the traditional cyanogen bromide procedure:

• Maximum carbohydrate binding activity of the coupled lectins is retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

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Agarose bound Soybean agglutinin is prepared using our affinity-purified lectins.?Composed of four subunits of approximately equal size, soybean agglutinin is a family of closely related isolectins. This glycoprotein has a molecular weight of about 120 kDa and an isoelectric point near pH 6.0. SBA preferentially binds to oligosaccharide structures with terminal α- or β-linked N-acetylgalactosamine, and to a lesser extent, galactose residues. Binding can be blocked by substitutions on penultimate sugars, such as fucose attached to the penultimate galactose in blood group B substance.

Features:

• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• Inhibiting/Eluting Sugar:?200 mM?N-acetylgalactosamine or Glycoprotein Eluting Solution (ES-2100)

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An important application for SBA is the separation of pluripotent stem cells from human bone marrow. Cells fractionated by SBA do not produce graft vs host disease and can be used in bone marrow transplantation across histocompatibility barriers.

Agarose bound* Soybean agglutinin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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 retained
• Linkage is stable over a range of pH values

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*4 mg lectin/ml gel

?

Features:

• Matrix is heat stable, cross-linked 4% agarose beads with a molecular exlusion of about 2×10⁷ daltons
• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Hydrophilic spacer arm is inserted between the lectin and the matrix
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• 3 mg lectin/ml gel
• Inhibiting/Eluting Sugar: 200 mM?N-acetylgalactosamine?or?Glycoprotein Eluting Solution (ES-2100)

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The binding specificity of Wisteria floribunda lectin (WFL) is not completely clear but this lectin appears to preferentially bind carbohydrate structures terminating in N-acetylgalactosamine linked α or β to the 3 or 6 position of galactose. This lectin has been used to fractionate lymphocyte populations, and although not mitogenic, elicits the production of lymphokines from murine splenocytes.

Agarose bound* WFL is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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 retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine

*3 mg lectin/ml gel

Agarose bound?Ulex europaeus agglutinin is prepared using our affinity-purified lectins.?Ulex europaeus agglutinin I binds to many glycoproteins and glycolipids containing α-linked fucose residues, such as ABO blood group glycoconjugates. This lectin preferentially binds blood group O cells and has been used to determine secretor status. It has been established as an excellent marker for human endothelial cells.

Features:

• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Product supplied as a 1:1 suspension in buffer
• Inhibiting/Eluting Sugar: 50 mM – 100 mM L-fucose?or?Glycoprotein Eluting Solution (ES-3100)

?

Agarose bound* Ulex europaeus agglutinin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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 retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*2 mg lectin/ml gel

Agarose bound?Vicia villosa lectin is prepared using our affinity-purified lectins. This lectin is a family of tetrameric glycoproteins consisting of combinations of A and B subunits similar in structure to PHA and GSL I. The dominant isolectins in our preparations appear to be B subunit-rich. VVL recognizes preferentially α- or β-linked terminal N-acetylgalactosamine, especially a single α-N-acetylgalactosamine residue linked to serine or threonine in a polypeptide (the Tn antigen).?

Features:

• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• Inhibiting/Eluting Sugar: 200 mM?N-acetylgalactosamine?or?Glycoprotein Eluting Solution (ES-2100)

?

Agarose bound* Vicia villosa lectin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x10⁷ daltons 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 retained
• Linkage is stable over a range of pH values

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

*3 mg lectin/ml gel

Agarose bound?Sambucus nigra lectin is prepared using our affinity-purified lectins.?Sambucus nigra lectin, isolated from elderberry bark,?binds preferentially to sialic acid attached to terminal galactose in α-2,6 and to a lesser degree, α-2,3 linkage. Binding is also inhibited to some extent by lactose or galactose. This lectin appears to bind sialic acid linked to?N-acetylgalactosamine or galactose.?

Features:

• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Hydrophilic spacer arm is inserted between the lectin and the matrix
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• 3 mg lectin/ml gel
• 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid or?Glycoprotein Eluting Solution (ES-7100)

?

Our?coupling method provides several advantages over the traditional cyanogen bromide procedure:

• Maximum carbohydrate binding activity of the coupled lectins is retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Elution: 500 mM lactose in buffered saline followed by 500 mM lactose in acetic acid

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Agarose bound?Galanthus nivalis lectin is prepared using our affinity-purified lectins.?Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca⁺⁺ or Mn⁺⁺ for binding. Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues.?

In contrast to most mannose-binding lectins, GNL will not bind α-linked glucose. Reports indicate that this lectin binds rat and mouse IgM but not IgG. The only protein from human serum reported to bind to this lectin is α2-macroglobulin. GNL binds to many viral glycoproteins.

Features:

• Bead diameter ranges in size from 45-165 microns
• Matrix is stable in solutions at pH 3-11 as well as many organic solvents
• Immobilized lectins are prepared using affinity purified lectins
• Covalent attachment preserves lectin activity and minimizes conformational changes that might result in nonspecific or hydrophobic interactions
• Hydrophilic spacer arm is inserted between the lectin and the matrix
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges present after conjugation. ?This minimizes non-specific binding to the matrix
• Product supplied as a 1:1 suspension in buffer
• 3 mg lectin/ml gel
• Inhibiting/Eluting Sugar: 100 mM – 200 mM α-methylmannoside?or?Glycoprotein Eluting Solution (ES-1100)

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?

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Our?coupling method provides several advantages over the traditional cyanogen bromide procedure:

• Maximum carbohydrate binding activity of the coupled lectins is retained
• Linkage is stable over a range of pH values
• Conjugated proteins are not leached off the beads by Tris or other routinely used buffers
• No residual charges are present after conjugation. This minimizes non-specific binding to the matrix.

Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.

Inhibiting/Eluting Sugar: 100 mM - 200 mM α-methylmannoside

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