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)

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

Agarose bound Wheat germ agglutinin (WGA) is prepared using 4% agarose beads. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane 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
• 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

Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). This lectin is used for the purification of insulin receptors and for neuronal tracing.

Agarose bound* WGA 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: Chitin Hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution generally required

*5 mg lectin/ml gel

Agarose bound Con A is prepared using our affinity-purified lectins. Con A recognizes α-linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins. At neutral and alkaline pH, Con A exists as a tetramer of four identical subunits; below pH 5.6, Con A dissociates into active dimers of 52 kDa. Acetylation, succinylation, or other derivatizations can also produce stable forms with dimeric structures. (See succinylated Con A). Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds.

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

Con A requires calcium or manganese ions at each of its four saccharide binding sites. Although these divalent metal ions are bound tightly to the polypeptide structure, buffers which can bind calcium (such as phosphate) generally should be avoided in diluting Con A, since a gradual loss in activity may occur.

Agarose bound* Con A 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. 

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.

Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside or Glycoprotein Eluting Solution (ES-1100)

*6 mg lectin/ml gel

Agarose bound PNA is prepared using our affinity-purified lectins. Peanut agglutinin binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and many other soluble and membrane-associated glycoproteins and glycolipids. With certain exceptions, the receptor sequence for PNA is normally sialylated which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). Even sialic acid which is not bound directly to the receptor sugars may inhibit binding. The presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence.

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 galactose or Glycoprotein Eluting Solution (ES-2100)

PNA is useful in distinguishing between normal and tumor tissues and in assessing malignancy in transitional mucosa. In addition, PNA binding can be used to measure cellular maturity in lymphoid tissues, to distinguish a variety of lymphocyte subpopulations in man and experimental animals, and to measure the levels of lymphoid cell populations in many diseases. PNA can be employed in the fractionation of stem cells in mice for use in bone marrow transplantation across histocompatibility barriers.

A major cell surface receptor for PNA may be asialo GM₁ ganglioside. Since PNA shares specificity with the antibody to this glycolipid, PNA and the antibody can be used interchangeably in some applications.

Agarose bound* PNA 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.

*5 mg lectin/ml gel

Agarose bound Ricinus communis agglutinin I is prepared using our affinity-purified lectins. This lectin consists of two subunits of 60 kDa which can be dissociated by reducing agents into closely related chains between 27 kDa and 33 kDa. One of the chains appears to be common to the B chain of another castor bean lectin, ricin, while the other chain is unique to RCA I.

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 galactose or lactose or Glycoprotein Eluting Solution (ES-2100)

Agarose bound* Ricinus communis agglutinin I 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