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)
Specifications
Unit Size
2 ml
Applications
Glycobiology, Affinity Chromatography
Recommended Storage
2-8 °C DO NOT FREEZE
Solution
10 mM HEPES, pH 7.5, 0.15 M NaCl, 0.1 mM CaCl2, 20 mM galactose, 0.08% sodium azide, 0.01 mM MnCl2
Recommended Usage
Wash gel thoroughly with buffer before use to remove sugar added to stabilize the lectin. Recommended product for eluting glycoconjugates bound to this agarose-lectin: Glycoprotein Eluting Solution, Cat. No. ES-2100. Alternatively, 0.2 M N-acetylgalactoseamine in buffered saline can be used. After use, wash the gel with several column volumes of buffered saline, then resuspend gel in buffered saline containing 0.08% sodium azide for storage.
Matrix Conjugate
Lectins
Sugar Specificity
Galactose, N-Acetylgalactosamine
Conjugate
Agarose
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