ROTI®Garose-Biotin and Streptavidin beads offer the perfect solution for the isolation of biotinylated and streptavidinated molecules in benchtop column chromatography or in batch procedures.
With a value of Ka~10-14/M, the affinity of avidin and streptavidin for biotin is the strongest non-covalent bond between molecules known in biochemistry. Efficient and highly specific isolation of biotinylatd or avidin/streptavidin-tagged molecules via affinity chromatography is based on this particular affinity.
The matrix is easy to pack and results in very evenly packed columns. Elution is carried out via 8 M guanidine-HCl or prior to gel loading during heating in gel loading buffer. Merely no unspecific binding of unlabelled molecules takes place, even during purification from raw extracts.
Biotin coupled agarose beads for affinity chromatography. 50 % bead suspension in 20 % ethanol.
ROTI®Garose-Streptavidin Beads offer the perfect solution for your specific application of low flow column chromatography or isolation in batch mode.
Recommended for isolation of biotinylated molecules in batch mode or via columns via low pressure affinity chromatography.
The matrix of ROTI®Garose-Streptavidin Beads consists of beaded 6 % cross-linked agarose. Elution of imminobiotinylated molecules is performed by 50 mM NH4-acetate buffer. Isolation of an antigen by biotinylated antibodies can be performed by 0.1 M glycine buffer.
Streptavidin is immobilised to the beads through a spacer arm and covalent carboxy/amide linkage, not only minimizing streptavidin leakage during elution, but also enhancing the binding capacity by reduction of steric effects.
Gebruikstip | Bead suspension, binding capacity ≥120 nmol/ml packed matrix |
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Particle size | 50-150 µm |
Beads (cross-linked agarose) | 6 % |
Ligand | Streptavidin |
Binding capacity (gel) (free biotin) | ≥120 nmol/ml |
Ethanol | 20 % |