Glyoxal Agarose Beads
Gold Biotechnology’s Glyoxal agarose resins are cross-linked, autoclavable agarose beads used for protein immobilization. Our resins are covalently bound to the agarose, giving them a qualitative advantage to resins activated by CNBr. These agarose resins have a higher binding capacity, faster conjugation, more reproducibility and a longer shelf life than CNBr. Glyoxal agarose resins are safer to use and are designed to bind with the amino groups on a protein with high specificity. GoldBio offers both low pressure resins (low density) for R&D scale experiments as well as high pressure resins (high density) for industrial scale separations. For best results, screen your proteins with our Glyoxal Resin Comparison Kit in order to optimize the activation of your specific protein.
Glyoxal (High Density) 6% Agarose Beads, Crosslinked
| Catalog ID | Size | Pricing | |
|---|---|---|---|
| G-303-25 | 25 mL | $ 196.00 | |
| G-303-100 | 100 mL | $ 590.00 | |
| G-303-1000 | 1 L | $ 5,407.00 |
Description
Biomolecules can be immobilized by binding them to a support under conditions that will then determine the characteristics of the complex. Immobilization is a technique that binds a ligand (enzyme, antibody, affinity proteins like Protein A or Protein G) to a support, giving high stability and making it easier to reuse the immobilized molecule.
Glyoxal beads allow a covalent binding of agarose to lysine amino groups (similar orientation to CNBr). Glyoxal agarose beads are ready to use and require no activation. The resin has a high amount of aldehydes groups (40-60 µmoles Glyoxal / ml gel) providing a very good option to conjugate affinity ligands improving the stability of the ligand.
The choice of Glyoxal or Aminoethyl will depend on the biomolecule to be immobilized, the accessibility of the reactive groups, and the direction/ orientation required for the binding to the support.
Product Specifications
| Catalog ID | G-303 |
|---|---|
| Storage/Handling | store at 4°C. Do NOT freeze. |
Glyoxal (Low Density) 6% Agarose Beads, Crosslinked
| Catalog ID | Size | Pricing | |
|---|---|---|---|
| G-302-25 | 25 mL | $ 147.00 | |
| G-302-100 | 100 mL | $ 464.00 |
Description
Biomolecules can be immobilized by binding them to a support under conditions that will then determine the characteristics of the complex. Immobilization is a technique that binds a ligand (enzyme, antibody, affinity proteins like Protein A or Protein G) to a support, giving high stability and making it easier to reuse the immobilized molecule.
Glyoxal beads allow a covalent binding of agarose to lysine amino groups (similar orientation to CNBr). Glyoxal agarose beads are ready to use and require no activation. The resin has a high amount of aldehydes groups (15-25 µmoles Glyoxal / ml gel) providing a very good option to conjugate affinity ligands improving the stability of the ligand.
The choice of Glyoxal or Aminoethyl will depend on the biomolecule to be immobilized, the accessibility of the reactive groups, and the direction/ orientation required for the binding to the support.
Product Specifications
| Catalog ID | G-302 |
|---|---|
| Storage/Handling | store at 4°C. Do NOT freeze. |
Glyoxal HTC 6% HIGH Density Agarose Beads
Glyoxal HTC 6% HIGH Density Agarose Beads
| Catalog ID | Size | Pricing | |
|---|---|---|---|
| G-312-25 | 25 mL | $ 217.00 | |
| G-312-100 | 100 mL | $ 655.00 |
Description
Glyoxal HTC 6% HIGH Density Agarose beads allow covalent binding of agarose to lysine amino groups (similar orientation to CNBr).
This product is adequate to work in large scale process (High Pressure). The resin has a high amount of aldehyde groups (40-60 µmoles Glyoxal / ml gel) providing multiple binding points and high immobilized ligand stability. The resin has been manufactured using 6% HTC agarose beads, and the pore size is adequate to work with enzymes, proteins & small ligands. The stability at high flow is adequate for large scale process.
Product Specifications
| Catalog ID | G-312 |
|---|---|
| Storage/Handling | store at 4°C. Do NOT freeze. |
