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Product introduction
Phenyl-6FF(HS) can interact with some hydrophobic protein or antibody under high ionic strength conditions (high ionic strength may increase the interaction between ligand and hydrophobic groups), thus to achieve the purpose of separation and purification. Phenyl-6FF (HS) is mainly used for capture of initial samples and moderate fine purification of samples.
Advantages
1. Rapid, easy to use (one-step purification).
2. Compared with reversed-phase chromatography, the ligand concentration in the hydrophobic interaction chromatography media is low and the elution conditions are mild, which helps to maintain the biological activity of biomolecules.
3. Wide application. Phenyl-6FF (HS) can be applied in preliminary capture and moderate purification, and it can be repeatedly used in combination ion exchange chromatography media.
4. High binding capacity.
Performance index
Ligand | Phenyl |
Matrix | Highly cross-linked 6% agarose |
Particle size range | 45-165 µm |
Average particle size | 90 µm |
Ligand density | 40-50 µmol/mL |
Binding capacity | 40 mg (IgG)/mL (media) |
pH stability | 2-14 (short-term) 3-13 (long-term) |
Chemical stability | All of the commonly used buffers, 8M urea, 6M guanidine hydrochloride |
Flow rate | 450 cm/h |
Storage buffer | 20% Ethanol |
Storage temperature | 4~30℃ (4~8℃ is preferred) |
Factors affecting hydrophobic chromatography
Influence | Function mechanism | Suggestion |
Ligand structure | The binding ability between different ligands and proteins is different. | Pre-experiment is recommended to screen suitable media, which can be referred to in Figure 1. |
Ligand density | The higher the concentration of ligand, the stronger the binding ability will be. | Pre-experiment is recommended to screen the optimum ligand density. |
Sample properties | The hydrophobicity of protein depends on the distribution of hydrophobic groups on its surface. | / |
Salt concentration | The higher the salt concentration, the stronger the binding between the ligand and the protein will be, but the excessive high concentration of salt may result in protein precipitation. | Check the solubility and stability of protein under different salt concentrations. |
Salt type | Different kinds of salts can result in different binding effects. | (NH4)2SO4 and NaCl are preferred, other selections can refer to Figure 2. |
Temperature | The higher the temperature, the stronger the protein hydrophobic will be. | Temperature must be maintained to be the same. Room temperature is recommended. |
pH | Excessive high or low pH may affect the solubility and stability of protein, and pH can affect the binding effect. | The recommended pH range is 5.0-8.5 on the premise of ensuring the solubility and stability of protein. |
Figure 1: Hydrophobic properties comparison of ligands with different concentrations
Figure 2: Salt dissolution and salting out effect of different ions
Application examples
Example 1:
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