Phenyl Focurose 6BB

    • Phenyl-6BB-Elabscience
    • Phenyl-6BB-Elabscience
    • Phenyl-6BB-Elabscience

      Catalog number:E-CM-HI04

      • 25mL
      • 100mL
      • 300mL
      • 500mL
      • 1L
      - +
      Price: Inquire

      Matrix: Cross-linked 6% agarose

      Particle size range: 165-300 µm

      Average particle size: 230 µm

      Ligand density: 25-30 µmol/mL

      Lead Time: 7~10 daysWelcome to order from local distributors.

      Add to cart Compare Bulk request Manual

      Product introduction

      Phenyl-6BB 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-6BB is mainly used for capture of initial samples and moderate purification of samples.



      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-6BB can be applied in preliminary capture and moderate purification, and it can be repeatedly used in combination ion exchange chromatography media.

      4. High flow rate.


      Performance index




      Cross-linked 6% agarose

      Particle size range

      165-300 µm

      Average particle size

      230 µm

      Ligand density

      25-30 µmol/mL

      Binding capacity

      25 mg (IgG)/mL (media)

      pH stability

      2-14 (short-term)

      3-13 (long-term)

      Chemical stability

      All of the commonly used buffers, 1M acetic acid, 1M NaOH, 8M urea, 6M guanidine hydrochloride, 30% isopropyl alcohol, 70% ethanol

      Maximum flow rate

       750 cm/h

      Storage buffer

      20% Ethanol

      Storage temperature

      4~30(4~8is preferred)


      Factors affecting hydrophobic chromatography


      Function mechanism


      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.


      The higher the temperature, the stronger the protein hydrophobic will be.

      Temperature must be maintained to be the same. Room temperature is recommended.


      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

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