Butyl-S 6FF 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. Butyl S-6FF is mainly used for capture of initial samples and moderate and fine 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. Butyl S-6FF can be applied in preliminary capture, moderate purification and fine purification, and it can be repeatedly used in combination ion exchange chromatography media.
Highly cross-linked 6% agarose
Particle size range
Average particle size
10-20 mg (Lysyme)/mL (media)
All of the commonly used buffers, 1M Acetic acid, 1M NaOH, 8M urea, 6M guanidine hydrochloride, 30% Isopropyl alcohol, 70% Ethanol
4~30℃ (4~8℃ is preferred)
Factors affecting hydrophobic chromatography
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.
The higher the concentration of ligand, the stronger the binding ability will be.
Pre-experiment is recommended to screen the optimum ligand density.
The hydrophobicity of protein depends on the distribution of hydrophobic groups on its surface.
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.
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
추가비용을 고객에게 부담시지키 않습니다. (단, 고객 변심 또는 주문 반복으로 인한 경우의 반환비용은 고객님이 부담하셔야
::: 교환 및 반품이 가능한 경우:::
단, 상품을 개봉하여 상품가치가 상실된 경우에는 교환/반품이 불가능합니다.
:::교환 및 반품이 불가능한 경우:::
주문 취소 및 반품으로 환불을 요청하실 경우에는 E-mail(firstname.lastname@example.org)이나 고객만족센터 (042-824-9026)을
통해 요청하시면 친절하게 처리해 드리겠습니다.주문 취소 후 반품 가능 여부를 확인한 다음 3일 이내에 결제 금액을 환불해 드리겠습니다.