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描述
Butyl-650M
產品線
TOYOPEARL®
形狀
slurry
包裝
bottle of 100 mL
參數
3 bar max. pressure
技術
HPLC: suitable
基質
polymer (65 μm)
基質活性組
C4 phase
粒徑
65 μm
工作pH值
1-13
容量
40 g/L±10 adsorption capacity (lysozyme)
分離技術
hydrophobic interaction (HIC)
一般說明
TOYOPEARL® HIC resins are hydrophobic interaction chromatography resins that offer the following advantages: strong affinity for water-soluble proteins, high recovery of mass and activity, high sample capacity up to 2-4 times that of gel media, fluctuating salt concentrations will not change the bed volume, mechanical stability to 7kg/cm squared (7 bar/100psi), stability at a wide pH range (2-12), clean in place with 0.5M NaOH, and autoclavable. The exclusion limit of 5x106 Da and large pore size, 1000Å, enables these packings to separate very large proteins by a hydrophobic interaction mechanism, without size exclusion effects.
應用
TOYOPEARL® media are used in hydrophobic interaction media, resins and separation media. TOYOPEARL® media offer high yield recovery of proteins, using various aqueous eluants.
規格
Clean in place with 0.5 M NaOH or 0.1 M HCl.
外觀
Shipped in 20% (v/v) ethanol.
其他說明
Toyopearl Butyl-650 resin has the second highest hydrophobicity of the HIC ligands offered by TBL. Its pore size is the largest of our three butyl resins. Primary applications are for the separation of proteins, their isoforms, and aggregate removal. It is typically used in interresinte purification and polishing steps
法律資訊
Toyopearl is a registered trademark of Tosoh Corporation
訊號詞
Warning
危險聲明
危險分類
Flam. Liq. 3
水污染物質分類（WGK）
WGK 1
個人防護裝備
Eyeshields, Gloves, type N95 (US)
Hongwei Luan et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 24(5), 867-873 (2008-08-30)
A beta-D-xylosidase from Leifsonia shinshuensis DICP 16 was purified to apparent homogeneity using a combination of ammonium sulfate precipitation, DE 52 anion-exchange, Q-Sepharose Fast Flow anion-exchange, Toyopearl Butyl 650C hydrophobic-interaction and Sephacryl S-300 HR gel-permeation chromatography. The purified xylosidase consisted
Hydrophobic interaction chromatography selectivity changes among three stable proteins: conformation does not play a major role
Jones, T.T. and Fernandez, E.J.
Biotechnology and Bioengineering, 87, 288-299 (2004)
V Stocchi et al.
Journal of chromatography. A, 676(1), 51-63 (1994-07-29)
Hydrophobic interaction chromatography (HIC) has been employed extensively in the separation of proteins by elution using a descending salt gradient, with and without the use of detergents or denaturing agents. In this study, a new hydrophobic interaction chromatographic support, Toyopearl
P Ceccaroli et al.
Journal of chromatography. B, Biomedical sciences and applications, 702(1-2), 41-48 (1998-02-04)
Hydrophobic interaction chromatography (HIC) has been used extensively for the separation of proteins and peptides by elution using a descending salt gradient, with and without the use of detergents or denaturing agents. In this paper we compare different hydrophobic interaction
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