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.
Application
TOYOPEARL® media are used in hydrophobic interaction media, resins and separation media. TOYOPEARL® media offer high yield recovery of proteins, using various aqueous eluants.
Specifications
Clean in place with 0.5 M NaOH or 0.1 M HCl.
Physical form
Shipped in 20% (v/v) ethanol.
Other Notes
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
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Legal Information
Toyopearl is a registered trademark of Tosoh Corporation
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
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
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
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)
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