814478
TOYOPEARL® Phenyl-650M Bulk Media
matrix polymer (65 μm), bottle of 100 mL, 65 μm
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Synonym(s):
TOYOPEARL® Phenyl-650 Bulk Media
UNSPSC Code:
41115700
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description
Phenyl-650M
product line
TOYOPEARL®
form
slurry
packaging
bottle of 100 mL
parameter
≤50% organic solvent
3 bar max. pressure
technique(s)
HPLC: suitable
matrix
polymer (65 μm)
matrix active group
phenyl phase
particle size
65 μm
operating pH
1-13
separation technique
hydrophobic interaction (HIC)
General description
Toyopearl Phenyl-650 resin is the middle hydrophobicity of the five HIC ligands offered by Tosoh Bioscience. Primary applications are for the separation of proteins, their isoforms, and aggregate removal. It is typically used in intermediate purification and polishing steps. For high performance separations, the use of TSKgel Phenyl-5PW resin is suggested. Both products have the same selectivity.
Application
Toyopearl media are used in separation media and resins. 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.
Legal Information
Toyopearl is a registered trademark of Tosoh Corporation
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Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 3
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Tara Tibbs Jones et al.
Biotechnology and bioengineering, 87(3), 388-399 (2004-07-29)
Interesting retention and selectivity changes have been noted for a number of proteins in hydrophobic interaction chromatography (HIC). In this study, we investigated the degree to which conformational changes may be responsible for selectivity changes of stable proteins. Hydrogen-deuterium isotope
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
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
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