P2459
Phenyl-Sepharose 6 Fast Flow
high substitution, extent of labeling: ~40 μmol per mL (high substitution)
Synonym(s):
Phenyl-Agarose
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About This Item
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form
suspension
extent of labeling
~40 μmol per mL (high substitution)
matrix
agarose, 6% cross-linked
matrix activation
epichlorohydrin
matrix attachment
ether
matrix spacer
3 atoms
particle size
45-165 μm
storage temp.
2-8°C
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General description
P2459-200ML′s updated product is GE17-0973-05
Application
Phenyl Sepharose™ is used in protein chromatography, affinity chromatography, hydrophobic interaction media, resins and separation media. Phenyl Sepharose™ has been used in studies that contributed to improving industrial applications in additives in detergents and feed industries. Phenyl Sepharose™ has also been used to study microbial communities inhabiting hypersaline environments.
Physical form
Suspension in 20% ethanol
aqueous ethanol suspension
Legal Information
Sepharose is a trademark of Cytiva
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Description
Pricing
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 3
Storage Class Code
3 - Flammable liquids
WGK
WGK 3
Flash Point(F)
104.0 °F
Flash Point(C)
40 °C
Certificates of Analysis (COA)
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K A Rye et al.
The Journal of biological chemistry, 271(8), 4243-4250 (1996-02-23)
The effect of sphingomyelin (SPM) on the structure and function of discoidal and spherical reconstituted high density lipoproteins (rHDL) has been studied. Three preparations of discoidal rHDL with 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC)/SPM/unesterified cholesterol (UC)/apolipoprotein (apo)A-I molar ratios of 99.6/0. 0/10.2/1.0, 86.0/13.6/10.8/1.0
K A Rye et al.
The Journal of biological chemistry, 270(1), 189-196 (1995-01-06)
The effect of cholesteryl ester transfer protein (CETP) on the size, composition, and structure of spherical, reconstituted HDL (rHDL) which contain apolipoprotein (apo) A-I as their sole apolipoprotein has been studied. Spherical rHDL were incubated with CETP and Intralipid for
Frank J Ruzicka et al.
Biochimica et biophysica acta, 1774(2), 286-296 (2007-01-16)
A gene eam in Clostridium difficile encodes a protein that is homologous to lysine 2,3-aminomutase (LAM) in many other species but does not have the lysyl-binding residues Asp293 and Asp330 in LAM from Clostridium subterminale SB4. The C. difficile protein
Purification and partial characterization of <I>Rhizomucor miehei</I> lipase for ester synthesis.
Wu, X.Y., et al.
Applied Biochemistry and Biotechnology, 59, 145-158 (1996)
C Mawadza et al.
Journal of biotechnology, 83(3), 177-187 (2000-10-29)
Cellulases produced by two Bacillus strains, CH43 and HR68, isolated from hot springs in Zimbabwe, were purified to homogeneity from culture supernatants. Both enzymes had molecular mass of 40 kDa and isoelectric point of 5.4. The enzymes also resembled each
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