Product Name
Phenyl-Sepharose CL-4B, extent of labeling: ~40 μmol per mL
form
suspension
extent of labeling
~40 μmol per mL
matrix
agarose, 4% cross-linked
matrix activation
epichlorohydrin
matrix attachment
hydroxyl
matrix spacer
3 atoms
particle size
45-165 μm
capacity
15-20 mg/mL binding capacity (human serum albumin)
3-5 mg/mL binding capacity (β-lactoglobulin)
storage temp.
2-8°C
Quality Level
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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.
General description
P7892-200ML′s updated product number is GE17-0810-01
Physical form
Suspension in 20% ethanol
aqueous ethanol suspension
Legal Information
Sepharose is a trademark of Cytiva
signalword
Warning
hcodes
Hazard Classifications
Flam. Liq. 3
Storage Class
3 - Flammable liquids
wgk
WGK 3
flash_point_f
96.8 °F
flash_point_c
36 °C
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O Ploux et al.
The Biochemical journal, 283 ( Pt 2), 327-331 (1992-04-15)
The 8-amino-7-oxopelargonate synthase [6-carboxyhexanoyl-CoA:L-alanine carboxyhexanoyltransferase (decarboxylating); EC 2.3.1.47] from Bacillus sphaericus involved in biotin biosynthesis was purified from an Escherichia coli overproducing strain. The purification afforded an electrophoretically homogeneous enzyme with a specific activity of 0.67 unit/mg. The purified enzyme
Cui, W., et al.
Enzyme and Microbial Technology, 24(3-4), 200-208 (1999)
W Kroutil et al.
Journal of biotechnology, 61(2), 143-150 (1998-07-09)
A highly enantioselective, soluble epoxide from Nocardia sp. EH1 was purified to homogeneity via a four-step procedure: (i) hydrophobic interaction chromatography on Phenyl Sepharose CL-4B, (ii) anion exchange chromatography on SOURCE 30Q, followed by (iii) a second hydrophobic interaction chromatography
Purification and properties of hepatic glutamine synthetases from the ureotelic gulf toadfish, <I>Opsanus beta</I>.
Walsh, P.J., et al.
Comp. Biochem. Physiol., B: Comp. Biochem., 115(4), 523-532 (1996)
Sheref S Mansy et al.
Nature, 454(7200), 122-125 (2008-06-06)
Contemporary phospholipid-based cell membranes are formidable barriers to the uptake of polar and charged molecules ranging from metal ions to complex nutrients. Modern cells therefore require sophisticated protein channels and pumps to mediate the exchange of molecules with their environment.
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