bead size
40-125 μm (dry)
pore size
~30,000 Da exclusion limit
operating pH
2-10
capacity
2.6-3.4 meq/g ion exchange capacity
compatibility
mode of use strong anion exchange chromatography
Quality Level
Application
QAE Sephadex® is used in protein chromatography, ion exchange chromatography, anion exchange media, resins and separation media. QAE Sephadex® has been used to develop methods to detect copper in water samples, resveratrol in beer, and indomethacin in both pharmaceuticals and urine samples.
General description
Q25120-100G′s updated product number is GE17-0190-01
Legal Information
Sephadex is a registered trademark of Cytiva
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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3-deoxy-d-manno-2-octulosonic acid (KDO) is a component of rhamnogalacturonan II, a pectic polysaccharide in the primary cell walls of plants.
York, W.S., et al.
Carbohydrate Research, 138(1), 109-126 (1985)
Purification and Partial Characterization of Host-Specific Toxins Produced by <I>Periconia circinata</I>.
Wolpert, T.J., and Dunkle, L.D.
Phytopathology, 70, 872-876 (1980)
A B Cantor et al.
The Journal of biological chemistry, 267(32), 23349-23356 (1992-11-15)
Cathepsin D is a bilobed lysosomal aspartyl protease that contains one Asn-linked oligosaccharide/lobe. Each lobe also contains protein determinants that serve as recognition domains for binding of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, the first enzyme in the biosynthesis of the mannose 6-phosphate
Heterogeneous Reaction of Shattercane to <I>Periconia circinata</I> and its Host-Specific Toxin.
Dunkle, L.D.
Phytopathology, 69, 260-262 (1979)
A Varki et al.
Archives of biochemistry and biophysics, 222(1), 145-149 (1983-04-01)
An enzyme that is capable of removing the outer N-acetylglucosamine residues from phosphodiesters present on the high-mannose-type oligosaccharides of newly synthesized lysosomal enzymes has been described. This enzyme has been called an alpha-N-acetylglucosaminylphosphodiesterase, based upon its substrate specificity and on
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