DCL6B100
DEAE–Sepharose™
CL-6B
Synonym(s):
Diethylaminoethyl–Sepharose™
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50 ML
₪928.00
100 ML
₪1,626.00
₪928.00
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50 ML
₪928.00
100 ML
₪1,626.00
About This Item
₪928.00
Please contact Customer Service for Availability
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Quality Level
form
suspension
technique(s)
affinity chromatography: suitable
matrix
6% cross-linked agarose
bead size
45-165 μm
pore size
~4,000,000 Da exclusion limit
pH
3—12
capacity
130-170 μeq/mL binding capacity (gel volume)(gel volume)
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General description
DCL6B100-500ML′s updated product number is GE17-0710-01
Application
DEAE-Sepharose® is used in affinity chromatography, protein chromatography and ion exchange chromatography. DEAE-Sepharose™ has been used to study pathogenesis of human disease and to develop a new assay for detecting the toxins of pathogenic strains of Clostridium difficile.
Legal Information
DEAE-Sepharose is a registered trademark of Cytiva
Sepharose is a trademark of Cytiva
replaced by
Product No.
Description
Pricing
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 3
Storage Class Code
3 - Flammable liquids
WGK
WGK 1
Flash Point(F)
100.4 - 109.4 °F
Flash Point(C)
38 - 43 °C
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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R K Sinha et al.
Vaccine, 15(6-7), 689-699 (1997-04-01)
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I Yu Bakunina et al.
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An alpha-N-acetylgalactosaminidase IV able to remove blood type specificity of human A(II)-erythrocytes and not effecting B(III)-erythrocytes was isolated from the marine bacterium Arenibacter latericius KMM 426T. The alpha-N-acetylgalactosaminidase IV preparation exhibits high activity during inhibition of hemagglutination with blood group
J J Wheeler et al.
Gene therapy, 6(2), 271-281 (1999-08-06)
A detergent dialysis procedure is described which allows encapsulation of plasmid DNA within a lipid envelope, where the resulting particle is stabilized in aqueous media by the presence of a poly(ethyleneglycol) (PEG) coating. These 'stabilized plasmid-lipid particles' (SPLP) exhibit an
M A Heine et al.
Molecular biology of the cell, 4(11), 1189-1204 (1993-11-01)
Epitope-tagged Xenopus nucleolin was expressed in Escherichia coli cells and in Xenopus oocytes either as a full-length wild-type protein or as a truncation that lacked the distinctive carboxy glycine/arginine-rich (GAR) domain. Both full-length and truncated versions of nucleolin were tagged
M Vasseur
Bioscience reports, 9(3), 341-346 (1989-06-01)
The rabbit intestinal sucrase-isomaltase complex has been purified to homogeneity after solubilization with Triton X 100 followed by chromatography on DEAE Sepharose CL 6B and a second solubilization with papain. After hydrophobic chromatography on Octyl Sepharose CL 6B, separation from
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