DCL6B100
DEAE–Sepharose™
CL-6B
Synonym(s):
Diethylaminoethyl–Sepharose™
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RM 1,524.00
100 ML
RM 2,531.00
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50 ML
RM 1,524.00
100 ML
RM 2,531.00
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RM 1,524.00
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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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Preparative affinity precipitation of L-lactate dehydrogenase.
Pearson, J.C., et al.
Journal of Biotechnology, 11(2-3), 267-274 (1989)
I A Oussenko et al.
Journal of bacteriology, 182(9), 2639-2642 (2000-04-13)
Studies of Bacillus subtilis RNases that are involved in mRNA degradation reveal a different pattern from that of Escherichia coli. A strain lacking polynucleotide phosphorylase, the major 3'-to-5' exoribonuclease activity in cell extracts, is viable. Here, we show that the
A. Serrano et al.
Plant physiology, 106(1), 87-96 (1994-09-01)
Highly purified plasma membrane fractions were obtained from onion (Allium cepa L.) roots and used as a source for purification of redox proteins. Plasma membranes solubilized with Triton X-100 contained two distinct polypeptides showing NAD(P)H-dependent dehydrogenase activities. Dehydrogenase I was
M L Zapp et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(17), 7734-7738 (1991-09-01)
The Rev protein of human immunodeficiency virus type 1 is a sequence-specific RNA binding protein that is essential for viral replication. Here we present evidence that Rev is a stable oligomer both in vitro and in vivo. Analysis of Rev
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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