DFF100
DEAE–Sepharose™
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Synonym(s):
Diethylaminoethyl–Sepharose™
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About This Item
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Quality Level
form
suspension
technique(s)
affinity chromatography: suitable
matrix
6% cross-linked agarose
bead size
45-165 μm (wet)
pore size
~4,000,000 Da exclusion limit
pH
2—12
capacity
110-160 μeq/mL binding capacity(gel volume)
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General description
DFF100-500Ml′s update product number is GE17-0709-01
Application
DEAE-Sepharose has been used in:
- anion exchange chromatography
- to screen polyisoprenyl phosphate phosphatase activity
- to purify isoinhibitors
- for the purification of human immunodeficiency virus (HIV)
- glycoprotein envelope (gp140 env)
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.
Biochem/physiol Actions
Diethylaminoethyl-sepharose (DEAE-sepharose) is a strong anion exchange column, where DEAE covalently binds to sepharose.
Legal Information
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
Regulatory Information
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Effective Purification Procedure of <I>Aspergillus oryzae</I> α−Amylase from Solid State Fermentation Cultures Including Concanavalin-A Sepharose
Terebiznik, M.R., et al.
Journal of Food Biochemistry, 19(5), 341-354 (1995)
Rapid high-level production of functional HIV broadly neutralizing monoclonal antibodies in transient plant expression systems
Rosenberg Y, et al.
Testing, 8(3), e58724-e58724 (2013)
Valérie Molinier-Frenkel et al.
Journal of virology, 76(1), 127-135 (2001-12-12)
The capacity of recombinant adenoviruses (rAd) to induce immunization against their transgene products has been well documented. In the present study, we evaluated the vaccinal adjuvant role of rAd independently of its vector function. BALB/c mice received one subcutaneous injection
Growth cone collapse and neurite retraction from cultured <I>Helisoma</I> neurons in response to antibody Fab fragments against an extracellular matrix protein.
Miller, J.D., et al.
Dev. Brain Res., 79(2), 203-218 (1994)
T M Schmidt et al.
Applied and environmental microbiology, 55(10), 2607-2612 (1989-10-01)
Luminescence of batch cultures of Xenorhabdus luminescens was maximal when cultures approached stationary phase; the onset of in vivo luminescence coincided with a burst of synthesis of bacterial luciferase, the enzyme responsible for luminescence. Expression of luciferase was aldehyde limited
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