Q1754
Q Sepharose™ High Performance
preswollen, 24-44 μm (wet), average exclusion limit ~4,000,000 Da
Synonym(s):
Q Sepharose™
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About This Item
Recommended Products
form
preswollen
technique(s)
RNA extraction: suitable
matrix active group
, —CH2N+(CH3)3
particle size
24-44 μm (wet)
pore size
~4,000,000 Da average exclusion limit
pH
2—12
capacity
150-200 μeq/mL, gel
storage temp.
2-8°C
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Application
Q Sepharose™ is used in protein chromatography, ion exchange chromatography and anion exchange media. Q Sepharose™ has been used to study compounds of plant defense with applications for natural control of phytopathogenic fungi. Q Sepharose™ has also been used to develop an efficient method for extracting high-quality mRNA from soil and to study the immunomodulatory proteins from garlic (Allium sativum).
Physical form
Preswollen in 20% ethanol
Legal Information
Sepharose is a trademark of Cytiva
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
Certificates of Analysis (COA)
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Fatima Clement et al.
International immunopharmacology, 10(3), 316-324 (2009-12-17)
Garlic (Allium sativum), an important medicinal spice, displays a plethora of biological effects including immunomodulation. Although some immunomodulatory proteins from garlic have been described, their identities are still unknown. The present study was envisaged to isolate immunomodulatory proteins from raw
Carsten Mettel et al.
Applied and environmental microbiology, 76(17), 5995-6000 (2010-07-14)
Here, we report an efficient method for extracting high-quality mRNA from soil. Key steps in the isolation of total RNA were low-pH extraction (pH 5.0) and Q-Sepharose chromatography. The removal efficiency of humic acids was 94 to 98% for all
Suzana M Ribeiro et al.
Peptides, 32(5), 868-874 (2010-10-20)
Antifungal proteins and peptides, essential compounds for plant defense, have been isolated from several tissues of various plants. These proteins could be used as a natural alternative to control phytopathogenic fungi. In this report a heterodimeric antifungal protein named Pa-AFP1
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