O0511
Octyl−Sepharose™ 4 Fast Flow
Synonym(s):
Octyl–Agarose
extent of labeling
~5 μmol per mL
Quality Level
matrix
agarose, 4% cross-linked
matrix activation
epichlorohydrin
matrix attachment
ether
matrix spacer
3 atoms
particle size
45-165 μm
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
General description
O0511-200ML′s updated product number is GE17-0946-02
Application
Octyl Sepharose™ is used in hydrophobic interaction media, resins and separation media. Octyl Sepharose™ has been used to determine the population of Acinetobacter species in sewage treatment plants.
Physical form
Suspension in 20% ethanol
Legal Information
Sepharose is a trademark of Cytiva
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 2
Storage Class Code
3 - Flammable liquids
WGK
WGK 3
Flash Point(F)
57.2 °F - closed cup
Flash Point(C)
14.0 °C - closed cup
Regulatory Information
危险化学品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
L De Bellis et al.
Plant physiology, 123(1), 327-334 (2000-05-12)
A novel pumpkin (Cucurbita pepo) short-chain acyl-coenzyme A (CoA) oxidase (ACOX) was purified to homogeneity by hydrophobic-interaction, hydroxyapatite, affinity, and anion-exchange chromatography. The purified enzyme is a tetrameric protein, consisting of apparently identical 47-kD subunits. The protein structure of this
Mats Sandgren et al.
Protein science : a publication of the Protein Society, 12(4), 848-860 (2003-03-22)
As part of a program to discover improved glycoside hydrolase family 12 (GH 12) endoglucanases, we have studied the biochemical diversity of several GH 12 homologs. The H. schweinitzii Cel12A enzyme differs from the T. reesei Cel12A enzyme by only
K Bhardwaj et al.
Plant physiology, 127(4), 1728-1738 (2001-12-18)
A thermally stable lipase (EC 3.1.1.3.) was first identified in rice (Oryza sativa) bran, and the enzyme was purified to homogeneity using octyl-Sepharose chromatography. The enzyme was purified to 7.6-fold with the final specific activity of 0.38 micromol min(-1) mg(-1)
Sunil Shekar et al.
Plant physiology, 128(3), 988-996 (2002-03-14)
The soluble fraction of immature peanut (Arachis hypogaea) was capable of dephosphorylating [(3)H]lysophosphatidic acid (LPA) to generate monoacylglycerol (MAG). The enzyme responsible for the generation of MAG, LPA phosphatase, has been identified in plants and purified by successive chromatography separations
Youliang Huang et al.
Lipids, 39(3), 251-257 (2004-07-06)
An extracellular lipase (EC 3.1.1.3) from Geotrichum marinum was purified 76-fold with 46% recovery using Octyl Sepharose 4 Fast Flow and Bio-Gel A 1.5 m chromatography. The purified enzyme showed a prominent band on SDS-PAGE and a single band on
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service