O0511
Octyl−Sepharose™ 4 Fast Flow
Synonym(s):
Octyl–Agarose
extent of labeling
~5 μmol per mL
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
Quality Level
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
signalword
Danger
hcodes
Hazard Classifications
Flam. Liq. 2
Storage Class
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
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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
Sejong Oh et al.
Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association, 44(8), 1184-1190 (2006-06-24)
This study was carried out to evaluate the effect of bacteriocin produced by Lactococcus sp. HY 449 against skin-inflammatory bacteria such as Staphylococcus epidermidis ATCC 12228, Staphylococcus aureus ATCC 65389, Streptococcus pyogenes ATCC 21059, and Propionibacterium acnes ATCC 6919. The
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)
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
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
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