O0511
辛基-琼脂糖
别名:
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
存储类别
3 - Flammable liquids
wgk
WGK 3
flash_point_f
57.2 °F - closed cup
flash_point_c
14.0 °C - closed cup
法规信息
危险化学品
此项目有
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
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
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
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