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Merck

E2511

Sigma-Aldrich

ExtrAvidin®

essentially salt-free, lyophilized powder

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About This Item

MDL號碼:
分類程式碼代碼:
12352203

形狀

essentially salt-free, lyophilized powder

品質等級

技術

dot blot: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
radioimmunoassay: suitable

運輸包裝

wet ice

儲存溫度

2-8°C

特異性

Binding Activity: at least 10 μg biotin per mg

應用

ExtrAvidin® has been used to tetramerize aliquots to generate HLA-A2 tetramers.

生化/生理作用

ExtrAvidin® is prepared from egg white avidin. It is a tetrameric protein containing four high affinity binding sites for biotin. It combines the high specific activity of avidin with the low background staining of streptavidin, a biotin binding protein produced by the bacteria Streptomyces avidinii. It binds biotin with the high affinity of egg white avidin, however, it does not exhibit the unwanted non-specific binding reported for egg white avidin at physiological pH, such as the staining of mast cells.

其他說明

A modified form of affinity purified egg white avidin.

法律資訊

ExtrAvidin is a registered trademark of Merck KGaA, Darmstadt, Germany

免責聲明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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Hanwei Gao et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(51), 20146-20151 (2008-12-17)
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E O'Connor et al.
Journal of immunological methods, 229(1-2), 155-160 (1999-11-11)
The ability to detect a protein is always limited to the sensitivity of the assays available. Progress in improving the sensitivity of protein detection will allow a more complete understanding of biological systems. Of particular interest to the field of
John E G McCarthy et al.
Methods in enzymology, 430, 247-264 (2007-10-05)
A growing number of biophysical techniques use immobilized reactants for the quantitative study of macromolecular reactions. Examples of such approaches include surface plasmon resonance, atomic force microscopy, total reflection fluorescence microscopy, and others. Some of these methods have already been

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