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Merck

E2511

Sigma-Aldrich

ExtrAvidin®

essentially salt-free, lyophilized powder

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.46

Form

essentially salt-free, lyophilized powder

Qualitätsniveau

Methode(n)

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

Versandbedingung

wet ice

Lagertemp.

2-8°C

Spezifität

Binding Activity: at least 10 μg biotin per mg

Anwendung

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

Biochem./physiol. Wirkung

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.

Sonstige Hinweise

A modified form of affinity purified egg white avidin.

Rechtliche Hinweise

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

Haftungsausschluss

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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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Demin Li et al.
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The tumor suppressor p53 is widely dysregulated in cancer and represents an attractive target for immunotherapy. Because of its intracellular localization, p53 is inaccessible to classical therapeutic monoclonal antibodies, an increasingly successful class of anticancer drugs. However, peptides derived from
Development of a T-cell Receptor Mimic Antibody against Wild-Type p53 for Cancer Immunotherapy
Li D, et al.
Cancer research, 77(10), 2699-2711 (2017)
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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