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Merck

E2511

Sigma-Aldrich

ExtrAvidin®

essentially salt-free, lyophilized powder

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.46

Forma

essentially salt-free, lyophilized powder

Minőségi szint

technika/technikák

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

kiszállítva

wet ice

tárolási hőmérséklet

2-8°C

Egyediség

Binding Activity: at least 10 μg biotin per mg

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Egyéb megjegyzések

A modified form of affinity purified egg white avidin.

Jogi információk

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

Jogi nyilatkozat

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.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


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Dokumentumtár megtekintése

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Li D, et al.
Cancer research, 77(10), 2699-2711 (2017)
Demin Li et al.
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Hanwei Gao et al.
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Surface plasmon polaritons (SPPs) are responsible for exotic optical phenomena, including negative refraction, surface enhanced Raman scattering, and nanoscale focusing of light. Although many materials support SPPs, the choice of metal for most applications has been based on traditional plasmonic
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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