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E2761

Sigma-Aldrich

ExtrAvidin®−FITC

buffered aqueous solution

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MDL number:
NACRES:
NA.46

conjugate

FITC conjugate

Quality Level

form

buffered aqueous solution

extent of labeling

3-6 mol fluorochrome per mol protein

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 20 μg/mL using human tissues
indirect immunofluorescence: 1:200

shipped in

dry ice

storage temp.

−20°C

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This Item
E2636A2050E4011
ExtrAvidin®−FITC buffered aqueous solution

E2761

ExtrAvidin®−FITC

Avidin–FITC from egg white buffered aqueous solution

A2050

Avidin–FITC from egg white

ExtrAvidin®−R-Phycoerythrin buffered aqueous solution

E4011

ExtrAvidin®−R-Phycoerythrin

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

shipped in

dry ice

shipped in

wet ice

shipped in

dry ice

shipped in

-

conjugate

FITC conjugate

conjugate

alkaline phosphatase conjugate

conjugate

FITC conjugate

conjugate

phycoerythrin (R-PE) conjugate

extent of labeling

3-6 mol fluorochrome per mol protein

extent of labeling

-

extent of labeling

3-5.5 mol fluorochrome per mol protein

extent of labeling

1-4 mol PE per mol ExtrAvidin®

General description

Avidin is a tetrameric or dimeric biotin-binding protein produced in the oviducts of birds, reptiles and amphibians and deposited in the whites of their eggs. It consists of four high affinity binding sites for biotin. ExtrAvidin is prepared from egg white avidin. It is a modified form of affinity purified avidin and combines high specific activity of avidin with the low background staining of streptavidin. It is a biotin binding protein produced by the bacteria Streptomyces avidinii. ExtrAvidin has been conjugated to fluorescein isothiocyanate (FITC) and is used for various techniques.

Application

ExtrAvidin®-FITC is suitable for the following applications:
  • immunohistochemistry (formalin-fixed, paraffin-embedded sections) at a concentration of 20μg/mL using human tissues.
  • Immunofluorescence
  • competitive binding assay

Physical form

Solution in 0.01 M phosphate buffered saline, containing 10% (v/v) 0.5 M carbonate buffer, pH 9.5, and 15 mM sodium azide

Preparation Note

Affinity purified protein

Legal Information

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

Disclaimer

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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D R Hampson et al.
The Journal of biological chemistry, 274(47), 33488-33495 (1999-11-24)
Metabotropic glutamate receptors (mGluRs) are G-protein-coupled glutamate receptors that subserve a number of diverse functions in the central nervous system. The large extracellular amino-terminal domains (ATDs) of mGluRs are homologous to the periplasmic binding proteins in bacteria. In this study
Expression and localization of urokinase-type plasminogen activator receptor in bovine cumulus--oocyte complexes
Garcia DC
Zygote, 24, 230-235 (2016)
Xueying Wang et al.
eLife, 3, e03427-e03427 (2014-07-17)
To understand the neural origins of rhythmic behavior one must characterize the central pattern generator circuit and quantify the population size needed to sustain functionality. Breathing-related interneurons of the brainstem pre-Bötzinger complex (preBötC) that putatively comprise the core respiratory rhythm
Therapeutic monoclonal antibodies for Ebola virus infection derived from vaccinated humans
Rijal P, et al.
Cell Reports, 27, 172-186 (2019)
R S Schwartz et al.
The Biochemical journal, 327 ( Pt 2), 609-616 (1997-11-14)
We report the cloning and sequencing from human reticulocytes of cDNA coding for the Cl- channel-associated protein, pICln. Human reticulocyte pICln (HRpICln) cDNA encodes a protein (predicted molecular mass 26293Da) identical with human non-pigmented ciliary epithelial cell pICln. By using

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