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E4011

ExtrAvidin®−R-Phycoerythrin

buffered aqueous solution

Synonym(s):

R-Phycoerythrin

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
MFCD00163600

Key Documents

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Product Name

ExtrAvidin®−R-Phycoerythrin, buffered aqueous solution

conjugate

phycoerythrin (R-PE) conjugate

form

buffered aqueous solution

storage condition

protect from light

extent of labeling

1-4 mol PE per mol ExtrAvidin®

technique(s)

flow cytometry: suitable using human peripheral blood lymphocytes with biotinylated antibody
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 5 μg/mL using human tissues

storage temp.

2-8°C

Quality Level

200

Application

ExtrAvidin®-R-Phycoerythrin has been used
  • In flow cytometric analysis to confirm membrane expression of ncamp-1 (cationic oligodeoxynucleotide binding protein).
  • In indirect immunofluorescence.
  • In Western blotting.

The ExtrAvidin-R-Phycoerythrin (PE) conjugate may be used in conjunction with biotinylated reagents in the avidin/biotin labeling system in flow cytometry.

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.

General description

ExtrAvidin is a chemically modified protein purified from egg whites.
The extravidin-R-phycoerythrin protein can be conjugated with fluorescein-labelled arylacetamide, a κ opioid ligand and biotin-conjugated anti-fluorescein IgG to identify the subpopulations of thymocytes that express κ opioid receptor. This product has shown specificity for rabbit anti-avidin in immunoelectrophoresis analysis.
ExtrAvidin, a uniquely modified avidin reagent, combines the high specific activity and sensitivity of avidin with the low background staining of streptavidin. Avidin consists of four identical subunits, each containing a single biotin binding site.

Immunogen

Thymocytes present in C57BL mice.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide

Legal Information

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

Storage Class

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

含少量动物源组分生物产品
常规特殊物品
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Certificates of Analysis (COA)

Lot/Batch Number
0000406692
0000372608
0000221256
0000307910
0000202680

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D M Lawrence et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(4), 1062-1066 (1995-02-14)
A method to visualize the kappa opioid receptor is described that uses a high-affinity fluorescein-conjugated opioid ligand and indirect immunofluorescence with the phycoerythrin fluorophore to amplify the signal. The mouse thymoma cell line R1E/TL8x.1.G1.OUAr.1 (R1EGO), which expresses the kappa 1
Molecular characterization of a novel pattern recognition protein from nonspecific cytotoxic cells: sequence analysis, phylogenetic comparisons and anti-microbial activity of a recombinant homologue
Evans DL, et al.
Developmental and Comparative Immunology, 29(12), 1049-1064 (2005)
Detection of opioid receptors on murine lymphocytes by indirect immunofluorescence: mature normal and tumor bearing mice lymphocytes
Karaji AG, et al.
International Immunopharmacology, 5(6), 1019-1027 (2005)
T A Ignatowski et al.
The Journal of pharmacology and experimental therapeutics, 284(1), 298-306 (1998-01-22)
Recent studies have shown kappa opioid receptor labeling on the R1EGO thymoma cell line by indirect immunofluorescence and flow cytometric analysis. The present study used a fluorescein-labeled arylacetamide (FITC-AA), a kappa opioid ligand, in conjunction with biotin-conjugated anti-fluorescein IgG and
In vitro binding of HFE to the cation-independent mannose-6 phosphate receptor
Schimanski LM, et al.
Blood Cells, Molecules and Diseases, 43(2), 180-193 (2009)
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