UltraAvidin™- Horseradish Peroxidase (HRPO)
| Prod. No.: | A106 |
| Conc.: | 1.0 mg/ml |
| Pkg. Size: | 1.0 mg, 2.0 mg |
Description
Background:
UltraAvidin is Leinco Technologies' trademark for a uniquely modified form of avidin which is isolated from chicken egg whites. With a molecular weight of 60,000 there are four identical subunits each capable of binding one molecule of biotin. UltraAvidin from Leinco Technologies has been de-glycosylated to prevent carbohydrate moieties from adhering to lectin-like receptors on the surface of cells, thus eliminating the possibility of false positives. Unlike native avidin, UltraAvidin has a near neutral pI which prevents electrostatic interactions with negatively charged serum or membrane proteins.
Recent studies have identified a universal recognition sequence in streptavidin which is similar to that found in several adhesion receptors.1 Strong interactions have been shown with streptavidin and cell surface molecules. This universal recognition sequence is not present in UltraAvidin.
UltraAvidin has been covalently conjugated to Horseradish Peroxidase. The conjugate is then purified chromatographically to remove unconjugated enzyme and UltraAvidin.
Reporter Molecule:
Horseradish Peroxidase (HRPO) is an enzyme purified from horseradish root with a molecular weight of approximately 44 kDa.
Host Species
Chicken Egg White
Formulation
UltraAvidin-HRPO is supplied in 0.01M phosphate buffered saline (PBS) pH 7.4, containing 1.0% BSA, and 0.01% thimerosol as a preservative. (Warning: Use of sodium azide as a preservative will inhibit the enzyme activity of horseradish peroxidase)
Source
Chicken Egg White
Storage and Stability
Stable when stored at 2 - 8°C. Do not freeze
Specific Activity
11-17 µg biotin bound/mg UltraAvidin™
Isoelectric Point
pI= 6.3 +/- 0.3
Applications and Suggested Working Dilutions
Western blotting: 1:5,000 - 1:10,000
ELISA: 1:5,000 - 1:20,000
Immunohistochemistry: 1:100 - 1:1,000
Western blotting and ELISA Chemiluminescent: 1:20,000 - 1:100,000
However, each investigator should determine their own optimal working dilution for each specific research application.
Country of Origin
USA
References
1. Alon, R., Bayer, E. A., and Wilchek, M.1 (1990) "Streptavidin Contains An RYD Sequence Which Mimics The RGD Receptor Domain Of Fibronectin" Biochemical and Biophysical Research Communications 170:1236-1241
Related Products
Products are for research use only. Not for use in diagnostic or therapeutic procedures.
