UltraAvidin™- Alkaline Phosphatase

UltraAvidin™ is Leinco Technologies' 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™ may not significantly increase sensitivity in all research systems but it will assure specificity.

UltraAvidin™ has been covalently conjugated to Alkaline Phosphatase from calf mucosa. The conjugate is then purified chromatographically to remove unconjugated enzyme and UltraAvidin™.

UltraAvidin™-Alkaline Phosphatase (Alk. Phos.) is supplied in 0.05M Tris pH 8.0, containing .001M MgCl_{2</sub), .0001M ZnCl2, 1.0% BSA and 0.09% sodium azide as a preservative.}

UltraAvidin™-Alkaline Phosphatase can be used to detect biotinylated biological probes such as antibodies or cytokines in a variety of applications such as protein blotting, immunohistochemistry or ELISA.

The suggested working concentration for ELISA, immunohistochemistry and western blotting is approximately 0.1 - 2.0 µg/ml. However, each investigator should determine their own optimal working dilution for each specific research application.

This Alkaline Phosphatase conjugate is stable when stored at 2-8°C. Do not freeze

Next Day 2-8°C

1. Wilchek, M. et al.(1990) Biochem Biophys Res Commun. 1990 170(3):1236-41.