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™.