Background:

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™.

Alkaline Phosphatase (Alk Phos) is an enzyme purified from bovine calf intestinal mucosa with a molecular weight of approximately 140 kDa.