UltraAvidin- Horseradish Peroxidase

UltraAvidin is Leinco Technologies' trademark for a uniquely modified form of avidin which is isolated from chicken egg whites (Also Known As: NeutrAvidin).

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 deglycosylated 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. Avidin binds to biotin with high affinity and similar to Streptavidin.

UltraAvidin-HRP is useful for detecting biotinylated antibodies, e.g., in ELISA or Western blotting.