Thermo Scientific™ NeutrAvidin Protein

Description

• NeutrAvidin Protein is deglycosylated native avidin from egg whites
• Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties
• Purified and conjugated forms of NeutrAvidin Protein provide exceptional performance in Western blot, ELISA and IHC applications that require biotin-binding probes
• Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin
• Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles and amphibia
• The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons
• Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons
• Carbohydrate-based lectin-binding is reduced to undetectable levels, yet biotin-binding affinity is retained
• NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation
• NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin binding proteins
• The specific activity for biotin-binding is approximately 14μg/mg of protein, which is near the theoretical maximum activity.