Thermo Scientific Maleimide-Activated NeutrAvidin Protein is a specially-prepared form of avidin that decreases background in biotin-binding.
Features of NeutrAvidin Protein:
• Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin
• Nearly devoid of glycosylation—decreased possibility of lectin binding compared to native avidin
• No RYD recognition sequence—no known off-target binding domains like streptavidin
• Affordable—significantly less expensive than streptavidin
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. Conjugated NeutrAvidin Protein provides 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 14 μg/mg of protein, which is near the theoretical maximum activity.
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| Code | Description |
|---|---|
| 31007 | Catalog Number: 31007 |
