 Thermo Scientific Immobilized NeutrAvidin Products are superior alternatives to avidin and streptavidin agarose and acrylamide beaded affinity resins. NeutrAvidin Protein is a modified avidin derivative that combines several key features to provide a biotin-binding protein with exceptionally low nonspecific binding properties. Native avidin is heavily glycosylated resulting in its high pI ad nonspecific binding properties. By contrast NeutrAvidin Protein contains no carbohydrate and has a near-neutral isoelectric point (6.3) features that provide for very low nonspecific binding and broader utility in a variety of applications.
NeutrAvidin Resins are prepared by covalently coupling NeutrAvidin Protein to the beaded agarose or UltraLink Biosupport using efficient and stable chemistries resulting in NeutrAvidin Agarose and UltraLink Resins that are resistant to leaching and stable at pH 2-11. The products are excellent choices for a variety of small- or large-scale affinity purification applications involving biotinylated macromolecules including separation of biotinylated molecules from samples and immunoprecipitation of antigens using biotin-labeled antibodies. To determine the best reagent to biotinylate a protein or other biomolecule visit the Biotinylation Reagent Selection Guide. Comparison of biotin-binding proteins. | | | Biotin-Binding Protein | Avidin | Streptavidin | NeutrAvidin | Molecular Weight | 67K | 53K | 60K | Biotin-binding Sites | 4 | 4 | 4 | Isoelectric Point (pI) | 10 | 6.8-7.5 | 6.3 | Specificity | Low | High | Highest | Affinity for Biotin (Kd) | 10-15 M | 10-15 M | 10-15 M | Nonspecific Binding | High | Low | Lowest |
Highlights: - Low nonspecific binding – Unlike avidin NeutrAvidin Protein has no carbohydrates eliminating nonspecific binding problems caused by sugars; unlike streptavidin NeutrAvidin Protein has no Arg-Tyr-Asp sequence which can be a source of binding to cell surface molecules.
- Proven coupling chemistries – The methods used to prepare these resins are superior to typical cyanogen bromide (CNBr) immobilization providing high functionality low nonspecific binding and excellent resistance to leaching.
- Versatile resins – Agarose (polysaccharide-based) and UltraLink Biosupport (acrylamide-based) resins provide two different options fo particular experimental conditions and are compatible with gravity-flow spin and FPLC methods.
- Available in multiple formats – Choose from two resin types regular or high capacity preparations and small or large-scale package sizes (bulk sizes are also available).
- Superior performance – High Capacity Resin has higher binding capacity than best alternative supplier streptavidin products allowing use of small amounts of resin for experiments.
Related Products:Streptavidin Agarose and UltraLink Resins
Avidin Agarose Resin
Pierce Monomeric Avidin Resins and Kit
Purified NeutrAvidin and NeutrAvidin Conjugates
NeutrAvidin Coated Plates References:- Butler J.E. et al. (1992). Methods for detection of a triplet repeat block and a functional mismatch binding protein in a biological fluid sample. J. Immunol. Meth. 150 77-90.
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- Lesa G.M. et al. (2000). The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein. J. Biol. Chem. 275 2831-2836.
- Liaw P.C.Y. et al. (2001). Identification of the potein C/activated protein C binding sites on the endothelial cell protein C receptor. J. Biol Chem. 276 8364-8370.
- Murakami T. et al. (2000). The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proc. Natl. Acad. Sci. USA97 343-348.
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