Thermo Scientific NeutrAvidin Agarose is a standard-capacity beaded agarose resin of immobilized NeutrAvidin Protein, a modified form of avidin with exceptional biotin-binding characteristics for affinity purification methods.
NeutrAvidin Agarose consists of a specially purified and deglycosylated form of avidin that has been covalently immobilized onto high-quality crosslinked 6% beaded agarose. Compared to native avidin, NeutrAvidin protein is more neutral and exhibits much less nonspecific binding properties in biotin-binding applications. The agarose beads have physical and chemical properties that enable them to be used in a variety of batch- or column-type affinity procedures. Generally, NeutrAvidin products function as well or better than their streptavidin counterparts and are less expensive.
- NeutrAvidin protein – purified, deglycosylated avidin protein (60kDa, pI 6.3); tetrameric with four biotin-binding site per molecule
- Agarose resin – support is crosslinked 6% beaded agarose (CL-6B), the most popular resin for protein affinity purification methods
- Inert and stable – NeutrAvidin protein is immobilized by charge-free, leach-resistant covalent bonds, resulting in low nonspecific binding and enabling multiple uses without decline in yield
- Standard capacity – this variety of beads has a normal load of immobilized NeutrAvidin protein, providing a binding capacity of 1 to 2mg of biotinylated BSA per mL of resin
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. NeutrAvidin resins are prepared by covalently coupling the protein using efficient and stable chemistries, resulting in supports 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.
Comparison of available Thermo Scientific NeutrAvidin Resins. Binding-capacity specifications (Capacity) are expressed as milligrams of biotinylated BSA bound per milliliter of resin. Capacity values in parentheses are estimates because these products are not tested using biotinylated BSA. Store all resins in water or buffer at 4°C; do not freeze. Also consider our Streptavidin Resins.
|Crosslinked 6% beaded agarose
||1 to 2mg
|Crosslinked 6% beaded agarose
|Co-polymer of crosslinked bisacrylamide and azlactone
||(1 to 2mg)
|NeutrAvidin Plus UltraLink Resin
||Co-polymer of crosslinked bisacrylamide and azlactone
Properties of crosslinked 6% beaded agarose (CL-6B):
- Support pH Stability: 2 to 14 (short term); 3 to 13 (long term)
- Average Particle Size: 45 to 165 microns
- Exclusion Limit: 10,000 to 4,000,000 daltons
- Maximum Volumetric Flow Rate: approx. 1mL/minute (for 1cm diameter column)
- Maximum Linear Velocity: 30cm per hour
- Maximum Pressure: less than 25psi (1.5 bar)
Comparison of biotin-binding proteins.
|Isoelectric Point (pI)
|Affinity for Biotin (Kd)
References (all NeutrAvidin Resins):
- 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.
- Cernuda-Morollon, E., et al. (2001). 15-deoxy-delta 12. 14-prostaglandin J2 inhibition of NF-kappa B-DNA binding through covalent modification of p50 subunit. J. Biol. Chem. 276 , 35530-35536.
- Conti, L.R., et al. (2001). Transmembrane topology of the sulfonylurea receptor SUR1. J. Biol. Chem. 276 , 41270-41278.
- Daniels, G.M. and Amara, S.G. (1998). Selective labeling of neurotransmitter transporters at the cell surface. Methods. Enzymol. 296 , 307-318.
- Hiller, Y., et al. (1987). Biotin binding to avidin. Oligosaccharide side chain not required for ligand association. Biochem. J. 248 , 167-171.
- Kim, K., et al. (2001). N -Acetylcysteine Induces Cell Cycle Arrest in Hepatic Stellate Cells through Its Reducing Activity. J. Biol. Chem. 276 , 40591-40598.
- Leighton, B.H., et al. (2002). A hydrophobic domain in glutamate transporters forms an extracellular helix associated with the permeation pathway for substrates. J. Biol. Chem. 277 , 29847-29855.
- 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 protein 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.
- Oda, Y, et al. (2001). Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nature Biotechnology 19 , 379-382.
- Trotti, D., et al. (2001). Amyotrophic lateral sclerosis-linked glutamate transporter mutant has impaired glutamate clearance capacity. J. Biol. Chem. 276 , 576-582.
Other Biotin-binding Affinity Resins
Purified NeutrAvidin Protein and Conjugates
NeutrAvidin Coated Plates