Thermo Scientific NeutrAvidin UltraLink Resin is a beaded polyacrylamide resin of immobilized NeutrAvidin Protein, a modified form of avidin with exceptional biotin-binding characteristics for affinity purification methods.
NeutrAvidin UltraLink Resin consists of a specially purified and deglycosylated form of avidin that has been covalently immobilized onto a beaded acrylamide support. Compared to native avidin, NeutrAvidin protein is more neutral and exhibits much less nonspecific binding properties in biotin-binding applications. UltraLink beads are hydrophilic, charge-free, highly crosslinked, rigid and durable. These properties make the affinity resin suitable for a variety of batch- or column-type affinity procedures that require medium-pressure chromatography. The resin provides an alternative to agarose supports when situations demand it. 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
- UltraLink Resin – acrylamide-based support provides an alternative to crosslinked beaded agarose supports for medium-pressure applications
- 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 Thermo Scientific UltraLink Resin:
- Support pH Stability: 1 to 13
- Average Particle Size: 50 to 80 microns
- Exclusion Limit: greater than 2,000,000 daltons
- Average Surface Area: greater than 250m2 per gram of beads
- Average Pore Volume: greater than 1.2mL per gram of beads (>60% of bead volume)
- Pore Size: 500 to 1000 angstroms (50 to 100nm)
- Maximum Linear Velocity: 3000cm per hour
- Maximum Pressure: 100psi (6.9 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