BioVision presents a broad array of Agarose, Sepharose & Magnetic beads coupled to Protein A, Protein G, Protein L, Protein A/G, Protein A/G/L or Jacalin. These are each effective in the purification of monoclonal and polyclonal antibodies from culture media, serum, ascites fluid or hybridoma supernatants, and help to identify antibody/antigen complexes in immunoprecipitation experiments.
Additionally, BioVision also provides Glutathione and Heparin-Sepharose, which are typically utilized for purifying GST-tagged fusion proteins and heparin-binding proteins, respectively.
Antibody Purification Resins
Proteins A, G and L have been broadly utilized for purifying IgG. BioVision’s Protein A, G and L resins are constituted by purified recombinant protein A, G & L, respectively, each of which has been covalently coupled to 6% cross-linked Agarose/Sepharose beads.
The recombinant proteins A and G solely comprise IgG binding domains and are purified from E. coli following various chromatographic stages (not affinity purified with human IgG). The albumin binding domain, cell wall binding domain and other non-specific regions have been extracted to guarantee optimally specific IgG binding.
In contrast to Protein A and Protein G, which bind principally through Fc regions (i.e., heavy chain) of immunoglobulin, Protein L binds Igs via interactivity with the light chains. The recombinant Protein L comprises only Kappa light chain binding region and is therefore able to bind a broader range of Ig categories (IgG, IgM, IgA, IgE and IgD) and subcategories.
Single chain variable fragments (ScFv) and Fab fragments also bind to Protein L. Purity of these recombinant proteins is > 98% by SDS-PAGE and HPLC. Endotoxin level is < 0.1 EU/mg of Protein. The 6-His-tag on N-terminus can be implemented for affinity purification or identification utilizing anti-His-tag antibodies.
BioVision has undertaken considerable research to generate noteworthy Hi-BindTM protein A & Hi-BindTM protein G-Agarose beads. These provide a higher binding capacity for IgG, higher flow rate & lower leaching of the ligand than other available regular Protein A & Protein G-Agarose. The Protein A, G and L resins exhibit high chemical and physical stability, alongside high flow rate, hydrophilicity & high gel strength. These resins can be obtained in various convenient unit sizes, and can be regenerated and reutilized several times if stored correctly.
Protein Purification Resins
The study of protein regulation, structure & function is strengthened by the expression and purification of recombinant proteins. A high proportion of the recombinant proteins are expressed as fusion proteins with short affinity tags, or small proteins, such as GST. GST specifically binds to reduced glutathione. BioVision’s Glutathione-Sepharose® is produced by covalently coupling glutathione to epoxy-activated 4% cross-linked sepharose beads to constitute a secure thioether linkage.
Heparin-Sepharose® is regularly utilized in the purification of serum proteins such as coagulation factors, lipases, lipoproteins, hormone receptors and growth factors. BioVision’s Heparin-Sepharose® is produced by covalently coupling heparin to epoxy-activated 6% cross-linked sepharose beads. The coupling methodology for Glutathione and Heparin-Sepharose® is enhanced to display high binding capacity ( ≥ 5 mg GST/ml Glutathione-Sepharose resin & ≥ 0.4 mg heparin-binding protein/ml of Heparin-Sepharose® resin), high flow rate & minimal leaching of the ligand.
BioVision, Inc., is a privately held Life Science company headquartered in the beautiful San Francisco Bay Area.
BioVision develops and offers a wide variety of products including assay kits, antibodies, recombinant proteins & enzymes, and other innovative research tools for studying Apoptosis, Metabolism, Cell Proliferation, Cellular Stress, Cell Damage and Repair, Diabetes, Obesity and Metabolic Syndrome, Stem Cell Biology, Gene Regulation, Signal Transduction, etc. BioVision's products are currently being sold in more than 60 countries worldwide.
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