BioVision Introduces Hi-Bind™ Protein A Agarose & Hi-Bind™ Protein G Agarose

MILPITAS, Calif. - Sept. 30, 2013 - PRLog -- Proteins A and G have been widely used for IgG purification. BioVision’s Protein A and G resins consist of purified recombinant protein A & G respectively that have been covalently coupled to 6% cross-linked Agarose/Sepharose beads. The recombinant protein A and G contain only IgG binding domains and are purified from E. coli via multiple chromatographic steps (not affinity purified with human IgG). The albumin binding domain, cell wall binding domain and other non-specific regions have been removed to ensure the maximum specific IgG binding. 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 used for affinity purification or detection using anti-His-tag antibodies. These resins are available in several convenient pack sizes and can be regenerated and reused multiple times when stored properly.

Hi-Bind™ Protein A-Agarose (Catalog #: 6520-1, 5, 25, 100) and Hi-Bind™ Protein G-Agarose (Catalog #: 6513-1, 5, 25, 100) - 1 ml, 5 ml, 25 ml, 100 ml: BioVision has performed extensive research to prepare these special Hi-Bind™ protein A & Hi-Bind™ protein G-Agarose beads that give a higher binding capacity for IgG, higher flow rate & minimal leaching of the ligand than the other regular Protein A & Protein G-Agarose on the market. The IgG binding capacity of Hi-Bind^TM Protein A-Agarose and Hi-Bind^TM Protein G-Agarose are ≥ 36 mg and ≥ 30 mg respectively for human or rabbit IgG per ml of wet beads. These Hi-Bind^TM beads display high chemical and physical stability as well as show high flow rate, hydrophilicity and high gel strength.

Relevance/Importance
· Purification of broad range of monoclonal and polyclonal antibodies.
· Isolation and purification of IgG from serum, culture media, ascites fluid or hybridoma supernatants.
· Isolation and purification of antigens and immune complexes by immune co-precipitation.
· Depletion of immunoglobulins from serum, culture media, ascites fluid or hybridoma supernatants.

Key Features of Protein A and Protein G resins
· Enhanced Specificity: BioVision Recombinant Protein A and Protein G contain only IgG-binding regions of native Protein A and native Protein G respectively. The cell wall binding region, albumin binding region and other non-specific regions have been eliminated to ensure the maximum specific IgG binding.
· High Binding Capacity and High Flow Rate: Lower molecular weight of the affinity protein permits higher density of its immobilization and elevated capacity
· Minimal leaching of the ligand: Our conjugation chemistry ensures stable immobilization that prevents loss of immobilized affinity proteins during elution and regeneration of the beads
· Versatility: Binds a broad range of IgG species and subclasses
· Durability: Can be regenerated and reused multiple times without deterioration of performance
· Convenience: Available in multiple sizes to match all your needs

For more information, please visit
http://www.biovision.com/search/results.html?keywords=hi-bind&x=0&y=0

For our complete range of Protein A/G/L & Affinity Conjugates & Related Products, please visit
http://www.biovision.com/protein-a-g-l-affinity-conjugates-related-products-1368/