Thermo Scientific™ NAb™ Protein A/G Spin Column, 5 mL

Affinity purify antibodies (IgG) with versatile, recombinant Protein A/G agarose offered in bottles, spin columns, filter plates and complete purification kits.

Supplier:  Thermo Scientific™ 89962

Catalog No. PI89962

Description

Thermo Scientific™ Pierce Protein A/G Agarose is a versatile, high-performance affinity resin for antibody purification that is available as bottled agarose beads, pre-packed spin columns, chromatography cartridges and complete IgG purification kits.

Pierce Protein A/G Agarose binds nearly all isotypes and mammalian species of IgG from serum, ascites fluid, cell culture supernantant and other antibody samples, thereby enabling effective antibody purification. Because the immobilized Protein A/G combines the immunoglobulin-binding domains of both Protein A and Protein G, the resin is effective for affinity purification of IgG antibodies from a broad range mammalian host species.

Pierce Protein A/G Agarose consists of purified Protein A/G recombinant fusion protein that has been covalently immobilized onto high-quality crosslinked 6% beaded agarose (CL-6B). This premiere variety of the resin provides the most versatile combination of chromatographic features for high yield and high purity purification of whole IgG from mammalian serum samples. The agarose beads have physical and chemical properties suitable for many affinity purification systems. Accordingly, Pierce Protein A/G Agarose is offered in several convenient package formats, including bottled resin slurries, three sizes of spin columns, complete purification kits, two sizes of FPLC-ready chromatography cartridges, and 96-well filter plates.

Highlights:

• Protein A/G – immobilized recombinant fusion protein of the antibody-binding domains of Protein A and Protein G enables polyclonal IgG purification from nearly any mammalian species

• Agarose resin – support is crosslinked 6% beaded agarose (CL-6B), the most popular resin for protein affinity purification methods

• Inert and stable – superior manufacturing method immobilizes Protein A/G by charge-free, leach-resistant covalent bonds, resulting in low nonspecific binding and enabling multiple uses without decline in yield

• Standard capacity – Pierce Protein A/G Agarose has a normal load of immobilized Protein A/G, providing a binding capacity greater than 7mg human IgG/mL resin

• Multiple formats – choose from bottled resin slurries, centrifuge-ready columns, complete purification kits and two sizes of FPLC-ready chromatography cartridges

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), defined as the maximum pressure drop across a column that the resin can withstand (Note: The indicated gauge pressure of a liquid chromatography apparatus may be measuring the total system pressure rather than the pressure drop across the column.)

Available Formats:

• Resin Slurries: 3mL and 15mL bottles
• Spin Columns: 0.2mL (microcentrifuge), 1mL, 5mL columns
• Purification Kits: complete kits in all three column sizes
• Chromatography Cartridges: compatible with automated liquid chromatography systems and with syringe processing
• Bulk and Custom: let us know your needs for bulk Pierce Protein A/G Agarose

Includes:

Purification kits contain Protein A/G Spin Columns, binding buffer, elution buffer and neutralization buffer

Specifications

• Product Type: Spin Column
• Column Type: Agarose Resin, Affinity
• Stationary Phase: Protein A/G
• Description: NAb Protein A/G Spin Columns, 5mL
• Quantity: 1 column

• Product Line: NAb™
• Format: 50 mL Conical Spin Column
• Purification Target: IgG Antibodies
• Content And Storage: Upon receipt store columns at 4°C

For Research Use Only. Not for use in diagnostic procedures.