Product nameProtein A/G/L Sepharose®
Supplied as a 50% slurry in 0.02% thimerosal; >5 mg Protein A/G/L per mL of Sepharose® beads.
Protein A/G/L binds to all IgGs that bind to Protein A, Protein G, and Protein L, making it the ideal choice for purification of a wide range of polyclonal or monoclonal IgG antibodies. The binding capacity is greater than 10 mg/mL of gel; high flow rate; low falling off of rProtein A/G/L; pH stability 2-10.
These beads are for use in column purification. If used in batch purification, we recommend not exceeding 150 x g when centrifuging.
Store beads at 4°C.
The beads may be damaged above 40°C.
DO NOT FREEZE.
Wash beads 3 times with 3x bead volume of desired buffer before use.
- Purification of monoclonal and polyclonal antibodies.
Sepharose is a registered trademark of GE Healthcare
Protein A/G/L Sepharose® is prepared by covalently coupling recombinant Protein A/G/L (containing five Ig-binding regions from Protein L, five IgG binding domains from Protein A, and three Ig-binding regions from Protein G) to 6% cross-linked Sepharose® beads. Cell wall binding regions, albumin binding regions and other non-specific binding regions have all been eliminated from the fusion protein to ensure maximum specific IgG binding. The coupling technique is optimized to give high binding capacity. The capacity of IgG binding could be greater than 10 mg of human IgG per ml of wet gel.
Tested applicationsSuitable for: Purification, IPmore details
Our Abpromise guarantee covers the use of ab193264 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Purification||Use at an assay dependent concentration.
Purification of monoclonal and polyclonal antibodies.
|IP||Use at an assay dependent concentration.|
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab193264 has not yet been referenced specifically in any publications.