Recombinant Protein A/G & Immobilized Protein A/G (3 Citations)
Recombinant Protein A/G contains four Fc-binding domains from Protein A and two from Protein G but lacks the albumin binding sites.
Immobilized Protein A/G consists of recombinant protein A/G ligand covalently immobilized onto 6% highly cross-linked agarose. The dynamic binding capacity will vary depending on several factors such as target antibody, flow rate etc.
Protein A/G binds well to IgG subclasses but does not bind IgA, IgM or serum albumin. This makes Protein A/G an excellent tool for purification and detection of monoclonal antibodies from IgG subclasses, without interference from IgA, IgM and serum albumin. Individual subclasses of monoclonals are likely to have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G.
The Immobilized Protein A/G 1ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples. Each 1ml column enables purification of 1-13mg IgG from 0.5-2ml of serum or other sample.
The Immobilized Protein A/G 0.2ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples. Each 0.2ml column enables purification of 0.1-1mg IgG from 25-500µl of serum or other sample.
Specific binding and elution buffers are also available.
Click here to request bulk or custom sizes.
- High binding capacity: 38mg human IgG/ml resin; >20mg sheep IgG/ml resin
- Ligand: Recombinant Streptococcal protein A/G lacking the albumin binding sites expressed in E. coli
- Bead size: 50-165μm
- Bead Structure: 6% highly cross-linked agarose
- Suitable for immunoaffinity chromatography and immunoprecipitation.
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|Protein A, Protein G, Protein A/G and Protein L Binding Affinity||A table highlighting the binding affinities of protein A, protein G, protein A/G and Protein L. Designed to help in the choice of Well-Coated™ plates.|
- Ahmed, S. et al (2017) Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein. J Biol Chem.doi: 10.1074/jbc.M117.776419
- Das, S. et al (2017) Identification and characterization of a naturally occurring, efficiently cleaved, membrane-bound, clade A HIV-1 Env, suitable for immunogen design, with properties comparable to membrane-bound BG505. Virology 510:22
- McCabe, K. E. et al (2014) Cell Death Dis. DOI: 10.1038/cddis.2014.448