Protein G (Recombinant Protein G – M.W. 26.1 kDa) from Streptococcus sp., expressed in E. coli, specifically binds the Fc region of immunoglobulins of many mammalian species  (see Table 1) , with an orientation that allows the F(ab)2 binding sites to be freely available for efficient binding to epitope. When coated onto microplates, the Protein G can securely capture IgG applied directly or as antigen/antibody complexes.

Example of applications:

  • specific and sterically oriented bond of IgG
  • separation of IgG from other immunoglobulins
  • separation of antigen-antibodies complexes
  • isolation and analysis of fusion proteins

Available configurations

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Uniformity

The coated products show a CV% less than 5 when used as a catcher of biotinylated human IgG in an ELISA format using streptavidin-HRP as detector and TMB as substrate.

Storage and Stability

The coated products, if unopened, are stable at 2-8°C until the expiration date printed on the label. If opened, store in closed pouch with desiccant and use within the expiration date.

Product specifications for microplates

Coating

Recombinant Protein G (M.W. 26.1 kDa) ,from Streptococcus sp., expressed in E.coli, is coated using 200 μl/well. The strips are post-coated (blocked) for low non specific binding and long-term stability.

Binding capacity

Microplate was saturated with human IgG at a concentration of 8.0 μg/ml ( 800 ng/well ) in an ELISA format using Streptavidin-HRP as detector and TMB as substrate.

see Binding Capacity technical note

Results:

~ 5.3 pmol IgG/well

Sensitivity

Biotinylated human IgG was detected at a concentration significantly above background in an ELISA format using streptavidin-HRP as detector and TMB as substrate.

see Sensititvity technical note

Results:

0.056 ng/well of human IgG

Product specifications for PCR 8 strip tubes

Coating

Recombinant Protein G (M.W. 26.1 kDa) ,from Streptococcus sp., expressed in E.coli, is coated using 100 µl/tube. The PCR 8 strip tubes are post-coated (blocked) for low non specific binding and long-term stability.