Recombinant Streptococcal Protein G lacking the albumin-binding produced in E. coli
>20mg sheep IgG and 38mg human/ml
Bead Size Range
GenDEPOT Protein G-Agarose is an affinity chromatography medium designed for easy, one-step purification of classes, subclasses and fragments of immunoglobulins from biological fluids and from cell culture media. The recombinant protein G ligand is coupled to 4% highly cross-linked agarose. The static binding capacity of Protein G-Agarose is greater than 20 mg sheep IgG/ml settled resin. The dynamic binding capacity will vary depending on several factors such as target antibody, flow rate etc. Protein G, a bacterial cell wall protein isolated from group G Streptococci, binds to mammalian IgGs mainly through Fc regions. Native protein G has 3 IgG binding domains and also sites for albumin and cell surface binding. The latter have been eliminated from recombinant protein G to reduce nonspecific binding. Although protein G has very similar tertiary structures to protein A, their amino acid compositions differ significantly, resulting in different binding characteristics. Protein G can be used for purification of mammalian monoclonal and polyclonal IgGs that do not bind well to protein A.
Protein G has greater affinity than protein A for most mammalian IgGs, especially for certain subclasses including human IgG3, mouse IgG1 and rat IgG2a. Unlike protein A, protein G does not bind to human IgM, IgD and IgA.