Recombinant Protein G, HRP Conjugated

Description
Recombinant Protein G is an immunoglobulin-binding protein derived from the cell wall of certain strains of beta-hemolytic Streptococci. It binds with high affinity to the Fc portion of various classes and subclasses of immunoglobulins from a variety of species. The albumin and cell surface binding domains have been eliminated from Recombinant Protein G to reduce nonspecific binding and, therefore, can be used to separate IgG from crude samples. Due to its affinity for the Fc region of many mammalian immunoglobulins, protein G is a major application in purifying antibodies. Protein G is considered a universal reagent in biochemistry and immunology.

Applications

Antibody purification

Protein purification

Isolates immune complexes

Immunoprecipitation

Immunoaffinity Purification

Western Blotting

Source
Purified from E.coli that carries the protein G gene of G Streptococci.

Purity
>98% by SDS-PAGE and HPLC analyses. The albumin binding domain as well as cell wall and cell membrane binding domains have been removed to ensure the maximum specific IgG binding capacity. This protein contains only IgG binding domains.

Recommended Storage Condition
-20 °C. Avoid freeze / thaw cycles.

Usage
Under optimal conditions, 1 mg protein G will bind approximately 5 mg human IgG. Optimal binding of Protein G to antibodies occurs at pH 5.0 to 6.0 and can be eluted over a pH range of 2.5 to 3.0.