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.
Recombinant Protein G is an immunoglobulin-binding protein derived from the cell wall of certain strains of b-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.
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.
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.
