Protein G binds to the immunoglobulin constant region of many species. It can be used to detect, quantify and purify IgG antibodies and antibody/antigen complexes. Recombinant protein G contains only IgG binding domains. 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.
The recombinant protein G is produced in Escherichia coli using the sequence from Streptococcus C1-C2-C3. Recombinant protein G contains amino acids 190-384 of the native sequence, and has a molecular mass of 21.6 kDa. Recombinant protein-G migrates on SDS-PAGE around 32 kDa. It has a higher affinity for most mammalian immunoglobulins than protein A, including human IgG3 and rat IgG2a. It does not bind to human IgM, IgD, or IgA. Purity is >95% as determined by SDS-PAGE and RP-HPLC.
Amino acid sequence:
MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.
Protein G is reported to be an excellent tool for purification and detection of IgG antibodies and antibody/antigen complexes.
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