Recombinant Protein G contains only two IgG binding domain, but lacks the albumin binding domain to ensure the maximum specific IgG binding capacity. Protein G binds to all IgG subclasses from human, mouse and rat species. The recombinant protein G is produced in Escherichia coli using sequence from Streptococcus C1-C2-C3. The protein G contains amino acids 190-384 having a molecular mass of 21.6 kDa. The protein G migrates on SDS PAGE around 32kDa.
Source: E. coli
Formulation: lyophilized white powder
Purity: >95% as determined by SDS PAGE and RP-HPLC
Amino acid sequence:
MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.
Specificity:
- Binds with greater affinity to most mammalian immunoglobulins than Protein A, including human IgG3 and rat IgG2a.
- Does not bind to human IgM, IgD and IgA.
Reconstitution: Reconstitute with deionized water or PBS
Application: G binds to the constant region of many species of Immunoglobulin G. 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.
Storage: 2 years at -20°C. After reconstitution, aliquot and store at -20°C.