Recombinant Protein G is produced using gene cloning and expression techniques. The gene encoding Protein G is inserted into a vector, which is then introduced into a host system, such as Escherichia coli (E. coli). The host cells express the recombinant protein, which can then be purified for various applications.
The His tag (histidine tag) is a string of six to nine histidine residues added to either the N- or C-terminus of a protein. This tag facilitates the purification and detection of recombinant proteins. The His tag binds to immobilized metal ions, such as nickel, cobalt, and copper, under specific buffer conditions. This binding allows for the efficient purification of His-tagged proteins using immobilized metal affinity chromatography (IMAC) .
Recombinant Protein G with a His tag is widely used in research and clinical laboratories for the following purposes:
The production of recombinant Protein G involves several steps:
Recombinant Protein G with a His tag is typically lyophilized for long-term storage. It should be stored at -20°C or lower to maintain its stability. The lyophilized product can be reconstituted according to the manufacturer’s instructions and should be used under sterile conditions to prevent contamination .