Glucagon is a peptide hormone produced by the alpha cells of the pancreas. It plays a crucial role in glucose metabolism by promoting the release of glucose into the bloodstream. Recombinant human glucagon, tagged with a polyhistidine (His) tag, is a biotechnologically engineered form of this hormone, designed for research and therapeutic purposes.
Glucagon is a 29-amino acid peptide that functions primarily to raise blood glucose levels by stimulating glycogenolysis and gluconeogenesis in the liver. The recombinant form, often expressed in yeast or bacterial systems, retains the biological activity of the native hormone. The His tag, typically added to the N- or C-terminus of the protein, facilitates purification and detection through affinity chromatography techniques.
The production of recombinant human glucagon involves the insertion of the glucagon gene into an expression vector, which is then introduced into a host organism such as yeast or E. coli. The host cells express the glucagon protein, which is subsequently purified using the His tag. This tag binds to nickel or cobalt ions, allowing for efficient isolation of the protein from the host cell lysate.
Recombinant human glucagon with a His tag is widely used in biochemical and pharmacological research. It serves as a tool for studying glucagon’s role in glucose metabolism, receptor binding, and signal transduction pathways. Additionally, it is employed in the development of therapeutic agents for conditions such as hypoglycemia and diabetes.
The His tag offers several advantages in the production and purification of recombinant proteins: