Granulocyte-Colony Stimulating Factor (G-CSF) is a glycoprotein that plays a crucial role in hematopoiesis, the process of forming blood cellular components. It specifically stimulates the bone marrow to produce granulocytes and stem cells and release them into the bloodstream . The recombinant form of G-CSF, tagged with a histidine (His) tag, is widely used in research and clinical applications.
The human recombinant G-CSF with a His tag is produced in Escherichia coli (E. coli). It is a single, non-glycosylated polypeptide chain containing 174 amino acids, with a molecular mass of approximately 23.19 kDa . The His tag, typically consisting of six histidine residues, is added to the N-terminus of the protein to facilitate purification through affinity chromatography.
G-CSF functions as a cytokine and hormone, promoting the proliferation and differentiation of neutrophils, a type of white blood cell essential for combating infections . It binds to the G-CSF receptor on the surface of hematopoietic cells, triggering a cascade of intracellular signaling pathways that lead to the production and release of neutrophils from the bone marrow .
Recombinant human G-CSF is used to manage neutropenia, a condition characterized by an abnormally low count of neutrophils. Neutropenia can result from chemotherapy, radiation therapy, or certain diseases . By increasing neutrophil counts, G-CSF reduces the risk of infections in patients undergoing these treatments .
The His-tagged version of recombinant human G-CSF is particularly valuable in research settings. The His tag allows for easy purification and detection of the protein, facilitating studies on its structure, function, and interactions with other molecules . Researchers use this recombinant protein to investigate the mechanisms of hematopoiesis and to develop new therapeutic strategies for treating neutropenia and other related conditions .