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A DNA sequence encoding the human G-CSF protein sequence (containing the signal peptide sequence, and the mature G-CSF sequence) was expressed in modified human 293 cells.

Granulocyte colony stimulating factor (G-CSF) is the primary extracellular regulator of granulopoiesis and regulates the production of neutrophils by stimulating proliferation and survival of specific bone marrow precursor cells and their differentiation into granulocytes. Neutrophils play a critical role in the defence against bacterial and fungal infections. G-CSF is produced by monocytes, macrophages, neutrophils, fibroblasts and endothelial cells and is capable of increasing the absolute number of circulating neutrophils and enhancing their antimicrobial function. Unlike GMCSF, the activity of G-CSF is not species specific. Additionally, G-CSF production is inducible by cytokines including TNF-alpha, IL-1, GM-CSF, IL-17 and IL-4. Granulocyte colony stimulating factor (G-CSF) is a glycoprotein consisting of 207 amino acids. Differential splicing of G-CSF mRNA can result in two protein variants either 177- or 180-amino acids in length. G-CSF contains 5 cysteine residues, four of which form inter-molecular disulfide bonds. There is a potential O-glycosylation site at Thr-166, which inhibits aggregation and stabilises the molecule. For a recent review emphasising current advances in knowledge regarding G-CSF signaling, mechanisms of G-CSF-induced stem cell mobilization, and how G-CSF influences T-cell function and dendritic cell activation please refer to Roberts AW (2005) Growth Factors. 23(1): 33-41.