IRF 2 Human

IRF-2 is a transcription factor that consists of 349 amino acids. It has a DNA-binding domain (DBD) at the N-terminal and a repression domain (RD) at the C-terminus . The DNA-binding domain allows IRF-2 to bind to specific DNA sequences, known as interferon-stimulated response elements (ISREs), which are found in the promoters of many virus and interferon-inducible mammalian genes .

IRF-2 is known to act as a repressor of transcription of IRF-1 inducible genes. However, it can also function as an activator of certain genes, such as the cell-cycle regulated H4 (histone) gene, VCAM-1 (Vascular Cell Adhesion Molecule-1), and TLR9 (Toll-like Receptor-9) gene . Moreover, both IRF-2 and IRF-1 are required for the expression of MHC II class molecules through the CIITA type IV promoter .

IRF-2 plays a significant role in cell growth regulation and has been shown to be a potential oncogene . It is involved in various biological processes, including host defense, oncogenesis, apoptosis, viral latency, and immune responses . The ability of IRF-2 to bind to DNA and regulate gene expression makes it a critical player in the cellular response to viral infections and other stress signals.

Recombinant human IRF-2 is expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant protein is biologically active and retains its DNA-binding activity, making it a valuable tool for research and therapeutic applications .