IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.
The IRF1 is purified by proprietary chromatographic techniques.
Interferon Regulatory Factor-1 (IRF-1) is a crucial transcription factor in the regulation of interferon (IFN) genes and plays a significant role in the immune response. It is a member of the IRF family, which consists of several transcription factors involved in the regulation of the IFN system and other genes related to immune responses .
IRF-1 was first identified as a transcription factor that binds to the IFN-stimulated response element (ISRE) in the promoters of IFN and IFN-stimulated genes . The IRF-1 protein comprises 325 amino acids and contains an N-terminal DNA-binding domain (DBD) characterized by a helix-turn-helix motif. This motif is highly conserved among all IRF proteins and is responsible for recognizing specific DNA sequences .
IRF-1 is known for its role in various cellular processes, including:
Recombinant human IRF-1 is produced using genetic engineering techniques, typically in Escherichia coli (E. coli) cells. The gene encoding IRF-1 is cloned and expressed in E. coli, resulting in the production of the recombinant protein . This recombinant protein is used in various research applications to study the biological functions of IRF-1 and its role in immune responses and tumor suppression .
Recombinant IRF-1 is valuable in research for several reasons: