Interferon-alpha 1b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids and having a molecular mass of 19.5 kDa. The Interferon-alpha 1b gene was obtained from human leukocytes. The IFN-a 1b is purified by proprietary chromatographic techniques.
Interferons were first discovered in 1957 by Isaacs and Lindenmann as antiviral factors . IFN-α1b is encoded by the IFNA1 gene in humans and is expressed in peripheral blood leukocytes and lymphoblastoid cells . The recombinant form of IFN-α1b is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 166 amino acids, with a molecular mass of approximately 19,392 Daltons .
IFN-α1b induces non-specific resistance against a broad range of viral infections . It also affects cell proliferation and modulates immune responses, making it a valuable therapeutic agent . The type I interferons, including IFN-α1b, are known for their ability to suppress the proliferation of cancer cells and modulate both innate and adaptive immune responses .
Recombinant human IFN-α1b has been used in various clinical settings. It is particularly noted for its antiviral properties and has been employed in the treatment of chronic viral infections . Additionally, IFN-α1b has shown promise in cancer therapy, particularly in improving survival rates in advanced melanoma .
Recent research has focused on enhancing the biological activity and extending the half-life of IFN-α1b to improve its clinical efficacy . For instance, novel long-acting recombinant forms of IFN-α2b have been developed, which show increased stability and prolonged activity in vivo . These advancements highlight the ongoing efforts to optimize interferon therapies for better patient outcomes.