IL-28A is produced as a recombinant protein in Escherichia coli (E. coli). The recombinant form is a single, non-glycosylated polypeptide chain consisting of 198 amino acids (26-200 a.a.) and has a molecular mass of approximately 22.1 kDa . This protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification through affinity chromatography .
IL-28A plays a crucial role in the innate immune response to viral infections. It is known to induce the expression of antiviral proteins and has antiproliferative and antitumor activities . IL-28A interacts with a heterodimeric class II cytokine receptor composed of the interleukin-10 receptor, beta (IL10RB), and the interleukin-28 receptor, alpha (IL28RA) .
Upon viral infection, IL-28A is produced and activates both monocytes and macrophages, leading to the production of a restricted panel of cytokines . This activation is crucial for initiating and sustaining the antiviral state in infected cells. IL-28A also induces the expression of ELR (-) CXC chemokine mRNA in human peripheral blood mononuclear cells, independent of IFN-gamma .
Recombinant IL-28A is used extensively in laboratory research to study its role in the immune response and its potential therapeutic applications. It is important to note that this product is intended for research use only and is not suitable for use as a drug, agricultural or pesticidal product, food additive, or household chemical .
The recombinant IL-28A protein is typically supplied as a sterile, filtered, colorless solution. It is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M urea . For short-term storage, it should be kept at 4°C if used within 2-4 weeks. For long-term storage, it is recommended to store the protein at -20°C and to add a carrier protein (0.1% HSA or BSA) to prevent degradation . Multiple freeze-thaw cycles should be avoided to maintain protein integrity .