The human recombinant IL-32 alpha is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. It contains 168 amino acids, with a molecular mass of approximately 19.1 kDa . The recombinant protein is fused to a 37 amino acid His Tag at the N-terminus, which facilitates its purification through conventional chromatography techniques .
IL-32 alpha is known for its ability to induce the production of other cytokines such as TNF-alpha, IL-1beta, and IL-6 from macrophages . It activates key cytokine signaling pathways, including NF-kappa-B and p38 MAPK . These pathways are crucial for the inflammatory response and play a role in various immune processes.
IL-32 alpha has been implicated in several diseases due to its proinflammatory properties. For instance, it is involved in the pathogenesis of rheumatoid arthritis, where it contributes to the chronic inflammation observed in the disease . Additionally, dysregulation of IL-32 has been noted in conditions such as myelodysplastic syndrome and chronic myelomonocytic leukemia, where it modulates apoptosis and impairs NK cell function .
The recombinant IL-32 alpha with a His Tag is widely used in laboratory research to study its biological functions and role in diseases. It is particularly useful in experiments requiring high purity and specific activity, such as those investigating cytokine signaling pathways and immune responses .
For optimal stability, the IL-32 alpha protein should be stored at 4°C if used within 2-4 weeks. For longer-term storage, it is recommended to keep the protein frozen at -20°C, with the addition of a carrier protein like 0.1% HSA or BSA to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the protein’s integrity.