Recombinant Human IL24 protein

Interleukin-24 (IL-24), a member of the interleukin-10 (IL-10) cytokine family, was initially identified as melanoma differentiation-associated gene-7 (MDA-7) due to its upregulated expression during melanoma cell differentiation. This secreted glycoprotein plays multifaceted roles in immune regulation, apoptosis induction, and anti-angiogenesis. Structurally, IL-24 binds to two heterodimeric receptor complexes: IL-20R1/IL-20R2 or IL-22R1/IL-20R2. activating downstream signaling pathways such as JAK-STAT and MAPK, which mediate its biological effects.

Recombinant IL-24 protein, produced via mammalian or bacterial expression systems followed by purification, retains the native protein's functional properties. Its unique ability to selectively induce apoptosis in cancer cells while sparing normal cells has driven extensive research in oncology. Preclinical studies demonstrate IL-24's tumor-suppressive effects through mechanisms including endoplasmic reticulum stress activation, reactive oxygen species generation, and immune microenvironment modulation by enhancing T-cell activity and suppressing pro-tumor macrophages.

Beyond cancer, recombinant IL-24 shows therapeutic potential in autoimmune diseases (e.g., psoriasis, rheumatoid arthritis) by regulating Th17/Treg balance and inhibiting inflammatory cytokines. However, its dual role in inflammation—acting as both a pro-inflammatory mediator and a tissue-protective factor—requires careful context-dependent evaluation. Clinical trials have explored IL-24 gene therapy and recombinant protein delivery, revealing challenges like systemic toxicity and short plasma half-life. Recent advancements in protein engineering, including PEGylation and fusion proteins, aim to improve stability and targeting. Ongoing research also investigates its role in metabolic diseases and tissue repair, expanding its therapeutic landscape despite unresolved questions about receptor specificity and signaling crosstalk.