Recombinant Human HJV protein

**Background of HJV Recombinant Protein**

HJV (hemojuvelin), also known as RGMc or HFE2. is a key regulator of iron metabolism, primarily involved in the modulation of hepcidin, a liver-derived hormone that controls systemic iron homeostasis. Discovered in 2003. HJV is encoded by the *HFE2* gene, and mutations in this gene are linked to juvenile hemochromatosis, a severe iron overload disorder. HJV exists in both membrane-bound and soluble forms. The membrane-bound form acts as a co-receptor for bone morphogenetic proteins (BMPs), enhancing the BMP-SMAD signaling pathway to upregulate hepcidin expression. The soluble form, generated through proteolytic cleavage or alternative splicing, may act as a competitive antagonist, modulating this pathway.

Recombinant HJV protein is produced using biotechnological methods, such as expression in mammalian cell lines (e.g., HEK293 or CHO cells) or prokaryotic systems, followed by purification via affinity chromatography. This engineered protein retains functional epitopes, enabling its use in *in vitro* and *in vivo* studies to dissect iron regulatory mechanisms. Researchers employ HJV recombinant protein to investigate BMP-SMAD signaling dynamics, screen therapeutic agents for iron disorders, or develop diagnostic tools for hereditary hemochromatosis.

Its therapeutic potential is also being explored, including as a replacement therapy for HJV-deficient patients or as a hepcidin agonist to treat anemia of chronic disease. However, challenges remain in optimizing stability, bioavailability, and tissue-specific targeting. Overall, HJV recombinant protein serves as a critical tool for advancing our understanding of iron metabolism and developing targeted therapies for iron-related diseases.