Recombinant mouse MFI2 protein

**Background of MFI2 Recombinant Protein**

MFI2 (Melanotransferrin), also known as MTF or CD228. is a member of the transferrin family of iron-binding proteins. Initially identified in melanoma cells, it shares structural homology with serum transferrin and lactoferrin but exhibits distinct functional properties. Unlike serum transferrin, which circulates in blood to regulate systemic iron transport, MFI2 is predominantly membrane-bound via a glycosylphosphatidylinositol (GPI) anchor or exists in a soluble form, suggesting roles in localized cellular iron homeostasis. The protein consists of two homologous lobes capable of binding ferric ions, though its iron-binding affinity and release mechanisms differ from classical transferrins.

MFI2 is implicated in diverse physiological and pathological processes. It is highly expressed in certain cancers, including melanoma and glioblastoma, where it may contribute to tumor cell survival by modulating iron uptake or mitigating oxidative stress. Studies suggest MFI2 influences cell proliferation, migration, and angiogenesis, potentially through iron-independent pathways, such as interactions with integrins or proteases. Its overexpression in malignancies has sparked interest in MFI2 as a biomarker or therapeutic target.

Recombinant MFI2 protein is engineered for research and potential clinical applications. Produced via expression systems like mammalian cells or *E. coli*, the purified protein retains functional domains for iron binding and receptor interaction. Researchers utilize it to study MFI2's role in iron metabolism, cancer biology, and cellular signaling. In drug discovery, it serves as an antigen for antibody development or a tool to explore iron-chelation strategies. Despite progress, MFI2's precise mechanisms and therapeutic potential remain under investigation, highlighting its relevance in both basic and applied biomedical research.