Melanoma Inhibitory Activity (MIA) protein is a small, secreted protein that plays a significant role in the progression and metastasis of malignant melanoma. It is also known as melanoma-derived growth regulatory protein. The recombinant form of this protein, tagged with a His (histidine) tag, is widely used in research to study its structure, function, and potential therapeutic applications.
The human recombinant MIA protein with a His tag is typically expressed in systems such as HEK 293 cells or Escherichia coli. The His tag, usually consisting of six histidine residues, is added to the N-terminus of the protein to facilitate purification using metal affinity chromatography. The recombinant protein is often produced with high purity, exceeding 95%, and has a molecular weight of approximately 14.23 kDa .
MIA protein is involved in the regulation of cell adhesion and migration, which are critical processes in cancer metastasis. It interacts with extracellular matrix components such as fibronectin, disrupting cell-matrix interactions and promoting the detachment of melanoma cells from the primary tumor site . This detachment is a key step in the metastatic spread of melanoma cells to distant organs.
MIA is a valuable biomarker for malignant melanoma. Elevated levels of MIA in the blood are associated with advanced stages of melanoma, particularly metastatic stages III and IV . Monitoring MIA levels can aid in the diagnosis and prognosis of melanoma, as well as in assessing the response to therapy.
The recombinant human MIA protein with a His tag is used in various research applications, including: