Human B2M Knockout Cell Line-Jurkat

Beta-2 microglobulin (B2M) is a small protein that associates with the beta chain of major histocompatibility complex (MHC) class I molecules. B2M is initially synthesized in the endoplasmic reticulum as part of MHC class I molecules. After assembly, the complex, including B2M, is transported to the cell surface. Unlike other components of MHC class I molecules, B2M non-covalently associates with the heavy chain and lacks a transmembrane region. It provides structural stability to the complex and assists in the folding and surface expression of MHC class I molecules. B2M can also become part of other class I molecules such as CD1, MR1, FcRn, and Qa-1.

One prominent function of B2M is its role in iron regulation. It interacts with HFE proteins to regulate the expression of hepcidin in the liver, thereby controlling iron transporters. This interaction is essential for maintaining iron homeostasis by regulating dietary iron absorption and iron release in macrophages. Disruption of this pathway due to loss of B2M function can lead to diseases such as hemochromatosis, which is characterized by excessive iron accumulation. Clinically, elevated levels of B2M in serum serve as a marker for a variety of pathological conditions. These include chronic kidney disease, in which B2M cannot be effectively filtered and accumulates in the blood, and a variety of malignancies such as multiple myeloma and lymphoma. In patients undergoing long-term hemodialysis, B2M can aggregate into amyloid fibrils and deposit in the joint space, leading to dialysis-associated amyloidosis.