DMT1 Recombinant Rabbit mAb

Divalent metal transporter 1 (DMT1, also known as DCT1 or SLC11A2) is a highly hydrophobic transmembrane protein belonging to the SLC11 family, composed primarily of 12 transmembrane helices (TM) with both the N- and C-termini located on the cytoplasmic side, and featuring a conserved intracellular loop (containing a histidine residue critical for substrate transport) between the 4th and 5th transmembrane helices. The protein exists in multiple splice variants that differ in whether they include an N-terminal or C-terminal iron-responsive element (IRE) for post-transcriptional regulation in response to intracellular iron levels. Physiologically, DMT1 is the principal transporter in mammalian iron metabolism, responsible for the apical uptake of divalent iron (Fe²⁺) from the intestinal lumen across enterocytes into the body, and also mediates the transport of Fe²⁺ released from the transferrin–transferrin receptor complex following endocytosis across the endosomal or lysosomal membrane into the cytoplasm. Additionally, it transports other divalent metal ions such as manganese (Mn²⁺), zinc (Zn²⁺), and cobalt (Co²⁺), with its proton-coupled transport mechanism relying on cotransport driven by the pH gradient between the intra- and extracellular compartments. Pathologically, mutations in the DMT1 gene cause a rare autosomal recessive disorder—congenital iron-deficiency anemia (also known as DMT1 deficiency)—characterized by childhood-onset microcytic hypochromic anemia, elevated serum ferritin, hepatic iron overload, and developmental delay. Dysregulated expression or functional abnormalities of DMT1 are also closely associated with the pathogenesis of neurodegenerative diseases (particularly Parkinson's disease), hemochromatosis, and anemia of inflammation, while its aberrant expression in the central nervous system may lead to iron accumulation in specific brain regions and oxidative stress damage.