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Band 3 anion transport protein, also known as anion exchanger 1 (AE1) or band 3 or solute carrier family 4 member 1 (SLC4A1), is a protein that is encoded by the SLC4A1 gene in humans.
Band 3 (or solute carrier family 4 member 1, SLC4A1) is the most abundant transmembrane protein found in human red blood cells (RBC). Eosin-5-maleimide (EMA) dye binds to band 3 on intact RBC's. A reduction of fluorescence intensity will be seen in hereditary spherocytosis.
Band 3 protein is a typical polytropic membrane protein and mediates the exchange of the cellular HCO3- with CI- in plasma, which has been known as the "Chloride Shift".
The Band 3 chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1) is one of the best-studied human membrane transport proteins. •. A recent 3.5 Å crystal structure of the Band 3 membrane domain provides new insights into its mechanism of action. •.
Band 3, an integral membrane protein of erythrocytes, constitutes about one-third of the membrane proteins. The amino-terminal region, positioned on the cytoplasmic side, comprises binding sites for hemoglobin, glycolytic enzymes, and ankyrin.
Central to the stability and functional regulation of the RBC membrane is band 3 (Anion exchanger 1, AE1), its most abundant protein at approximately 1.2x10 6 copies per cell.
Band 3 protein (B3p), anion transporter, allows the HCO 3 − /Cl − exchange across plasma membrane and plays an important role for erythrocytes homeostasis. In addition, B3p is linked to proteins cytoskeleton, thus contributing to cell shape and deformability, essential to erythrocytes adjustment within narrowest capillaries.
Band 3 is the most abundant membrane protein in human erythrocytes (1–1.2 million molecules per RBC), with two major functions: (1) cell mechanical support through its physical linkage to ankyrin and the cytoskeletal network (Low et al., 1991); (2) blood CO 2 /HCO 3— exchange through its bicarbonate transport activity.
Band 3, the major integral protein of the red cell, has two primary functions: ion transport and maintenance of protein-protein interactions. Band 3 mediates chloride-bicarbonate exchange and provides a binding site for glycolytic enzymes, hemoglobin, and the skeletal proteins ankyrin, protein 4.1, and protein 4.2.
Band 3 (Anion Exchanger 1, AE1), the predominant protein of erythrocyte membranes, facilitates Cl<sup>-</sup>/HCO<sub>3</sub><sup>-</sup> exchange and anchors the plasma membrane to the cytoskeleton.