Anti-SLC4A1/CD233/Band 3 Antibody Picoband® Fluoro488 Conjugated

Band 3 is also known as SLC4A1. The protein encoded by this gene is part of the anion exchanger (AE) family and is expressed in the erythrocyte plasma membrane, where it functions as a chloride/bicarbonate exchanger involved in carbon dioxide transport from tissues to lungs. The protein comprises two domains that are structurally and functionally distinct. The N-terminal 40kDa domain is located in the cytoplasm and acts as an attachment site for the red cell skeleton by binding ankyrin. The glycosylated C-terminal membrane-associated domain contains 12-14 membrane spanning segments and carries out the stilbene disulphonate-sensitive exchange transport of anions. The cytoplasmic tail at the extreme C-terminus of the membrane domain binds carbonic anhydrase II. The encoded protein associates with the red cell membrane protein glycophorin A and this association promotes the correct folding and translocation of the exchanger. This protein is predominantly dimeric but forms tetramers in the presence of ankyrin. Many mutations in this gene are known in man, and these mutations can lead to two types of disease: destabilization of red cell membrane leading to hereditary spherocytosis, and defective kidney acid secretion leading to distal renal tubular acidosis. Other mutations that do not give rise to disease result in novel blood group antigens, which form the Diego blood group system.

E. coli-derived human SLC4A1 (Position: E28-N365) . Human SLC4A1 shares 75.7% and 74.5% amino acid (aa) sequence identity with mouse and rat SLC4A1, respectively.

Cancer, Cancer Metabolism, Carbohydrate Metabolism, Developmental Biology, Energy Metabolism, Energy Transfer Pathways, Lineage Markers, Lineage Specification, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Metabolism of Lipids and Lipoproteins, Pathways and Processes, Signal Transduction, Stem Cells

Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine. .

1. Jarolim P, Palek J, Amato D, Hassan K, Sapak P, Nurse GT et al. (1991) . Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.Proc. Natl. Acad. Sci. U.S.A. 88 (24) : 11022–6. 2. Schlüter K, Drenckhahn D (August 1986) .Co-clustering of denatured hemoglobin with band 3: its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 83 (16) : 6137–41.

Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Detected in the erythrocyte cell membrane and on the basolateral membrane of alpha-intercalated cells in the collecting duct in the kidney.