Recombinant Human Band 3/AE 1 protein (Tagged) is a Human Fragment protein, in the 1 to 403 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex 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 (PubMed:1538405, PubMed:20151848, PubMed:35835865). 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 (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307). (Microbial infection) Acts as a receptor for P.falciparum (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of erythrocytes (PubMed:12692305).
CD233, AE1, DI, EPB3, SLC4A1, Band 3 anion transport protein, Anion exchange protein 1, Solute carrier family 4 member 1, AE 1, Anion exchanger 1
Recombinant Human Band 3/AE 1 protein (Tagged) is a Human Fragment protein, in the 1 to 403 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex 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 (PubMed:1538405, PubMed:20151848, PubMed:35835865). 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 (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307).
Belongs to the anion exchanger (TC 2.A.31) family.
Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation.
Previously labelled as Band 3.
Band 3 also known as AE1 or Anion Exchanger 1 is an important protein found in red blood cells with a mass of approximately 100 kDa. It primarily facilitates the exchange of chloride (Cl-) and bicarbonate (HCO3-) ions across the cell membrane. This protein plays a significant role in maintaining the acid-base balance in the blood and in carbon dioxide transport. Besides red blood cells Band 3 is also expressed in the kidney specifically in the basolateral membrane of alpha-intercalated cells.
Band 3 acts as a component of the larger protein complex responsible for the anion exchange process. It interacts with other proteins such as ankyrin and spectrin forming a structural link between the plasma membrane and the cytoskeleton. This interaction is essential in maintaining the red blood cell shape and flexibility. Band 3 also serves as a docking site for various glycolytic enzymes contributing to metabolic regulation within the cell.
Band 3 plays a part in the bicarbonate transport pathway critical for regulating blood pH and carbon dioxide removal from tissues to the lungs. It closely interacts with carbonic anhydrase a protein that catalyzes the conversion between carbon dioxide and bicarbonate. Another pathway where Band 3 is involved is the erythrocyte cytoskeleton organization pathway in which it works with proteins like spectrin to stabilize the red blood cell membrane.
Band 3 mutations or deficiencies can lead to conditions like hereditary spherocytosis and distal renal tubular acidosis. Hereditary spherocytosis marked by hemolytic anemia involves the improper formation of red blood cells due to defective Band 3 interactions with ankyrin. Meanwhile a malfunction in Band 3's ion exchange capacity can result in distal renal tubular acidosis affecting the kidneys' ability to maintain acid-base homeostasis. Scientists study these conditions to understand better how Band 3 functions across different cell types and its interactions with related proteins.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab235968.
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