B3AT (Band 3 anion transport protein), Polyclonal Antibody

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

IgG

Rabbit

Purified by antigen-specific affinity chromatography.

Liquid

1ug/ul (lot specific)

This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use. For extended storage, aliquot contents and freeze at -20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Small volumes of anti-B3AT antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

B3AT (Band 3 anion transport protein) is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides s for cytoskeletal proteins, glycolytic enzymes, and hemoglobin. it spans the membrane asymmetrically and appears to be tetrameric.

Western Blot (WB), ELISA (EIA)

94,195 Da

solute carrier family 4 member 1 (Diego blood group)

band 3 anion transport protein

Band 3 anion transport protein

AE1; DI; EPB3; AE 1; Anion exchanger 1  [Similar Products]

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. Southeast Asian ovalocytosis (SAO, Melanesian ovalocytosis) results from the heterozygous presence of a deletion in the encoded protein and is common in areas where Plasmodium falciparum malaria is endemic. One null mutation in this gene is known, resulting in very severe anemia and nephrocalcinosis. [provided by RefSeq, Jul 2008]

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.

Lux, S.E., et al, Proc. Natl. Acad. Sci. U.S.A. 86 (23), 9089-9093 (1989) Tanner, M.J., et al, Biochem. J. 256 (3), 703-712 (1988) Yannoukakos, D., et al, Biochim. Biophys. Acta 998 (1), 43-49 (1989) Kaul, R.K., et al, J. Biol. Chem. 258 (13), 7981-7990 (1983) Drickamer, L.K., J. Biol. Chem. 253 (20), 7242-7248 (1978) Kollert-Jons, A., et al, Am. J. Physiol. 265 (6 PT 2), F813-F821 (1993) Kawano, Y., et al, J. Biol. Chem. 263 (17), 8232-8238 (1988) Jennings, M.L. and Smith, J.S., J. Biol. Chem. 267 (20), 13964-13971 (1992) Okubo, K., et al, J. Biol. Chem. 266 (25), 16420-16424 (1991)

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