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|Product Name||Anti-CD233/(Band 3) extracellular domain Monoclonal Antibody, PE|
|Description||Mouse monoclonal antibody to human CD233/(Band3) extracellular domain PE conjugate. CD233 (also known as erythrocyte band 3, EPB3, anion exchange protein 1, AE1, solute carrier family 4, SLC4A1) is an integral membrane protein in human erythrocytes, present at approximately 106 copies per human erythrocyte. It comprises two domains that are structurally and functionally distinct. The cytoplasmic N-terminal 40kDa domain has binding sites for erythrocyte cytoskeletal proteins, namely ankyrin and protein 4.2, which help to maintain the mechanical properties and integrity of the erythrocyte. This domain also binds a number of other erythrocyte peripheral proteins. The 55kDa glycosylated C-terminal membrane-associated domain contains 12-14 membrane spanning segments which function as a chloride/bicarbonate anion exchanger involved in carbon dioxide transport. The cytoplasmic tail at the extreme C-terminus of the membrane domain binds carbonic anhydrase II. CD233 associates with the erythrocyte membrane protein glycophorin A (GPA) which promotes the correct folding and translocation during biosynthesis of CD23. Many CD233 mutations are known in man and these mutations can lead to two types of disease; destabilization of the erythrocyte membrane leading to hereditary spherocytosis, and defective kidney acid secretion leading to distal renal tubular acidosis. Other CD233 mutations that do not give rise to disease result in novel blood group antigens, which form the Diego blood group system. The CD233 gene is located on chromosome 17q21-q2.|
|Synonyms||CD233, erythrocyte band 3, EPB3, anion exchange protein 1, AE1, solute carrier family 4, SLC4A1|
|Immunogen||CD233 was made in response to intact human erythrocytes|
|Form||PE-conjugate, in PBS buffer, pH 7.2 containing 0.1% sodium azide, 1% BSA|
|Isotype||Mouse IgG3 kappa light chain|
|Storage||2-8C, do not freeze|
|Intended Use||For Research Use Only|
|References||Bruce L.J. and Tanner M.J.A. (Review) PROW 2:9-17 (2001).
Smythe J.S., Spring F.A., Gardner B., Parsons S.F., Judson P.A. and Anstee D.J. Blood 85:2929-2936 (1995).
Steck T.L. J Supramolec Struct 8:311 (1978).
Jennings M.L., Adams-Lackey M., Denney G.H. J Biol Chem 259: 4652 (1984).
Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., Tanner M.J.A. Blood 85:541 (1995).
Groves J.D., Ring S.M., Schofield A.E., Tanner M.J.A. FEBS Lett 330: 196 (1983).
Toye A.M. et al (2004) J. Cell Science 117, 1399-1410.
Beckmann R. et al (1998) Blood 92, 4428-4438.
Beckmann R. et al (2001) Blood 97, 2496-2505.
Bruce L. J. et al (2003) Blood 101, 4180-4188
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