Purified by antigen-specific affinity chromatography.
Immunogen
Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human B3AT(Band 3 anion transport protein)
Application Notes
ELISA, Western blotting: 1µg/ml for 2hrs.
Restrictions
For Research Use only
Format
Liquid
Buffer
This antibody is stored in PBS, 50% glycerol
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Kollert-Jöns, Wagner, Hübner, Appelhans, Drenckhahn: "Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus." in: The American journal of physiology, Vol. 265, Issue 6 Pt 2, pp. F813-21, (1994) (PubMed).
Jennings, Smith: "Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681." in: The Journal of biological chemistry, Vol. 267, Issue 20, pp. 13964-71, (1992) (PubMed).
Okubo, Hamasaki, Hara, Kageura: "Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus." in: The Journal of biological chemistry, Vol. 266, Issue 25, pp. 16420-4, (1991) (PubMed).
Kawano, Okubo, Tokunaga, Miyata, Iwanaga, Hamasaki: "Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein." in: The Journal of biological chemistry, Vol. 263, Issue 17, pp. 8232-8, (1988) (PubMed).
Target
B3AT
(Band 3 Anion Exchange Protein (B3AT))
Alternative Name
B3AT
Background
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 binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin. it spans the membrane asymmetrically and appears to be tetrameric.