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Anti-MRP2 Antibody, clone 4C9.2 clone 4C9.2, from mouse

ITEM#: 3042-MABN1545

MFR#: MABN1545

Canalicular multispecific organic anion transporter 1 (UniProt Q92887; also known as ATP-binding cassette sub-family C member 2, Canalicular multidrug resistance protein, cMRP, Multidrug resistance-associated protein 2) is encoded by the ABCC2 (also

Canalicular multispecific organic anion transporter 1 (UniProt Q92887; also known as ATP-binding cassette sub-family C member 2, Canalicular multidrug resistance protein, cMRP, Multidrug resistance-associated protein 2) is encoded by the ABCC2 (also known as CMOAT, CMOAT1, CMRP, DJS, MRP2) gene (Gene ID 1244) in human. MRP2/ABCC2 belongs to the family of human ATP-binding cassette (ABC) transporters that are classified into seven subfamilies from ABC-A to ABC-G based on their sequence similarities. P-glycoprotein (P-gp/ABCB1), MRP2/ABCC2, and breast cancer resistance protein (BCRP/ABCG2) are well known plasma membrane ABC transporters that mediate the export of intracellular drugs, drug conjugates and metabolites. MRP2/ABCC2 is the second member of the ABCC subfamily of 13 transporters (ABCC1 to ABCC13). MRP2 is expressed in the apical hepatocyte plasma membrane, renal proximal tubules and small intestine, where it plays a role in the elimination and oral bioavailability of drugs, xenotoxins and their metabolites. MRP2 primarily functions as an organic anion transporter to mediate the elimination of bile acids, GSH and conjugated metabolites of numerous drugs and other xenobiotics. Weakly basic drugs appear to be co-transported with GSH by MRP2. Methotrexate, anthracyclines (doxorubicin, epirubicin), mitoxantrone, cisplatin, and etoposide are well known chemotherapeutic substrates of MRP2. MRP2 contains 17-transmembrane helices (a.a. 28-48, 69-89, 94-114, 127-147, 166-186, 314-334, 361-381, 438-458, 462-482, 545-565, 588-608, 972-992, 1034-1054, 1098-1118, 1120-1140, 1212-1232, 1235-1255), having its N-terminal end (a.a. 1-27) exposed extracellularly and C-terminal end (a.a. 1256-1545) at the cytoplasmic side. Two conserved nucleotide-binding domains (NBDs; a.a. 671-678 and 1334-1341) mediate the binding and hydrolyzing ATP via an ATPase, thereby providing energy for substrates export from the cytoplasm to the extracellular space.