MRP2 Antibody (M2III-5): sc-59611

MRP2 Antibody (M2III-5) is a mouse monoclonal IgG2b antibody that detects MRP2 in mouse, rat, and human samples through applications such as western blotting (WB), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and flow cytometry (FCM). Anti-MRP2 antibody (M2III-5) is available in a non-conjugated form, allowing for versatile experimental setups. MRP2, also known as canalicular multispecific organic anion transporter (cMOAT), plays a crucial role in the excretion of various organic anions, including drugs and their metabolites, from hepatocytes into bile. This function is particularly important in the context of drug metabolism and resistance, as MRP2 helps to regulate the intracellular concentration of potentially toxic compounds, thereby influencing the pharmacokinetics of therapeutic agents. MRP2 is predominantly localized to the apical membrane of liver cells, where MRP2 facilitates the transport of conjugated substances, ensuring their elimination from the body. Understanding MRP2 function and localization is vital for developing strategies to overcome multidrug resistance in cancer therapy, as well as for predicting drug interactions and optimizing drug delivery systems.

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MRP2 Antibody (M2III-5) References:

1. Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane.  |  König, J., et al. 1999. Hepatology. 29: 1156-63. PMID: 10094960
2. MRP3, a new ATP-binding cassette protein localized to the canalicular domain of the hepatocyte.  |  Ortiz, DF., et al. 1999. Am J Physiol. 276: G1493-500. PMID: 10362653
3. Characterization of the 5'-flanking region of the human multidrug resistance protein 2 (MRP2) gene and its regulation in comparison withthe multidrug resistance protein 3 (MRP3) gene.  |  Stöckel, B., et al. 2000. Eur J Biochem. 267: 1347-58. PMID: 10691972
4. The drug efflux pump MRP2: regulation of expression in physiopathological situations and by endogenous and exogenous compounds.  |  Payen, L., et al. 2002. Cell Biol Toxicol. 18: 221-33. PMID: 12206135
5. Physiological and pharmacological functions of Mrp2, Mrp3 and Mrp4 as determined from recent studies on gene-disrupted mice.  |  Kruh, GD., et al. 2007. Cancer Metastasis Rev. 26: 5-14. PMID: 17273943
6. MRP2 and the Transport Kinetics of Cysteine Conjugates of Inorganic Mercury.  |  Oliveira, C., et al. 2018. Biol Trace Elem Res. 184: 279-286. PMID: 28980184
7. Characterization of in vitro Mrp2 transporter model based on intestinal organoids.  |  Zhang, L., et al. 2019. Regul Toxicol Pharmacol. 108: 104449. PMID: 31449916
8. Reduced Mrp2 surface availability as PI3Kγ-mediated hepatocytic dysfunction reflecting a hallmark of cholestasis in sepsis.  |  Beer, AJ., et al. 2020. Sci Rep. 10: 13110. PMID: 32753644
9. Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein.  |  Versantvoort, CH., et al. 1995. Br J Cancer. 72: 82-9. PMID: 7599070
10. Hepatic canalicular membrane 5: Expression and localization of the conjugate export pump encoded by the MRP2 (cMRP/cMOAT) gene in liver.  |  Keppler, D. and Konig, J. 1997. FASEB J. 11: 509-16. PMID: 9212074
11. Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines.  |  Kool, M., et al. 1997. Cancer Res. 57: 3537-47. PMID: 9270026
12. Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain.  |  Bakos, E., et al. 1998. J Biol Chem. 273: 32167-75. PMID: 9822694

The preferred MRP2 antibody is MRP2 Antibody (G-1): sc-518048.