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M3692

Sigma-Aldrich

Anti-MRP2 antibody, Mouse monoclonal

clone CPR96, purified from hybridoma cell culture

Synonym(s):

Anti-ABCC2, Anti-Multidrug Resistance Associated Protein 2, Anti-cMOAT, Anti-cMRP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

CPR96, monoclonal

form

buffered aqueous solution

mol wt

antigen ~180 kDa

species reactivity

human

concentration

~1.5 mg/mL

technique(s)

indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using cell extracts of 293T cells transfected with human MRP2

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ABCC2(1244)

General description

Anti-MRP2 antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the CPR96 hybridoma produced by the fusion of mouse myeloma cells (NS1) and splenocytes from BALB/c mice immunized with a synthetic peptideintestine.
The gene MRP2 (Multidrug Resistance-associated Protein 2), also referred to as ABCC2 (ATP binding cassette subfamily C member 2), encodes a glycosylated protein belonging to the subfamily of MRP efflux pumps, the members of which are localized exclusively to the apical membrane domain of polarized cells, such as hepatocytes, renal proximal tubule epithelia, and intestinal epithelia. The protein consists of 1545 aa residues having a molar mass of ∼190 kDa. The gene with 32 exons is mapped to human chromosome 10q24.

Application

Anti-MRP2 antibody, Mouse monoclonal has been used in:
  • western blotting
  • immunohistochemistry
  • immunofluorescence microscopy
  • enzyme linked immunosorbent assay (ELISA)

Biochem/physiol Actions

Multidrug Resistance-associated Protein 2 (MRP2) contributes to bile flow and plays a detoxification role and provides protection against oxidative stress. Upregulation of MRP2 expression may be found in hepatocellular carcinomas.
The gene MRP2 (Multidrug Resistance-associated Protein 2) encodes a protein involved in organic anion efflux. It is involved in biliary transport and the efflux of many conjugated compounds across the apical membrane of the hepatocyte into the bile canaliculi. It also participates in multi-drug resistance in mammalian cells. Mutations in this gene have been associated with Dubin-Johnson syndrome (DJS), an autosomal recessive disorder characterized by an increased concentration of bilirubin glucuronosides in blood.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Vasilis Vasiliou et al.
Human genomics, 3(3), 281-290 (2009-05-01)
There exist four fundamentally different classes of membrane-bound transport proteins: ion channels; transporters; aquaporins; and ATP-powered pumps. ATP-binding cassette (ABC) transporters are an example of ATP-dependent pumps. ABC transporters are ubiquitous membrane-bound proteins, present in all prokaryotes, as well as
Role of Nrf2 in the regulation of the Mrp2 (ABCC2) gene
Vollrath V, et al.
The Biochemical Journal, 395(3), 599-609 (2006)
Heidi R Kast et al.
The Journal of biological chemistry, 277(4), 2908-2915 (2001-11-14)
The multidrug resistance-associated protein 2 (MRP2, ABCC2), mediates the efflux of several conjugated compounds across the apical membrane of the hepatocyte into the bile canaliculi. We identified MRP2 in a screen designed to isolate genes that are regulated by the
High activity P-gp, MRP2 and BCRP membrane vesicles prepared from transiently transfected HEK293-EBNA cells
Karlsson JE, et al.
Drug Metabolism and Disposition, dmd-109 (2010)
Molecular characterization of the NPC1L1 variants identified from cholesterol low absorbers
Wang LJ, et al.
The Journal of Biological Chemistry, 286(9), 7397-7408 (2011)

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