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Mouse Anti-ABCC2 Recombinant Antibody (V2-179008) (CBMAB-A0243-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-179008
Antibody Isotype
IgG2a
Application
IHC-Fr, FC, IHC-P, WB

Basic Information

Immunogen
Bacterial fusion protein of cMOAT/MRP2 containing the 202 amino acid C-terminal end of the protein.
Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
ELISA1:30-1:3,000
IF(ICC)1:50-1:500
IP1-2 µl per 100-500 µg of total protein (1 ml of cell lysate)

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.1 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
ATP Binding Cassette Subfamily C Member 2
Introduction
ABCC2 is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN
Entrez Gene ID
1244
UniProt ID
Q92887
Alternative Names
ATP Binding Cassette Subfamily C Member 2; ATP-Binding Cassette, Sub-Family C (CFTR/MRP), Member 2; Canalicular Multispecific Organic Anion Transporter 1; Multidrug Resistance-Associated Protein 2; Canalicular Multidrug Resistance Protein; CMOAT; CMRP;
Function
ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports a wide variety of conjugated organic anions such as sulfate-, glucuronide- and glutathione (GSH)-conjugates of endo- and xenobiotics substrates. Mediates hepatobiliary excretion of mono- and bis-glucuronidated bilirubin molecules and therefore play an important role in bilirubin detoxification. Mediates also hepatobiliary excretion of others glucuronide conjugates such as 17beta-estradiol 17-glucosiduronic acid and leukotriene C4. Transports sulfated bile salt such as taurolithocholate sulfate. Transport various anticancer drugs, such as anthracycline, vinca alkaloid and methotrexate and HIV-drugs such as protease inhibitors. Confers resistance to several anti-cancer drugs including cisplatin, doxorubicin, epirubicin, methotrexate, etoposide and vincristine.
Biological Process
Benzylpenicillin metabolic process
Bile acid and bile salt transport
Bile acid signaling pathway
Bilirubin transport
Canalicular bile acid transport
Cellular chloride ion homeostasis
Cellular response to dexamethasone stimulus
Cellular response to drug
Cellular response to interleukin-1
Cellular response to interleukin-6
Cellular response to lipopolysaccharide
Cellular response to tumor necrosis factor
Drug export
Drug transmembrane transport
Female pregnancy
Heme catabolic process
Inflammatory response
Leukotriene transport
Mercury ion transport
Negative regulation of gene expression
Prostaglandin transport
Regulation of bile acid secretion
Response to 17alpha-ethynylestradiol
Response to antineoplastic agent
Response to arsenic-containing substance
Response to estradiol
Response to estrogen
Response to glucagon
Response to heat
Response to methotrexate
Response to oxidative stress
Thyroid hormone transport
Transepithelial transport
Transmembrane transport
Transport across blood-brain barrier
Xenobiotic catabolic process
Xenobiotic detoxification by transmembrane export across the plasma membrane
Xenobiotic transport across blood-brain barrier
Cellular Location
Apical cell membrane
Involvement in disease
Autosomal recessive disorder characterized by conjugated hyperbilirubinemia, an increase in the urinary excretion of coproporphyrin isomer I, deposition of melanin-like pigment in hepatocytes, and prolonged retention of sulfobromophthalein, but otherwise normal liver function.
Topology
Extracellular: 1-27 aa
Helical: 28-48 aa
Cytoplasmic: 49-68 aa
Helical: 69-89 aa
Extracellular: 90-93 aa
Helical: 94-114 aa
Cytoplasmic: 115-126 aa
Helical: 127-147 aa
Extracellular: 148-165 aa
Helical: 166-186 aa
Cytoplasmic: 187-313 aa
Helical: 314-334 aa
Extracellular: 335-360 aa
Helical: 361-381 aa
Cytoplasmic: 382-437 aa
Helical: 438-458 aa
Extracellular: 459-461 aa
Helical: 462-482 aa
Cytoplasmic: 483-544 aa
Helical: 545-565 aa
Extracellular: 566-587 aa
Helical: 588-608 aa
Cytoplasmic: 609-971 aa
Helical: 972-992 aa
Extracellular: 993-1033 aa
Helical: 1034-1054 aa
Cytoplasmic: 1055-1097 aa
Helical: 1098-1118 aa
Extracellular: 1119 aa
Helical: 1120-1140 aa
Cytoplasmic: 1141-1211 aa
Helical: 1212-1232 aa
Extracellular: 1233-1234 aa
Helical: 1235-1255 aa
Cytoplasmic: 1256-1545 aa
More Infomation

Zhang, L., Huang, P., Huang, C., Jiang, L., Lu, Z., & Wang, P. (2021). Varied clinical significance of ATP-binding cassette C sub-family members for lung adenocarcinoma. Medicine, 100(16).

Zan, X., Yue, G., Hao, Y., & Sima, X. (2021). A systematic review and meta-analysis of the association of ABCC2/ABCG2 polymorphisms with antiepileptic drug responses in epileptic patients. Epilepsy Research, 106678.

Li, X., Miyamoto, K., Takasu, Y., Wada, S., Iizuka, T., Adegawa, S., ... & Watanabe, K. (2020). ATP-binding cassette subfamily a member 2 is a functional receptor for Bacillus thuringiensis Cry2A toxins in Bombyx mori, but not for Cry1A, Cry1C, Cry1D, Cry1F, or Cry9A toxins. Toxins, 12(2), 104.

Wu, L., Li, Y., Song, Y., Zhou, D., Jia, S., Xu, A., ... & Ou, X. (2020). A recurrent ABCC2 p. G693R mutation resulting in loss of function of MRP2 and hyperbilirubinemia in Dubin-Johnson syndrome in China. Orphanet journal of rare diseases, 15(1), 1-8.

Gentiluomo, M., Puchalt García, P., Galeotti, A. A., Talar-Wojnarowska, R., Tjaden, C., Tavano, F., ... & Campa, D. (2019). Genetic variability of the ABCC2 gene and clinical outcomes in pancreatic cancer patients. Carcinogenesis, 40(4), 544-550.

Sato, R., Adegawa, S., Li, X., Tanaka, S., & Endo, H. (2019). Function and role of ATP-binding cassette transporters as receptors for 3D-Cry toxins. Toxins, 11(2), 124.

Wu, L., Zhang, W., Jia, S., Zhao, X., Zhou, D., Xu, A., ... & Ou, X. (2018). Mutation analysis of the ABCC2 gene in Chinese patients with Dubin‑Johnson syndrome. Experimental and therapeutic medicine, 16(5), 4201-4206.

Gentiluomo, M., Galeotti, A., Pezzilli, R., Boggi, U., Capurso, G., Małecka-Panas, E., ... & Campa, D. (2018). Genetic variability of the ABCC2 gene and overall survival in pancreatic cancer. In Pancreatology: Abstract book of the 50th Jubilee Meeting of the European Pancreatic Club: 13-16 June 2018, Berlin, Germany/Organization: INTERPLAN Congress, Meeting & Event Management AG. Basel; New York; New Delhi: Karger; Elsevier, 2018, vol. 18, iss. 4, suppl.

Bustos-Cruz, R. H., Martínez, L. R., García, J. C., Barreto, G. E., & Suárez, F. (2018). New ABCC2 rs3740066 and rs2273697 polymorphisms identified in a healthy Colombian Cohort. Pharmaceutics, 10(3), 93.

Jiang, J., Wang, H. G., Wu, W. L., & Peng, X. X. (2017). Mixed Dubin-Gilbert Syndrome: A Compound Heterozygous Phenotype of Two Novel Variants in ABCC2 Gene. Chinese medical journal, 130(8), 1003.

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For research use only. Not intended for any clinical use.

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