|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for ABCC1(NM_004996.3) Search again
Product ID:
HQP011322
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ABC29, ABCC, DFNA77, GS-X, MRP, MRP1
Gene Description:
ATP binding cassette subfamily C member 1
Target Gene Accession:
NM_004996.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
The protein encoded by this gene 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, GCN20, White). This full transporter is a member of the MRP subfamily which is involved in multi-drug resistance. This protein functions as a multispecific organic anion transporter, with oxidized glutatione, cysteinyl leukotrienes, and activated aflatoxin B1 as substrates. This protein also transports glucuronides and sulfate conjugates of steroid hormones and bile salts. Alternative splicing by exon deletion results in several splice variants but maintains the original open reading frame in all forms. [provided by RefSeq].
Gene References into function
- sequence deletion in Pseudoxanthoma elasticum
- Immunolabeling and dye efflux assays indicate that MRP activity and functional expression levels are elevated in monocyte-derived dendritic cells when compared to those present in parental monocytes.
- polyclonal antibodies recognizing both human and rodent MRP1
- MDR transpiorter proteins have a limited role in the treatment failure of patients treated with ifarubicin-based regimens
- overexpression of MRP1 in DS brain may have some relevance to the disorder either by deranging substrate homeostasis or limiting drug access.
- In vivo analysis of human multidrug resistance protein 1 (MRP1) activity using transient expression of fluorescently tagged MRP1.
- Expression of MRP1 can be induced by nonsteroidal anti-inflammatory drugs in a reactive oxygen species-dependent but cyclooxygenase-2-independent manner.
- determination of substrate specificity
- MRP1 mRNA was detected in non-HTLV-1 Tax producing ATL cell lines, but MRP1 is not activated by transfected HTLV-1 Tax expression.
- no difference of expression between diagnosis and relapse of AML; not associated with clinical resistant disease in AML
- Antisense hairpin loop oligonucleotides as inhibitors of expression of multidrug resistance-associated protein 1: their stability in fetal calf serum and human plasma
- Multidrug resistance-associated protein--reduction of expression in human leukaemia cells by antisense phosphorothioate olignucleotides
- rate of uptake of arsenic trioxide and of antimony tartrate in GLC4 and GLC4/ADR cells overexpressing MRP1
- ATP hydrolysis causes a conformational change in MRP1 that reduces the affinity of the protein for this inhibitor
- Mutations in mrp1 results in decreased organic anion transport and increased doxorubicin resistance in Hela cells
- directly interacts with several tyrosine kinase inhibitors
- cytoplasmic retraction of the amino terminus
- S-decyl-glutathione nonspecifically stimulates the ATPase activity of the nucleotide-binding domains of the human multidrug resistance-associated protein, MRP1 (ABCC1).
- evidence for the role of glycosylation in accessibility of the extracellular domains of human MRP1
- Results show efficient GTP hydrolysis by the N-terminal nucleotide binding domain (NBD1) of MRP1
- importance of Lys(332) and His(335) in determining substrate specificity and of Asp(336) in overall transport activity
- the amino terminus of human MRP1 is important and that the Cys(7) residue plays a critical role in maintaining the proper structure and function of human MRP1
- Trp residues are critical for the transport activity and substrate specificity of MRP1
- MRP1 has a functional role in the maintenance of cellular folate homeostasis
- RNA expression of this protein in breast cancer correlates with response to chemotherapy.
- down- and up-regulation of MRP1 (and MRP3) expression can influence cellular folate homeostasis, in particular when cellular retention by polyglutamylation of folates is attenuated.
- MRP1 and MRP5 increase with trophoblast maturation, suggesting a particular role for these proteins in the organ functional developmen
- MRP1 does not have a role in increased resistance to oxidative stress
- ATP binding at nucleotide binding domain 1 at low concentration plays a more important regulatory role than the binding at high concentration and that ATP hydrolysis at nucleotide binding domain 2 plays a dominant role in LTC4 transport.
- A novel silent mutation G816A in exon 8 was found
- MRP1 and MRP2 were expressed in peripheral blood cells, with more than sevenfold higher MRP1 expression in all cell populations investigated. The MRP1 mRNA expression was highest in CD4+ cells >, followed by CD8+ > CD19+ > CD56+ cells.
- Trp653 is involved in the binding of ATP to the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1.
- importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1)
- structural data for MRP1 that might be used to elucidate its mechanism of transport
- phospholipid translocation in the erythrocyte membrane depends on ATP and glutathione
- Basal membrane localization of MRP1 in the placental trophoblast.
- MRP1 transport function requres helices TM6, TM8, TM10, TM11, and TM14 and CL7 may play a differential role in coupling the activity of the nucleotide binding domains to the translocation of different substrates across the membrane
- MRP1 may be a target for MYCN-mediated gene regulation
- Refractory epilepsy phenotype in tuberous sclerosis can be associated with the expression of multidrug resistance MRP-1 transporter in epileptogenic cortical tubers.
- both signature sequences of MRP1 are involved in ATP hydrolysis and must be intact for the ATP hydrolysis and the transport by MRP1.
- MRP1 transports inorganic arsenic as a tri-GSH conjugate, and GSTP1-1 may have a synergistic role in this process
- Glu(1204) serves a dual role in membrane expression of MRP1 and a step in its catalytic cycle subsequent to initial substrate binding
- MRP1 mediates ATP-dependent cellular export of unconjugated bilirubin and supports its role in protecting cells from bilirubin toxicity
- suggest that the conserved glycine residues in both LSGGQ segments are part of the conformational network, which is responsible for the accelerated hydrolytic activity upon interaction of the protein with its transported substrates
- MRP1 gene undergoes alternative splicing at a higher frequency in ovarian tumors than in matched normal tissues, and some of these splice variants confer resistance to doxorubicin.
- properties of multidrug resistance protein 1 are altered by mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue
- MRP1 overexpression is associated with DNA aneuploid carcinomatous cells in non-small cell lung canc
- analysis of nucleotide binding domains and conformation of MRP1
- Hgh-resolution map of leukotriene c4 binding domains in MRP1 and first direct evidence for LTC(4) binding.
- For accurate assessment of changes in MRP1 expression between tumour and normal tissues both protein and mRNA detection are necessary.
- Altered MRP1 levels is associated with intrinsic treatment resistance of non-small cell lung cancer
- The interaction between the 2 nucleotide binding domains of MRP1 and the effects of their binding properties on its ATPase activity are reported.
- ABCB1, ABCC1, ABCC2, and ABCG2 haplotypes influence response to nelfinavir
- analysis of MRP1/ABCC1 variants, none of which are likely by themselves to have major deleterious effects in healthy individuals
- Plant flavonoids were able to reverse drug resistance in human cells transfected with ABCC4; direct inhibition of MRP1-mediated [3H]dinitrophenyl S-glutathione in inside-out vesicles prepared from human erythrocytes was observed.
- cluster of basic amino acids at the TM15/CL7 interface are important for both MRP1 expression and activity and each of the three residues plays a distinct role in the substrate specificity and catalytic activity of the transporter
- ABCB1, ABCC1, and ABCG1 are expressed differently in gastric and nongastric gastrointestinal stromal tumors and do not impair the initial response of the tumor to imatinib
- it is concluded that CIAPIN1 confers multidrug resistance in gastric cancer cells, likely by upregulating MDR-1 and MRP-1
- A novel polymorphism in the 5'UTR of the MRP1 gene.
- expression of MRP1 on resting and activated human T cells, and T cell activation dependence upon MRP1 function
- MRP1 expression and its localization in detergent-resistant membranes were not affected by ganglioside depletion.
- mutations of the Walker A lysine residue, K684L and K1333L, alter tertiary structure; the mutations alter ATP binding and hydrolysis
- GSH has a role in estrone sulfate binding and translocation by the multidrug resistance protein 1
- MRP1 seems to fulfill an important physiological role in dendritic cells development and dendritic cells functions
- the first high-resolution crystal structure of human MRP1 nucleotide binding domain 1.
- Taken together, these results suggest that glutathione conjugation and MRP1-mediated conjugate transport can attenuate nitrolinoleic acid (LNO(2)) bioactivity and thereby play important roles in the regulation of cellular signaling by LNO(2).
- results indicate that two K+ currents (MaxiK and Kv) and the organic anion transporter MRP1 are reciprocally expressed in H69 and H69AR cells
- the ABCC1 amino terminus has a U-shaped folding with a gating function
- The mRNA induction of MDR1, MRP1, MRP2 and MRP3 by rifampicin (Rif), dexamethasone (Dex) and omeprazole (Ome) was investigated in primary cultures of cryopreserved human and rat hepatocytes.
- Data show that tetrahydrocurcumin inhibits the efflux function of ABCB1, ABCC1, and ABCG2 and it is able to extend the multidrug resistance reversing activity of curcuminoids in vivo.
- In locally advanced breast cancer, ABC1 gene expression during chemotherapy dos not contribute to clinical unresponsiveness.
- Transport of sphingosine-1-phosphate by ABCC1 influenced migration of mast cells toward antigen but not degranulation
- MDR1 expression, MRP1 expression, and MRP7 expression are refractory factors in head and neck cancer chemotherapy; induction of MRP7 expression is involved in drug resistance to natural products, especially to docetaxel in salivary gland adenocarcinoma
- PI3K/Akt activation may lead to the development of chemoresistance in AML blasts through a mechanism involving a p53-dependent suppression of MRP1 expression.
- the amino-terminal membrane-spanning domain of human ABCC1/MRP1 has a role in regulation of function by dimerization
- The molecular mechanism of ATP-dependent solute transport by MRP1 is addressed.
- Triton X-100 extraction of detergent-resistant membranes provide evidence that MRP1 is not located in raft-like structures and that its activity is downregulated by cholesterol
- Data suggest that the increase in MRP1 gene dosage observed in drug resistant leukemic cell lines is not responsible for the upregulation of MRP1 expression in leukemic patients.
- MRP1 was significantly hypersensitive against KP772.
- MRP1-Pro(1150), MRP2-Pro(1158), and MRP3-Pro(1147) in the cytoplasmic loop 7 differ in their influence on substrate specificity but share a common role in the nucleotide interactions at nucleotide binding domain 2 of these transporters.
- Retinoblastoma intrinsically expresses both P-gp and MRP-1 and their expressions are not related to tumor differentiation. The expressions of P-gp and MRP-1 do not seem to be induced by chemotherapy and are not related to the degree of tumor invasion.
- neither MRP1 nor MRP2 appears to have a role in response to cisplatin-based chemotherapy in resected non-small cell lung cancer
- Results identified MRP1 as the major transporter of BCPCF in the human erythrocyte membrane and showed for the first time that the active transport of fluorescent substrate into inside-out vesicles can be monitored by flow cytometry.
- The expression analyses of MRP1 and MDR1 drug efflux proteins in doxorubicin-sensitive and -resistant HL60 cells revealed that there was an upregulation of MRP1 gene in HL60/DOX cells as compared to parental sensitive cells.
- statistically significant correlations between MRP1 and LRP expression and between MRP1 or LRP expression and MDR1 expression
- This study showed that manipulation of drug efflux transporters may be a useful strategy for increasing the intracellular concentration and thereby enhancing the clinical efficacy of lopinavir.
- comparative modeling has been used to generate models of human MRP1
- induction of ABCC2 and ABCG2 by tBHQ is mediated by the Nrf2/Keap1 system, whereas the induction of ABCC1 may involve a Keap1-dependent but Nrf2-independent mechanism.
- Infection with Sb-resistant (Sb r) L. donovani induces the upregulation of MRP1 and P-gp in host cells, resulting in a nonaccumulation of intracellular Sb following treatment with sodium antimony gluconate (SAG) favoring parasite replication.
- Determination of P-glycoprotein, MDR-related protein 1, breast cancer resistance protein, and lung-resistance protein expression in leukemic stem cells of acute myeloid leukemia.
- Expression of MRP1 in breat cancer cells greatly reduces sulforaphane accumulation.
- These results suggest that guggulsterone, a natural dietary hypolipidemic agent have dual inhibitory effects on P-gp and MRP1 and the potencies to cause food-drug interactions.
- MRP-overexpressing teniposide-resistant T-cell lymphoma xenografts are inhibited by a tubulin-binding agent
- The functional role of Proline1150 in ABCC1 is investigated.
- MRP1 expression can be used as a molecular risk factor and guide for chemotherapeutic regimens in patients with advanced stages of nasopharyngeal carcinoma.
- Expression and localization MRP1 were significantly higher in hepatoid than in control adenocarcinoma
- Results demonstrate that basal and apoptotic glutathione release are markedly enhanced in cells overexpressing multidrug resistance-associated protein 1.
- Results compare the relative amounts of ABCb1 (Pgp) and ABCc1 (Mrp1)at the blood-brain and blood-cerebrospinal fluid barriers, located respectively at the brain capillary endothelium and the choroid plexus epithelium.
- Celecoxib upregulates MRP1 in colon cancer and results in lack of synergy with standard chemotherapy.
- in prostate cancer cells at least two mechanisms of drug resistance are interconnected. PTEN and mTOR signaling were shown: to be involved into regulation of MRP1 and BCRP
- MRP1-deficient cells accumulated significantly more UCB and suffered greater cytotoxicity than controls.
- the expression of MRP(multiple drug resistance-associated protein)1, MRP2, and MRP3 molecules in systemic lupus erythematosus mononuclear cells was not different from normal
- MRP1 protects intestinal epithelial cells against inflammation-induced apoptotic cell death and provides a functional role for MRP1 in the inflamed intestinal epithelium of IBD patients.
- doxorubicin but not daunorubicin challenged-MRP1 overexpressing HL-60 cells have elevated cytosolic pH
- the rate of release of ADP bynucleotide binding domain 1 in the D793E background may be the rate-limiting step in the transport cycle of MRP1.
- high expression of MRP1 was associated with the MDR phenotype in both acute myeloid leukemia and acute lymphoblastic leukemia patients.
- The current study demonstrated that common polymorphisms in the 3' untranslated region of ABCB1 and ABCC1 may contribute to the etiology of lung cancer.
- ABCC1 gene did not have a significant influence on either disease-free or overall survival in patients with locally advanced breast cancer
- ABCC1 immunostaining was prominent early in the choroid plexus and ventricular ependyma, and noted later in large pyramidal neurons in infants born at 22 (0/7)-42 (0/7) weeks of gestation.
- MRP1 overexpression can mediate Multidrug resistance in patients.