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Eli Lilly mrp5 protein
Mrp5 Protein, supplied by Eli Lilly, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mrp5+protein/mrp5+protein/pm16586096-255-19-14
Average 90 stars, based on 1 article reviews
mrp5 protein - by Bioz Stars, 2026-09
90/100 stars

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Related Articles

Transfection:

Article Title: Multidrug resistance-associated proteins 3, 4, and 5.
Article Snippet: A reasonable explanation for the discrepancy is that the single transfectant studied in the Eli Lilly lab has more functional MRP5 in the cellular plasma membrane than the 5I clone used for most experiments in the Borst lab.

Functional Assay:

Article Title: Multidrug resistance-associated proteins 3, 4, and 5.
Article Snippet: A reasonable explanation for the discrepancy is that the single transfectant studied in the Eli Lilly lab has more functional MRP5 in the cellular plasma membrane than the 5I clone used for most experiments in the Borst lab.

Clinical Proteomics:

Article Title: Multidrug resistance-associated proteins 3, 4, and 5.
Article Snippet: A reasonable explanation for the discrepancy is that the single transfectant studied in the Eli Lilly lab has more functional MRP5 in the cellular plasma membrane than the 5I clone used for most experiments in the Borst lab.

Membrane:

Article Title: Multidrug resistance-associated proteins 3, 4, and 5.
Article Snippet: A reasonable explanation for the discrepancy is that the single transfectant studied in the Eli Lilly lab has more functional MRP5 in the cellular plasma membrane than the 5I clone used for most experiments in the Borst lab.



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ATP-dependent uptake of [3H]-pravastatin by vesicles prepared from baculovirus infected Sf9 insect cells transfected with human MRP1, MRP2, MRP3, and BCRP transporters and vesicles purified from human (K) cells overexpressing the P-gp, <t>MRP4,</t> and MRP5 transporters. No ATP-dependent uptake was observed in vesicles prepared from mock-transfected cells (control). In vesicles expressing BCRP, MRP1, MRP2, MRP4 and MRP5, the difference between total and nonspecific uptake was statistically significant (P<0.05). The highest pravastatin uptake was observed into vesicles transfected with BCRP and MRP1 transporters. In BCRP and MRP1 vesicles the ratios of pravastatin uptake in the presence of ATP vs its uptake in the presence of AMP were 2.1 ± 0.1 and 5.0 ± 0.6, respectively. The data are shown as mean ± SD of duplicates from three experiments.
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Figure 5. Expressions of MDR1, MRP2, MRP3 and <t>MRP5</t> proteins in BEL-7402/ADM cells by WB. BEL-7402/ADM cells were treated with TMP or VRP (positive control) for 24 h. Proteins were extracted and subjected to Western blotting to determine P-gp, MRP2, MRP3 and MRP5 expression. Data presented are means ± SD values, n=3. **P<0.01 vs. Resistance.
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Figure 5. Expressions of MDR1, MRP2, MRP3 and <t>MRP5</t> proteins in BEL-7402/ADM cells by WB. BEL-7402/ADM cells were treated with TMP or VRP (positive control) for 24 h. Proteins were extracted and subjected to Western blotting to determine P-gp, MRP2, MRP3 and MRP5 expression. Data presented are means ± SD values, n=3. **P<0.01 vs. Resistance.
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Image Search Results


ATP-dependent uptake of [3H]-pravastatin by vesicles prepared from baculovirus infected Sf9 insect cells transfected with human MRP1, MRP2, MRP3, and BCRP transporters and vesicles purified from human (K) cells overexpressing the P-gp, MRP4, and MRP5 transporters. No ATP-dependent uptake was observed in vesicles prepared from mock-transfected cells (control). In vesicles expressing BCRP, MRP1, MRP2, MRP4 and MRP5, the difference between total and nonspecific uptake was statistically significant (P<0.05). The highest pravastatin uptake was observed into vesicles transfected with BCRP and MRP1 transporters. In BCRP and MRP1 vesicles the ratios of pravastatin uptake in the presence of ATP vs its uptake in the presence of AMP were 2.1 ± 0.1 and 5.0 ± 0.6, respectively. The data are shown as mean ± SD of duplicates from three experiments.

Journal: Biochemical pharmacology

Article Title: Role of the Efflux Transporters BCRP and MRP1 in Human Placental Bio-disposition of Pravastatin

doi: 10.1016/j.bcp.2018.09.012

Figure Lengend Snippet: ATP-dependent uptake of [3H]-pravastatin by vesicles prepared from baculovirus infected Sf9 insect cells transfected with human MRP1, MRP2, MRP3, and BCRP transporters and vesicles purified from human (K) cells overexpressing the P-gp, MRP4, and MRP5 transporters. No ATP-dependent uptake was observed in vesicles prepared from mock-transfected cells (control). In vesicles expressing BCRP, MRP1, MRP2, MRP4 and MRP5, the difference between total and nonspecific uptake was statistically significant (P<0.05). The highest pravastatin uptake was observed into vesicles transfected with BCRP and MRP1 transporters. In BCRP and MRP1 vesicles the ratios of pravastatin uptake in the presence of ATP vs its uptake in the presence of AMP were 2.1 ± 0.1 and 5.0 ± 0.6, respectively. The data are shown as mean ± SD of duplicates from three experiments.

Article Snippet: Vesicles purified from human (K) cells overexpressing the MDR1/P-gp, MRP4, and MRP5 transporter proteins were purchased from Solvo Biotechnology through Sigma-Aldrich (St. Louis, MO, USA).

Techniques: Infection, Transfection, Purification, Control, Expressing

Expression of efflux transporter proteins in vesicles prepared from apical and basal membranes of human placenta. Lanes 1–2 - 0.5 and 0.05 μg of positive controls (vesicles prepared from baculovirus infected insect cells (Sf9) expressing human BCRP, MRP1, MRP2, MRP3, and vesicles purified from human (K) cells overexpressing the MDR1/P-gp, MRP4, and MRP5, and HeLa cells). Lanes 3–5 - vesicles prepared from apical membranes of human placentas (# 1,2,3); Lanes 6–8 - vesicles prepared from basal membranes of human placentas (#1,2,3). Both preparations showed immunoreactivity toward trophoblast marker cytokeratin 7.

Journal: Biochemical pharmacology

Article Title: Role of the Efflux Transporters BCRP and MRP1 in Human Placental Bio-disposition of Pravastatin

doi: 10.1016/j.bcp.2018.09.012

Figure Lengend Snippet: Expression of efflux transporter proteins in vesicles prepared from apical and basal membranes of human placenta. Lanes 1–2 - 0.5 and 0.05 μg of positive controls (vesicles prepared from baculovirus infected insect cells (Sf9) expressing human BCRP, MRP1, MRP2, MRP3, and vesicles purified from human (K) cells overexpressing the MDR1/P-gp, MRP4, and MRP5, and HeLa cells). Lanes 3–5 - vesicles prepared from apical membranes of human placentas (# 1,2,3); Lanes 6–8 - vesicles prepared from basal membranes of human placentas (#1,2,3). Both preparations showed immunoreactivity toward trophoblast marker cytokeratin 7.

Article Snippet: Vesicles purified from human (K) cells overexpressing the MDR1/P-gp, MRP4, and MRP5 transporter proteins were purchased from Solvo Biotechnology through Sigma-Aldrich (St. Louis, MO, USA).

Techniques: Expressing, Infection, Purification, Marker

The effect of 100 μM of the transporters inhibitors indomethacin and benzbromarone on ATP-dependent uptake of [3H]-pravastatin was determined using the following vesicle preparations: (i) vesicles prepared from apical and basal membranes of term human placentas, and (ii) purchased vesicle preparations overexpressing MRP1, MRP2, MRP3, MRP4, MRP5, BCRP, and P-gp. The rates of ATP-dependent uptake of [3H]-pravastatin are expressed as percent of control (absence of inhibitors) and represent the mean ± SD of two experiments performed in triplicates.

Journal: Biochemical pharmacology

Article Title: Role of the Efflux Transporters BCRP and MRP1 in Human Placental Bio-disposition of Pravastatin

doi: 10.1016/j.bcp.2018.09.012

Figure Lengend Snippet: The effect of 100 μM of the transporters inhibitors indomethacin and benzbromarone on ATP-dependent uptake of [3H]-pravastatin was determined using the following vesicle preparations: (i) vesicles prepared from apical and basal membranes of term human placentas, and (ii) purchased vesicle preparations overexpressing MRP1, MRP2, MRP3, MRP4, MRP5, BCRP, and P-gp. The rates of ATP-dependent uptake of [3H]-pravastatin are expressed as percent of control (absence of inhibitors) and represent the mean ± SD of two experiments performed in triplicates.

Article Snippet: Vesicles purified from human (K) cells overexpressing the MDR1/P-gp, MRP4, and MRP5 transporter proteins were purchased from Solvo Biotechnology through Sigma-Aldrich (St. Louis, MO, USA).

Techniques: Control

Figure 5. Expressions of MDR1, MRP2, MRP3 and MRP5 proteins in BEL-7402/ADM cells by WB. BEL-7402/ADM cells were treated with TMP or VRP (positive control) for 24 h. Proteins were extracted and subjected to Western blotting to determine P-gp, MRP2, MRP3 and MRP5 expression. Data presented are means ± SD values, n=3. **P<0.01 vs. Resistance.

Journal: Oncology Reports

Article Title: Inhibition of tetramethylpyrazine on P-gp, MRP2, MRP3 and MRP5 in multidrug resistant human hepatocellular carcinoma cells

doi: 10.3892/or_00000625

Figure Lengend Snippet: Figure 5. Expressions of MDR1, MRP2, MRP3 and MRP5 proteins in BEL-7402/ADM cells by WB. BEL-7402/ADM cells were treated with TMP or VRP (positive control) for 24 h. Proteins were extracted and subjected to Western blotting to determine P-gp, MRP2, MRP3 and MRP5 expression. Data presented are means ± SD values, n=3. **P<0.01 vs. Resistance.

Article Snippet: TMP was purchased from Changchun Guoao Pharmaceutical Company (China), verapamil (VRP) was purchased from Shanghai Hefeng Pharmaceutical Company (China), adriamycin (ADM) from Zhejiang Haizheng Pharmaceutical Co., Ltd. (China), P-gp and ß-actin monoclonal antibodies from Sigma-Aldrich Chemical Company (USA), while multidrug resistance-associated protein 2 (MRP2), multidrug resistance-associated protein 3 (MRP3) and multidrug resistance-associated protein 5 (MRP5) monoclonal antibodies from Santa Cruz Biotechnology, Inc. (USA).

Techniques: Positive Control, Western Blot, Expressing