mercaptopurine 6 mp Search Results


purity  (Chem Impex International)
95
Chem Impex International purity
Purity, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
purity - by Bioz Stars, 2026-04
95/100 stars
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6 mercaptopurine  (MedChemExpress)
94
MedChemExpress 6 mercaptopurine
Excessive Cu induced cell death through the NADH‐reductive stress‐related pathway. A) Schematic of cytosolic NADH‐reductive stress involving purine biosynthesis and energy stress. NADH interacts with PRPS2 to provoke purine biosynthesis, which causes huge ATP consumption and induces energy stress. The upregulated phosphorylation of AMPK is a self‐defense response of cells under energy stress. Compounds marked in red are protective against NADH‐reductive stress. PRPS2, phosphoribosyl pyrophosphate synthetase 2. R5P, Ribose 5‐phosphate. PRPP, phosphoribosyl pyrophosphate. p‐AMPK, phosphorylated AMP‐activated protein kinase. AKB, α‐ketobutyrate. 6‐MP, <t>6‐mercaptopurine.</t> AICAR, 5‐aminoimidazole‐4‐carboxamide ribonucleoside. B) AMP and GMP levels of SH‐SY5Y cells treated with 250 µ m CuSO 4 for 24 h (unpaired t ‐test, n = 6). C) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . n = 3. D) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB, 500 µ m CuSO 4, and (R)‐GNE‐140. n = 3. E) Viability of SH‐SY5Y cells treated with 500 µ m CuSO 4 and 100 µ m 6‐MP, 400 µ m AICAR for 24 h ( n = 3, unpaired t ‐test). F) Viability of SH‐SY5Y cells pretreated with 600 n m CsA for 2 h, then treated with 500 µ m CuSO 4 and 150 n m CsA for 24 h ( n = 3, unpaired t ‐test). G) ATP levels of SH‐SY5Y cells pretreated 2 h with 1 m m AKB, 100 µ m 6‐MP, 400 µ m AICAR, and 600 n m CsA, then treated with 250 µ m CuSO 4 for 24 h (n = 3, unpaired t ‐test). H,I). Western blot analysis (H) and quantification of p‐AMPK/AMPK ratio (I) of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . The p‐AMPK/AMPK ratio indicates AMPK activation ( n = 3, two‐way ANOVA with Tukey's test). Means ± SD. Images of the cell viability assay are shown in the .
6 Mercaptopurine, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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6 mercaptopurine - by Bioz Stars, 2026-04
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vinblastine  (Selleck Chemicals)
93
Selleck Chemicals vinblastine
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
Vinblastine, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
vinblastine - by Bioz Stars, 2026-04
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6-mercaptopurine (6-mp  (Merck & Co)
90
Merck & Co 6-mercaptopurine (6-mp
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
6 Mercaptopurine (6 Mp, supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
6-mercaptopurine (6-mp - by Bioz Stars, 2026-04
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6- mmp  (Sinopharm ltd)
90
Sinopharm ltd 6- mmp
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
6 Mmp, supplied by Sinopharm ltd, 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/result/6- mmp/product/Sinopharm ltd
Average 90 stars, based on 1 article reviews
6- mmp - by Bioz Stars, 2026-04
90/100 stars
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mice  (TargetMol)
91
TargetMol mice
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
Mice, supplied by TargetMol, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews
mice - by Bioz Stars, 2026-04
91/100 stars
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mercaptopurine (6-mp)  (Deepak Inc)
90
Deepak Inc mercaptopurine (6-mp)
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
Mercaptopurine (6 Mp), supplied by Deepak Inc, 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/result/mercaptopurine (6-mp)/product/Deepak Inc
Average 90 stars, based on 1 article reviews
mercaptopurine (6-mp) - by Bioz Stars, 2026-04
90/100 stars
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6-mercaptopurine  (Aladdin Industrial Corporation)
90
Aladdin Industrial Corporation 6-mercaptopurine
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
6 Mercaptopurine, supplied by Aladdin Industrial Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
6-mercaptopurine - by Bioz Stars, 2026-04
90/100 stars
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6-mercaptopurine 6-mp  (Sangon Biotech)
90
Sangon Biotech 6-mercaptopurine 6-mp
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
6 Mercaptopurine 6 Mp, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
6-mercaptopurine 6-mp - by Bioz Stars, 2026-04
90/100 stars
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6-mercaptopurine 6-mp  (HiMedia Laboratories)
90
HiMedia Laboratories 6-mercaptopurine 6-mp
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
6 Mercaptopurine 6 Mp, supplied by HiMedia Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
6-mercaptopurine 6-mp - by Bioz Stars, 2026-04
90/100 stars
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antipurine 6- mercaptopurine (6-mp) puri-nethol  (DSM Pharmaceuticals Inc)
90
DSM Pharmaceuticals Inc antipurine 6- mercaptopurine (6-mp) puri-nethol
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
Antipurine 6 Mercaptopurine (6 Mp) Puri Nethol, supplied by DSM Pharmaceuticals Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
antipurine 6- mercaptopurine (6-mp) puri-nethol - by Bioz Stars, 2026-04
90/100 stars
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alkylcarbonyloxymethyl (acom) prodrugs of -mercaptopurine (6-mp) and 5-fluorouracil (5-fu)  (Hairess Corporation)
90
Hairess Corporation alkylcarbonyloxymethyl (acom) prodrugs of -mercaptopurine (6-mp) and 5-fluorouracil (5-fu)
A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), <t>Vinblastine</t> (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.
Alkylcarbonyloxymethyl (Acom) Prodrugs Of Mercaptopurine (6 Mp) And 5 Fluorouracil (5 Fu), supplied by Hairess Corporation, 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/result/alkylcarbonyloxymethyl (acom) prodrugs of -mercaptopurine (6-mp) and 5-fluorouracil (5-fu)/product/Hairess Corporation
Average 90 stars, based on 1 article reviews
alkylcarbonyloxymethyl (acom) prodrugs of -mercaptopurine (6-mp) and 5-fluorouracil (5-fu) - by Bioz Stars, 2026-04
90/100 stars
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Excessive Cu induced cell death through the NADH‐reductive stress‐related pathway. A) Schematic of cytosolic NADH‐reductive stress involving purine biosynthesis and energy stress. NADH interacts with PRPS2 to provoke purine biosynthesis, which causes huge ATP consumption and induces energy stress. The upregulated phosphorylation of AMPK is a self‐defense response of cells under energy stress. Compounds marked in red are protective against NADH‐reductive stress. PRPS2, phosphoribosyl pyrophosphate synthetase 2. R5P, Ribose 5‐phosphate. PRPP, phosphoribosyl pyrophosphate. p‐AMPK, phosphorylated AMP‐activated protein kinase. AKB, α‐ketobutyrate. 6‐MP, 6‐mercaptopurine. AICAR, 5‐aminoimidazole‐4‐carboxamide ribonucleoside. B) AMP and GMP levels of SH‐SY5Y cells treated with 250 µ m CuSO 4 for 24 h (unpaired t ‐test, n = 6). C) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . n = 3. D) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB, 500 µ m CuSO 4, and (R)‐GNE‐140. n = 3. E) Viability of SH‐SY5Y cells treated with 500 µ m CuSO 4 and 100 µ m 6‐MP, 400 µ m AICAR for 24 h ( n = 3, unpaired t ‐test). F) Viability of SH‐SY5Y cells pretreated with 600 n m CsA for 2 h, then treated with 500 µ m CuSO 4 and 150 n m CsA for 24 h ( n = 3, unpaired t ‐test). G) ATP levels of SH‐SY5Y cells pretreated 2 h with 1 m m AKB, 100 µ m 6‐MP, 400 µ m AICAR, and 600 n m CsA, then treated with 250 µ m CuSO 4 for 24 h (n = 3, unpaired t ‐test). H,I). Western blot analysis (H) and quantification of p‐AMPK/AMPK ratio (I) of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . The p‐AMPK/AMPK ratio indicates AMPK activation ( n = 3, two‐way ANOVA with Tukey's test). Means ± SD. Images of the cell viability assay are shown in the .

Journal: Advanced Science

Article Title: NADH‐Reductive Stress Induced by Dihydrolipoamide Dehydrogenase Activation Contributes to Cuproptosis

doi: 10.1002/advs.202520444

Figure Lengend Snippet: Excessive Cu induced cell death through the NADH‐reductive stress‐related pathway. A) Schematic of cytosolic NADH‐reductive stress involving purine biosynthesis and energy stress. NADH interacts with PRPS2 to provoke purine biosynthesis, which causes huge ATP consumption and induces energy stress. The upregulated phosphorylation of AMPK is a self‐defense response of cells under energy stress. Compounds marked in red are protective against NADH‐reductive stress. PRPS2, phosphoribosyl pyrophosphate synthetase 2. R5P, Ribose 5‐phosphate. PRPP, phosphoribosyl pyrophosphate. p‐AMPK, phosphorylated AMP‐activated protein kinase. AKB, α‐ketobutyrate. 6‐MP, 6‐mercaptopurine. AICAR, 5‐aminoimidazole‐4‐carboxamide ribonucleoside. B) AMP and GMP levels of SH‐SY5Y cells treated with 250 µ m CuSO 4 for 24 h (unpaired t ‐test, n = 6). C) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . n = 3. D) Viability of SH‐SY5Y cells after 24 h treatment with 1 m m AKB, 500 µ m CuSO 4, and (R)‐GNE‐140. n = 3. E) Viability of SH‐SY5Y cells treated with 500 µ m CuSO 4 and 100 µ m 6‐MP, 400 µ m AICAR for 24 h ( n = 3, unpaired t ‐test). F) Viability of SH‐SY5Y cells pretreated with 600 n m CsA for 2 h, then treated with 500 µ m CuSO 4 and 150 n m CsA for 24 h ( n = 3, unpaired t ‐test). G) ATP levels of SH‐SY5Y cells pretreated 2 h with 1 m m AKB, 100 µ m 6‐MP, 400 µ m AICAR, and 600 n m CsA, then treated with 250 µ m CuSO 4 for 24 h (n = 3, unpaired t ‐test). H,I). Western blot analysis (H) and quantification of p‐AMPK/AMPK ratio (I) of SH‐SY5Y cells after 24 h treatment with 1 m m AKB and CuSO 4 . The p‐AMPK/AMPK ratio indicates AMPK activation ( n = 3, two‐way ANOVA with Tukey's test). Means ± SD. Images of the cell viability assay are shown in the .

Article Snippet: N‐acetylcysteine (HY‐B0215), 6‐mercaptopurine (HY‐13677), ammonium tetrathiomolybdate (HY‐W076067), BOC‐D‐FMK (HY‐13229), ferrostatin‐1 (HY‐100579), CPI‐613 (HY‐15453), cyclosporin A (HY‐B0579), (R)‐GNE‐140 (HY‐100742A), AICAR (HY‐13417), and bortezomib (HY‐10227) were purchased from Med Chem Express.

Techniques: Phospho-proteomics, Western Blot, Activation Assay, Viability Assay

A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), Vinblastine (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.

Journal: bioRxiv

Article Title: SARS-CoV-2 nsp16 is regulated by host E3 ubiquitin ligases, UBR5 and MARCHF7

doi: 10.1101/2024.08.30.610469

Figure Lengend Snippet: A. The non-structural proteins nsp8, nsp11 and nsp16 could be restored by the proteasome inhibitor MG132. HEK293T cells in 12-well plates were transfected with the plasmids of 16 nonstructural proteins (nsp1-16) encoded by SARS-CoV-2. Thirty-six hours later, the cells were treated with MG132 (10 µM) or DMSO for 12 h before collection. The protein level was detected by Immunoblotting (IB). Quantification of nsp protein levels relative to the control protein is shown. Data are representative of three independent experiments and shown as average ±SD (n = 3). Significance was determined by a two-tailed t-test: *P < 0.05; **P < 0.01; ***P < 0.001. B. Proteasomal inhibitors but no other inhibitors stabilized nsp16 protein. HEK293T cells transfected with the nsp16-Flag expression vector were treated with dimethyl sulfoxide (DMSO), MG132 (10 µM), Bortezomib (10 µM), Carfilzomib (10 µM), Bafilomycin A1 (5 µM), Vinblastine (2.5 µM), or NH 4 CL (2.5 µM) for 12 h prior to harvest. The cell lysates were analyzed by anti-Flag antibody. (C-D). The half-life of nsp16 was prolonged by the proteasome inhibitor MG132. C. HEK293T cells were transfected with the nsp16-Flag-expressing plasmids. 12 hours later, the cells were treated with DMSO or MG132 (10 µM) for 12 h, then 50 µg/mL cycloheximide (CHX) was added. Cells were harvested at the indicated times to detect the level of viral protein by anti-Flag antibody. D. Quantification of nsp16 protein levels relative to tubulin at different time points is shown. Results are shown as mean ± SD (n = 3 independent experiments). ***, P < 0.001 by by a two-tailed t-test. E. Samples were prepared for mass spectrometry, and nsp16 interacting proteins were obtained by immunoprecipitation (IP). The plasmids were transfected into HEK293T cells for 48 h. Treat cells with or without MG132 (10 µM) for 12 h prior to harvest. The whole-cell lysates were incubated with protein G agarose beads conjugated with anti-Flag antibodies and used for IB with anti-Flag antibodies to detect the nsp16 protein. Samples enriched for proteins were analyzed by mass spectrometry.

Article Snippet: The drugs used in this study were as follows: MG132 (catalog no. S2619), Bafilomycin A1 (catalog no. S1413), Bortezomib (catalog no. S1013), Carfilzomib (catalog no. S2853) and Vinblastine (catalog no. S4504) were purchased from Selleck (Houston, TX, USA).

Techniques: Transfection, Western Blot, Control, Two Tailed Test, Expressing, Plasmid Preparation, Mass Spectrometry, Immunoprecipitation, Incubation