g6pd enzyme activity  (MedChemExpress)

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Purification scheme of G6PD from yellow catfish liver.

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques: Purification, Activity Assay

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Purification and kinetic properties of G6PD isolated from yellow catfish liver. ( a ) Affinity column elution profile of G6PD. ( b ) SDS-PAGE photograph of G6PD. Lane 1: purified G6PD (red arrow). Lane 4: standard proteins. ( c ) G6PD standard molecule weighs Rf-logMw graph. ( d ) Effect of different pH on G6PD activity. ( e ) Effect of different temperatures on G6PD activity. ( f ) The double-reciprocal plot of initial velocity against G-6-P as varied substrate at different fixed NADP + concentrations for the reaction catalyzed by G6PD from yellow catfish liver. ( g ) The double-reciprocal plot of initial velocity against NADP + as varied substrate at different fixed G-6-P concentrations. ( h ) The double-reciprocal plots of the inhibition of G6PD by NADPH at three different concentrations to determine K i . The controls show reactions with no inhibitor present.

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques: Purification, Isolation, Affinity Column, SDS Page, Activity Assay, Inhibition

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Kinetic parameters of G6PD from yellow catfish liver.

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques:

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Activity (%) vs metals regression analysis graphs for yellow catfish G6PD in the presence of different metals concentrations ( a ) Cu 2+ , ( b ) Al 3+ , ( c ) Zn 2+ , ( d ) Cd 2+ .

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques: Activity Assay

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: The effect of metal ion on mRNA and activity of G6PD in CCO by QRT-PCR in the presence of different metals concentrations. mRNA of G6PD on ( a ) Cu 2+ , ( b ) Al 3+ , ( c ) Zn 2+ , ( d ) Cd 2+ . Activity of G6PD on ( e ) Cu 2+ , ( f ) Al 3+ , ( g ) Zn 2+ , ( h ) Cd 2+ . The *, **, and *** represent significant differences with p < 0.05, < 0.01, and < 0.001.

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques: Activity Assay, Quantitative RT-PCR

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Cu 2+ , Zn 2+ , and Cd 2+ docking with G6PD. Score diagram of binding residues of metal ions in G6PD amino acid sequences ( a ). Schematic diagram of the interaction between Cu 2+ , Zn 2+ , and Cd 2+ and amino acids at the highest score binding residues position ( b ).

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques: Binding Assay

Journal: Scientific Reports

Article Title: Kinetic properties of glucose 6-phosphate dehydrogenase and inhibition effects of several metal ions on enzymatic activity in vitro and cells

doi: 10.1038/s41598-024-56503-6

Figure Lengend Snippet: Primer sequences used in the qRT-PCR experiment.

Article Snippet: G6PD activity was assessed using a G6PD enzyme activity assay kit (Beyotime Biotechnology, S0189).

Techniques:

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: HPV16 E6 promotes cell proliferation mediated by G6PD. PHKs and C33A cells were stably transduced with lentiviruses expressing the vector, HPV16 E6, or HPV16 E7. These cells were then treated with the G6PD inhibitor 6-An (81.06 μM or 26.78 μM) or infected with a lentivirus expressing shG6PD. (A–D) Cell proliferation rates were determined by performing a CCK8 assay (left). The percentage reduction in cell viability on day 6 is shown independently (right). (E) In total, C33A-Vector, C33A-HPV16E6, and C33A-HPV16E7 cells (1 × 10 6 ) were inoculated subcutaneously into the right flanks of 4- to 5-week-old female nude mice (n = 5 each). Images are shown of nude mouse xenograft tumors derived from C33A-HPV16 E6 and C33A-HPV16 E7 cells treated with 4 mg/kg/3d 6-An. Tumor sizes were measured every 5 days for 3 weeks. Intracellular NADPH (G), NADPH/NADP + (H), GSH (I), GSH/GSSH (J) ROS (K–L) H 2 O 2 (M), and protein carbonylation levels (N) were tested. Each dot represents an independent biological replicate in the plots. Data are presented as mean ± SD. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 compared with indicated groups. Statistical significance was determined using unpaired two-tailed t -test. NS, not significant.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: Stable Transfection, Transduction, Expressing, Plasmid Preparation, Infection, CCK-8 Assay, Derivative Assay, Two Tailed Test

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: HPV16 E6 increases G6PD enzyme activity by promoting the formation of G6PD dimers. PHKs and C33A cells were stably transduced with lentiviruses expressing the vector, HPV16 E6, HPV16 E7, or HPV16 E6E7. (A) mRNA levels of G6PD in the transduced cells were determined via qPCR. (B–C) Immunoblots were used to detect G6PD, Rb, and p53 levels in cell lysates. GAPDH served as a loading control. (D–F) G6PD enzyme activity was examined in these cells. (G–I) Cells were harvested and crosslinked using DSS (3 mM), followed by western blotting with an anti-G6PD antibody. Data are presented as mean ± SD. Each dot represents an independent biological replicate in the plots. * P < 0.05, *** P < 0.001, **** P < 0.0001 compared with indicated groups. Statistical significance was determined using unpaired two-tailed t -test. NS, not significant.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: Activity Assay, Stable Transfection, Transduction, Expressing, Plasmid Preparation, Western Blot, Control, Two Tailed Test

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: HPV16 E6 regulates G6PD enzyme activity independent of p53. (A) KEGG enrichment analysis of the differential genes screened based on GEO (GSE58841). (B) PHKs-E6 cells were treated with 5 μM MG132 for the indicated duration. The whole-cell extracts (WCEs) were then collected for immunoblotting to detect p53 levels in the cells. (C) G6PD enzyme activity was assayed after treating PHKs-E6 cells with MG132 (5 μM) for 6 h. (D) PHKs-E6 cells were treated with 5 μM of MG132 for 6 h. Cells were harvested and crosslinked using DSS (3 mM), followed by western blotting with an anti-G6PD antibody. (E) PHKs-E6 cells were stably transduced with lentiviruses expressing shUBE3A. WCEs were analyzed via immunoblotting for UBE3A and p53. (F) PHKs-E6-shUBE3A cells were employed for the detection of G6PD enzyme activity. (G) Crosslinking with DSS followed by immunoblotting to detect dimeric and monomeric G6PD. Each dot represents an independent biological replicate in the plots. Data are presented as mean ± SD. ** P < 0.01 compared with indicated groups. Statistical significance was determined using unpaired two-tailed t -test. NS, not significant. HPV, human papilloma virus; G6PD, glucose-6-phosphate dehydrogenase; DSS, disuccinimidyl suberate.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: Activity Assay, Western Blot, Stable Transfection, Transduction, Expressing, Two Tailed Test, Virus

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: HPV16 E6 inhibits G6PD lactylation modifications. (A) Pan-lactyation levels were detected in C33A and PHKs expressing HPV16 E6, HPV16 E7, and the vector via western blotting. (B) Immunoblotting for lactylation in the anti-G6PD immunoprecipitates. The immunoprecipitates were isolated from the C33A and PHKs cells overexpressing the vector and HPV16 E6. (C) Intracellular lactate levels were examined in C33A and PHKs cells overexpressing the vector and HPV16 E6. (D) Immunoblotting for lactylation in the anti-G6PD immunoprecipitates. The immunoprecipitates were isolated from C33A and PHKs cells overexpressing the vector and HPV16 E6 upon NaLa treatment (25 mM) for 24 h. (E) G6PD enzyme activity was assayed in C33A and PHKs cells overexpressing the vector and HPV16 E6 upon NaLa treatment (25 mM) for 24 h. (F) Cells were harvested and crosslinked using DSS (3 mM), followed by western blotting with an anti-G6PD antibody. (G–H) LDHA levels were detected in C33A cells expressing HPV16 E6, HPV16 E7, and the vector. mRNA levels of LDHA in the transduced cells were determined via qPCR. Each dot represents an independent biological replicate in the plots. Data are presented as mean ± SD. * P < 0.05, **** P < 0.0001 compared with indicated groups.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: Expressing, Plasmid Preparation, Western Blot, Isolation, Activity Assay

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: The G6PD K45 lactylation modification reduces its enzymatic activity. (A) Schematic diagram of the G6PD structure (PDB: 2BH9 ). Each G6PD monomer consists of a catalytic NADP + and a structural NADP + . Dual G6PD monomers are stacked into a dimer. (B) Species conservation analysis of potential l0 lactylation modification sequence sites for G6PD. (C–E) Re-expression of mutation in PHKs and C33A cells with the knockdown G6PD was used to detect G6PD enzyme activity. (F) Crosslinking with DSS, followed by immunoblotting to detect dimeric and monomeric G6PD. (G–H) Acetylation levels were blotted with a pan-anti-acetyllysine antibody (a-Ac). (I) 3D structure of ligand-receptor interactions shown in the left panel. The right panel shows the 2D representation of the interaction with ligands and the receptors in the binding pocket. Each dot represents an independent biological replicate in the plots. Data are presented as mean ± SD. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 compared with indicated groups. Statistical significance was determined using unpaired two-tailed t -test. NS, not significant.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: Modification, Activity Assay, Sequencing, Expressing, Mutagenesis, Knockdown, Western Blot, Binding Assay, Two Tailed Test

Journal: Redox Biology

Article Title: Human papillomavirus-16 E6 activates the pentose phosphate pathway to promote cervical cancer cell proliferation by inhibiting G6PD lactylation

doi: 10.1016/j.redox.2024.103108

Figure Lengend Snippet: Elevated levels of G6PD K45 lactylation inhibit cell proliferation in vivo and in vitro (A–C) PHKs, C33A cells, and MEFs were transfected with the indicated plasmids. Cell proliferation was analyzed via cell viability assays. (D) SiHa (HPV16 positive) cells stably expressing shCtrl or shG6PD were further infected with lentiviruses expressing WT G6PD or its mutation, as indicated. (E) G6PD-knockdown cells or those cells rescued by WT G6PD or the K45T or K45A mutation were treated with NAC (2 mM), and cell proliferation was analyzed 5 days after treatment. (F) β-Galactosidase staining was used to detect the level of senescence in MEF cells. Right panel: analysis of β-galactosidase-positive cells. Left panel: representative images. (G–H) Tumors were weighed after mice were euthanized at the endpoint. (I–J) C33A and SiHa cell xenograft tumors were used to determine G6PD enzyme activity. Each dot represents an independent biological replicate in the plots. Data are presented as mean ± SD. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 compared with indicated groups. Statistical significance was determined using unpaired two-tailed t -test. NS, not significant. G6PD, glucose-6-phosphate dehydrogenase; NAC, N-acetyl- l -cysteine.

Article Snippet: G6PD enzyme activity was determined by using a Solarbio kit (BC0265) according to the manufacturer's instruction.

Techniques: In Vivo, In Vitro, Transfection, Stable Transfection, Expressing, Infection, Mutagenesis, Knockdown, Staining, Activity Assay, Two Tailed Test

Journal: Heliyon

Article Title: HuaChanSu suppresses the growth of hepatocellular carcinoma cells by interfering with pentose phosphate pathway through down-regulation of G6PD enzyme activity and expression

doi: 10.1016/j.heliyon.2024.e25144

Figure Lengend Snippet: HuaChanSu restrains G6PD level and enzyme activity in HepG2 and Huh-7 cells. (A) Quantitative RT-PCR assay of G6PD mRNA level in tumor cells after HuaChanSu (0, 8 μg/mL) treatment for 24 h. (B) Immunoblotting analysis of G6PD protein expression level in tumor cells treated with series concentrations of HuaChanSu (0, 2, 4, 8 μg/mL) for 24 h. (C) The G6PD enzyme activity of tumor cells treated with HuaChanSu for 24 h. (D) Tumor cells were treated with HuaChanSu at 0, 8 μg/mL for 24 h, then incubated with or without 1 mM DSS solution, followed by immunoblotting. *P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 vs control group. The data are representative of three independent experiments, and each was performed at least in triplicate.

Article Snippet: G6PD enzyme activity detection kit was purchased from Beyotime Biotechnology (Shanghai, China).

Techniques: Activity Assay, Quantitative RT-PCR, Western Blot, Expressing, Incubation, Control

Journal: Heliyon

Article Title: HuaChanSu suppresses the growth of hepatocellular carcinoma cells by interfering with pentose phosphate pathway through down-regulation of G6PD enzyme activity and expression

doi: 10.1016/j.heliyon.2024.e25144

Figure Lengend Snippet: HuaChanSu suppresses G6PD enzyme activity via down-regulation of PLK1 in HepG2 and Huh-7 cells. (A) Quantitative RT-PCR assay of PLK1 mRNA level in tumor cells treated with HuaChanSu (0, 8 μg/mL) for 24 h. (B) Immunoblotting analysis of PLK1 protein expression level in tumor cells treated with series concentrations of HuaChanSu (0, 2, 4, 8 μg/mL) for 24 h. Tumor cells were transfected with siRNAs targeting PLK1, (C) the PLK1 and G6PD protein expression levels were detected by immunoblotting, (D) the G6PD enzyme activity was examined. (E) Tumor cells transfected with siPLK1 or siNC were incubated with or without 1 mM DSS solution, followed by immunoblotting analyses. NC: Negative control. ** P < 0.01, *** P < 0.001, **** P < 0.0001 vs control group. The data are representative of three independent experiments, and each was performed at least in triplicate.

Article Snippet: G6PD enzyme activity detection kit was purchased from Beyotime Biotechnology (Shanghai, China).

Techniques: Activity Assay, Quantitative RT-PCR, Western Blot, Expressing, Transfection, Incubation, Negative Control, Control

Journal: Heliyon

Article Title: HuaChanSu suppresses the growth of hepatocellular carcinoma cells by interfering with pentose phosphate pathway through down-regulation of G6PD enzyme activity and expression

doi: 10.1016/j.heliyon.2024.e25144

Figure Lengend Snippet: HuaChanSu inhibits the proliferation of HepG2 and Huh-7 cells via down-regulation of G6PD expression. (A) Immunoblotting analysis of G6PD protein expression level in tumor cells transfected with siG6PD or siNC. (B) Cell proliferative potential was detected by colony formation assay in tumor cells transfected with siG6PD or siNC. (C) Cell proliferation rates were detected by CCK-8 assay in tumor cells transfected with siG6PD or siNC. (D) Cell viability of tumor cells transfected with siG6PD or siNC treated with or without HuaChanSu for 48 h. NC: Negative control. *: siNC (0, 1, 2, 3 Days) vs siG6PD (0, 1, 2, 3 Days), respectively; % : siNC control group vs siNC treated with HuaChanSu (0.5, 1, 2 μg/mL), respectively; # : siNC treated with HuaChanSu (0, 0.5, 1, 2 μg/mL) vs siG6PD treated with HuaChanSu (0, 0.5, 1, 2 μg/mL), respectively; & : siG6PD control group vs siG6PD treated with HuaChanSu (0.5, 1, 2 μg/mL), respectively. ** P < 0.01, *** P < 0.001, **** P < 0.0001; %%% P < 0.001, %%%% P < 0.0001; ## P < 0.01, ### P < 0.001, #### P < 0.0001; && P < 0.01, &&& P < 0.001.

Article Snippet: G6PD enzyme activity detection kit was purchased from Beyotime Biotechnology (Shanghai, China).

Techniques: Expressing, Western Blot, Transfection, Colony Assay, CCK-8 Assay, Negative Control, Control

Journal: Heliyon

Article Title: HuaChanSu suppresses the growth of hepatocellular carcinoma cells by interfering with pentose phosphate pathway through down-regulation of G6PD enzyme activity and expression

doi: 10.1016/j.heliyon.2024.e25144

Figure Lengend Snippet: Schematic diagram of HuaChanSu-mediated effects on human hepatoma cells by inhibition of G6PD.

Article Snippet: G6PD enzyme activity detection kit was purchased from Beyotime Biotechnology (Shanghai, China).

Techniques: Inhibition

Journal: Cell reports

Article Title: G6PD inhibition sensitizes ovarian cancer cells to oxidative stress in the metastatic omental microenvironment

doi: 10.1016/j.celrep.2022.111012

Figure Lengend Snippet: Gene-expression data revealed metabolic differences of primary ovarian tumors and omental tumors from patients with stage III OC (n = 30). (A) Distinct clustering in t-SNE plot of metabolic gene data from matched primary ovarian tumors (blue) and omental metastases (red). (B) Volcano plot of gene-expression changes for paired ovarian and omental tumors highlighted genes significantly upregulated in omental tumors (red) and ovarian tumors (blue). (C) Pathway analysis of the significantly altered genes. (D) Volcano plot of metabolite abundances determined by liquid chromatography-mass spectrometry (LC-MS) metabolomic analysis of matched ovarian and omental pairs (n = 8). (E) Pathway enrichment analysis of metabolomics data; symbol size indicates pathway impact and color indicates p value. (F) Changes in PPP metabolite abundances are plotted as outlined circles. Blue circles indicate the normalized primary tumor measurements for all tumor pairs (n = 8). (G) G6PD expression in ovarian and omental metastases (n = 8) was quantified using qPCR. (H) G6PD activity of tumor pairs (n = 3) was measured via enzymatic assay. (I) Tumor lysates (n = 3 pairs) were incubated with 25 μM DCFH-DA, and fluorescence was measured at 30 minutes. All summary bar graphs represent mean ± SD. Statistical significances are noted as *p < 0.05, **p < 0.01 by two-tailed Student’s t tests.

Article Snippet: The G6PD enzyme activity (Sigma Aldrich) was performed according to the supplier’s instructions and as described previously ( ; ).

Techniques: Expressing, Liquid Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Activity Assay, Enzymatic Assay, Incubation, Fluorescence, Two Tailed Test

Journal: Cell reports

Article Title: G6PD inhibition sensitizes ovarian cancer cells to oxidative stress in the metastatic omental microenvironment

doi: 10.1016/j.celrep.2022.111012

Figure Lengend Snippet: (A) HEYA8, SKOV3, and IGROV1 tumors were imaged by IVIS (n = 2 per cell line). (B) Intravital imaging showed metastatic seeding and growth in the omentum at 6 and 42 h. (C) Immunoblotting for G6PD expression in murine omental tumor samples. (D) Enzymatic measurement of G6PD activity in primary tumors and omental metastases (n = 4). (E) Tumor lysates were incubated with 25 μM DCFH-DA, and fluorescence was quantified (n = 3). The sample size (n) represents the number of technical replicates. All summary bar graphs represent mean ± SD. Statistical significances are noted as *p < 0.05, **p < 0.01 by two-tailed Student’s t tests.

Article Snippet: The G6PD enzyme activity (Sigma Aldrich) was performed according to the supplier’s instructions and as described previously ( ; ).

Techniques: Imaging, Western Blot, Expressing, Activity Assay, Incubation, Fluorescence, Two Tailed Test

Journal: Cell reports

Article Title: G6PD inhibition sensitizes ovarian cancer cells to oxidative stress in the metastatic omental microenvironment

doi: 10.1016/j.celrep.2022.111012

Figure Lengend Snippet: (A) OC cell lines grown in OCM were incubated with DCFH-DA, and fluorescence was quantified (n = 6). (B) SKOV3 OC cells were transfected with constructs for the intracellular H 2 O 2 sensor, HyPer (n = 3). Ratiometric fluorescence was measured at 0, 12, 24, and 48 h. (C) HyPer signal quantification of OC organoids cultured in omental conditioned organoid media (n = 3). Scale bars, 100 μM. (D and E) G6PD expression via immunoblotting (D) and G6PD activity measured via enzymatic assay (E) in OCM-cultured cells (n = 3). (F) NADPH/NADP+ ratios of OC cells invading an ex vivo omental culture measured by iNAP, a NADPH/NADP+ ratiometric biosensor (n = 3). Scale bars, 100 μM. (G) Immunoblotting for G6PD in OC cell lines after lentiviral shRNA knockdown. (H) Quantification of oxidative stress measured via DCFH-DA signal in WT and G6PD shRNA-expressing OC cells cultured in OCM (n = 3). (I) Quantification of cytotoxicity measured via Sytox staining of OCM and polydatin-treated OC cells (n = 3). The sample size (n) represents the number of technical replicates. All summary bar graphs represent mean ± SD. Statistical significances are noted as *p < 0.05, **p < 0.01 by two-tailed Student’s t tests.

Article Snippet: The G6PD enzyme activity (Sigma Aldrich) was performed according to the supplier’s instructions and as described previously ( ; ).

Techniques: Incubation, Fluorescence, Transfection, Construct, Cell Culture, Expressing, Western Blot, Activity Assay, Enzymatic Assay, Ex Vivo, shRNA, Staining, Two Tailed Test

Journal: Cell reports

Article Title: G6PD inhibition sensitizes ovarian cancer cells to oxidative stress in the metastatic omental microenvironment

doi: 10.1016/j.celrep.2022.111012

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: The G6PD enzyme activity (Sigma Aldrich) was performed according to the supplier’s instructions and as described previously ( ; ).

Techniques: Recombinant, Transduction, Activity Assay, Staining, Isolation, Next-Generation Sequencing, Expressing, shRNA, TaqMan Assay, Plasmid Preparation, Software