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Valiant Co Ltd propidium iodide pi
Propidium Iodide Pi, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 95/100, based on 317 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Functional roles of HADH and ECHS1 in AML progression and tryptophan metabolism. (A) RT-qPCR to verify HADH and ECHS1 expression in MOLM-13 cells and MV4-11 cells. (B) CCK8 assay in two AML cells. (C) Knockdown of HADH and ECHS1 accelerated <t>apoptosis</t> in 2 cell lines, as demonstrated by flow cytometry. (D) Kaplan-Meier curve analysis of HADH and ECHS1 in AML patients and normal controls.
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Functional roles of HADH and ECHS1 in AML progression and tryptophan metabolism. (A) RT-qPCR to verify HADH and ECHS1 expression in MOLM-13 cells and MV4-11 cells. (B) CCK8 assay in two AML cells. (C) Knockdown of HADH and ECHS1 accelerated <t>apoptosis</t> in 2 cell lines, as demonstrated by flow cytometry. (D) Kaplan-Meier curve analysis of HADH and ECHS1 in AML patients and normal controls.
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MMP11 silencing reduced the migration of ESCA cells. MMP11 silencing significantly reduced MMP11 expression in ESCA cells (A) while inhibiting PD-L1 expression (B). (C) MMP11 silencing significantly reduced relative wound width in ESCA cells (10×, 200 μm). (D) MMP11 silencing increased <t>apoptosis</t> in ESCA cells significantly. Data were expressed as mean ± SD. Differences among groups were compared using independent samples t -test. *** P < 0.001 compared with the sh-NC. n = 3 represents three biological replicates.
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HeLa cells were challenged with A 9.375–600 HU/mL candidalysin (Clys), B 4–2000 HU/mL aerolysin (Aero), C 31–2000 HU/mL SLO, or A – C a mass equivalent to wild-type toxin of candidalysin mutAA , aerolysin Y221G , or monomer-locked SLO (SLO ML) in RPMI supplemented with 2 mM CaCl 2 and 20 μg/ml <t>propidium</t> iodide (PI) at 37 °C. PI uptake was analyzed by flow cytometry and % specific lysis was determined. D The amount of toxin needed to kill 50% of the cells (LC 50 ) was calculated by logistic modeling. E HeLa cells were challenged with 9.375–600 HU/mL Clys, 31–2000 HU/mL Aero, or 31–2000 HU/mL SLO at 37 °C in RPMI supplemented with either 2 mM CaCl 2 , or 2 mM EGTA. PI uptake was analyzed by flow cytometry. The LC 50 was calculated as described above. Dotted lines indicate the lower and upper limits of detection. Graphs show the mean ± S.E.M. of A – D six or E five independent experiments, with D , E independent experiments plotted as data points. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 by repeated-measures one-way ANOVA with Tukey’s multiple comparison test.
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Image Search Results


Functional roles of HADH and ECHS1 in AML progression and tryptophan metabolism. (A) RT-qPCR to verify HADH and ECHS1 expression in MOLM-13 cells and MV4-11 cells. (B) CCK8 assay in two AML cells. (C) Knockdown of HADH and ECHS1 accelerated apoptosis in 2 cell lines, as demonstrated by flow cytometry. (D) Kaplan-Meier curve analysis of HADH and ECHS1 in AML patients and normal controls.

Journal: Frontiers in Pharmacology

Article Title: Prediction of prognosis and immunotherapy response of tryptophan metabolism genes in acute myeloid leukemia

doi: 10.3389/fphar.2025.1714246

Figure Lengend Snippet: Functional roles of HADH and ECHS1 in AML progression and tryptophan metabolism. (A) RT-qPCR to verify HADH and ECHS1 expression in MOLM-13 cells and MV4-11 cells. (B) CCK8 assay in two AML cells. (C) Knockdown of HADH and ECHS1 accelerated apoptosis in 2 cell lines, as demonstrated by flow cytometry. (D) Kaplan-Meier curve analysis of HADH and ECHS1 in AML patients and normal controls.

Article Snippet: Apoptosis was assessed using an Annexin V-FITC/propidium iodide (PI) Apoptosis Detection Kit (Lianke Bio, AP101-01, China).

Techniques: Functional Assay, Quantitative RT-PCR, Expressing, CCK-8 Assay, Knockdown, Flow Cytometry

MMP11 silencing reduced the migration of ESCA cells. MMP11 silencing significantly reduced MMP11 expression in ESCA cells (A) while inhibiting PD-L1 expression (B). (C) MMP11 silencing significantly reduced relative wound width in ESCA cells (10×, 200 μm). (D) MMP11 silencing increased apoptosis in ESCA cells significantly. Data were expressed as mean ± SD. Differences among groups were compared using independent samples t -test. *** P < 0.001 compared with the sh-NC. n = 3 represents three biological replicates.

Journal: Translational Oncology

Article Title: MMP11 promotes immune escape in esophageal carcinoma cells via the PD-L1/c-Myc signaling pathway

doi: 10.1016/j.tranon.2025.102604

Figure Lengend Snippet: MMP11 silencing reduced the migration of ESCA cells. MMP11 silencing significantly reduced MMP11 expression in ESCA cells (A) while inhibiting PD-L1 expression (B). (C) MMP11 silencing significantly reduced relative wound width in ESCA cells (10×, 200 μm). (D) MMP11 silencing increased apoptosis in ESCA cells significantly. Data were expressed as mean ± SD. Differences among groups were compared using independent samples t -test. *** P < 0.001 compared with the sh-NC. n = 3 represents three biological replicates.

Article Snippet: Cell apoptosis was assessed using the Annexin V-APC/propidium iodide (PI) Apoptosis Kit (cat. no AP107; Multi Sciences Biotech Co., Ltd.).

Techniques: Migration, Expressing

MMP11 overexpression promoted the growth of ESCA cells. (A) MMP11 was significantly overexpressed. MMP11 overexpression increased ESCA cell relative wound width (B) while decreasing ESCA cell apoptosis (C). (D-E) The effect of MMP11 overexpression on PD-L1 and c-Myc signaling pathway protein expression in ESCA cells. (F-H) The ratio of CD4 + /CD8 + /CD25 + Foxp3 + positive cells in Treg cells co-cultured with OE19 and OE33 cells. (I-L) TNF-ɑ, TGF-β, IFN-γ, and IL-10 levels were measured using ELISA in ESCA cells overexpressing MMP11. Data were expressed as mean ± SD. Differences among groups were compared using independent samples t -test. *** P < 0.001 compared with the pcDNA. n = 3 represents three biological replicates.

Journal: Translational Oncology

Article Title: MMP11 promotes immune escape in esophageal carcinoma cells via the PD-L1/c-Myc signaling pathway

doi: 10.1016/j.tranon.2025.102604

Figure Lengend Snippet: MMP11 overexpression promoted the growth of ESCA cells. (A) MMP11 was significantly overexpressed. MMP11 overexpression increased ESCA cell relative wound width (B) while decreasing ESCA cell apoptosis (C). (D-E) The effect of MMP11 overexpression on PD-L1 and c-Myc signaling pathway protein expression in ESCA cells. (F-H) The ratio of CD4 + /CD8 + /CD25 + Foxp3 + positive cells in Treg cells co-cultured with OE19 and OE33 cells. (I-L) TNF-ɑ, TGF-β, IFN-γ, and IL-10 levels were measured using ELISA in ESCA cells overexpressing MMP11. Data were expressed as mean ± SD. Differences among groups were compared using independent samples t -test. *** P < 0.001 compared with the pcDNA. n = 3 represents three biological replicates.

Article Snippet: Cell apoptosis was assessed using the Annexin V-APC/propidium iodide (PI) Apoptosis Kit (cat. no AP107; Multi Sciences Biotech Co., Ltd.).

Techniques: Over Expression, Expressing, Cell Culture, Enzyme-linked Immunosorbent Assay

HeLa cells were challenged with A 9.375–600 HU/mL candidalysin (Clys), B 4–2000 HU/mL aerolysin (Aero), C 31–2000 HU/mL SLO, or A – C a mass equivalent to wild-type toxin of candidalysin mutAA , aerolysin Y221G , or monomer-locked SLO (SLO ML) in RPMI supplemented with 2 mM CaCl 2 and 20 μg/ml propidium iodide (PI) at 37 °C. PI uptake was analyzed by flow cytometry and % specific lysis was determined. D The amount of toxin needed to kill 50% of the cells (LC 50 ) was calculated by logistic modeling. E HeLa cells were challenged with 9.375–600 HU/mL Clys, 31–2000 HU/mL Aero, or 31–2000 HU/mL SLO at 37 °C in RPMI supplemented with either 2 mM CaCl 2 , or 2 mM EGTA. PI uptake was analyzed by flow cytometry. The LC 50 was calculated as described above. Dotted lines indicate the lower and upper limits of detection. Graphs show the mean ± S.E.M. of A – D six or E five independent experiments, with D , E independent experiments plotted as data points. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 by repeated-measures one-way ANOVA with Tukey’s multiple comparison test.

Journal: Cell Death Discovery

Article Title: The fungal peptide toxin candidalysin induces distinct membrane repair mechanisms compared to bacterial pore-forming toxins

doi: 10.1038/s41420-025-02923-w

Figure Lengend Snippet: HeLa cells were challenged with A 9.375–600 HU/mL candidalysin (Clys), B 4–2000 HU/mL aerolysin (Aero), C 31–2000 HU/mL SLO, or A – C a mass equivalent to wild-type toxin of candidalysin mutAA , aerolysin Y221G , or monomer-locked SLO (SLO ML) in RPMI supplemented with 2 mM CaCl 2 and 20 μg/ml propidium iodide (PI) at 37 °C. PI uptake was analyzed by flow cytometry and % specific lysis was determined. D The amount of toxin needed to kill 50% of the cells (LC 50 ) was calculated by logistic modeling. E HeLa cells were challenged with 9.375–600 HU/mL Clys, 31–2000 HU/mL Aero, or 31–2000 HU/mL SLO at 37 °C in RPMI supplemented with either 2 mM CaCl 2 , or 2 mM EGTA. PI uptake was analyzed by flow cytometry. The LC 50 was calculated as described above. Dotted lines indicate the lower and upper limits of detection. Graphs show the mean ± S.E.M. of A – D six or E five independent experiments, with D , E independent experiments plotted as data points. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 by repeated-measures one-way ANOVA with Tukey’s multiple comparison test.

Article Snippet: Propidium iodide (PI) was from Biotium (Fremont, CA, USA) (Cat # 40016).

Techniques: Flow Cytometry, Lysis, Comparison