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Proteintech cyt c

HIF disrupts mitochondrial homeostasis and decreases ATP production. (A–C) Representative immunofluorescence images show the subcellular localization and nuclear translocation <t>of</t> <t>AIF,</t> MIF, and Cytochrome c (Cyt c) in HCT15 and HCT116 cells following 24 h HIF treatment. (D, E) Quantification of intracellular reactive oxygen species (ROS) levels in HCT15 and HCT116 cells, respectively. (F, G) Quantification of mitochondrial ROS intensity using mitoSOX staining in HCT15 and HCT116 cells, respectively. (H, I) Oxygen consumption rate (OCR) fluorescence intensity in HCT15 and HCT116 cells, reflecting changes in mitochondrial respiration. (J, K) Relative intracellular ATP levels in HCT15 and HCT116 cells following HIF treatment. (L) Flow cytometric analysis of mitochondrial membrane potential (Δψm) in HCT15 and HCT116 cells after HIF treatment, assessed using JC‐1 staining. The red‐to‐green fluorescence intensity ratio was used to quantify alterations in membrane potential (right panels). ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Cyt C, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 706 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/cyt+c/Cytochrome+c+Antibody/pmc13045231-226-122-125
Average 96 stars, based on 706 article reviews

cyt c - by Bioz Stars, 2026-09

96/100 stars

Images

1) Product Images from "Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death"

Article Title: Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death

Journal: Advanced Science

doi: 10.1002/advs.202511406

Figure Legend Snippet: HIF disrupts mitochondrial homeostasis and decreases ATP production. (A–C) Representative immunofluorescence images show the subcellular localization and nuclear translocation of AIF, MIF, and Cytochrome c (Cyt c) in HCT15 and HCT116 cells following 24 h HIF treatment. (D, E) Quantification of intracellular reactive oxygen species (ROS) levels in HCT15 and HCT116 cells, respectively. (F, G) Quantification of mitochondrial ROS intensity using mitoSOX staining in HCT15 and HCT116 cells, respectively. (H, I) Oxygen consumption rate (OCR) fluorescence intensity in HCT15 and HCT116 cells, reflecting changes in mitochondrial respiration. (J, K) Relative intracellular ATP levels in HCT15 and HCT116 cells following HIF treatment. (L) Flow cytometric analysis of mitochondrial membrane potential (Δψm) in HCT15 and HCT116 cells after HIF treatment, assessed using JC‐1 staining. The red‐to‐green fluorescence intensity ratio was used to quantify alterations in membrane potential (right panels). ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Techniques Used: Immunofluorescence, Translocation Assay, Staining, Fluorescence, Membrane

HIF suppresses CRC tumor growth in vivo. (A) Tumor growth in mouse models bearing HCT116 cells treated with HIF, 5‐FU, or the combination. (B) Final tumor weights were measured at the end of treatment across treatment groups. (C) Representative images of excised tumors from each group. (D) Body weight monitoring throughout the treatment period. (E, F) H&E and IHC analysis of tumor tissues for Ki67, Cyt c, c‐Caspase‐3, and c‐PARP, with corresponding quantification. (G) H&E and IHC staining of kidney and liver tissues to evaluate potential organ toxicity. (H–J) Immunofluorescence analysis of γ‐H2AX, AIF, and MIF localization in tumor tissues. Nuclei are stained with DAPI (blue), and target proteins appear in green. (K) Schematic representation illustrating the proposed mechanism by which HIF‐induced DNA damage leads to mitochondrial apoptosis and parthanatos‐mediated colorectal tumor cell death. ** p < 0.01, **** p < 0.0001.

Figure Legend Snippet: HIF suppresses CRC tumor growth in vivo. (A) Tumor growth in mouse models bearing HCT116 cells treated with HIF, 5‐FU, or the combination. (B) Final tumor weights were measured at the end of treatment across treatment groups. (C) Representative images of excised tumors from each group. (D) Body weight monitoring throughout the treatment period. (E, F) H&E and IHC analysis of tumor tissues for Ki67, Cyt c, c‐Caspase‐3, and c‐PARP, with corresponding quantification. (G) H&E and IHC staining of kidney and liver tissues to evaluate potential organ toxicity. (H–J) Immunofluorescence analysis of γ‐H2AX, AIF, and MIF localization in tumor tissues. Nuclei are stained with DAPI (blue), and target proteins appear in green. (K) Schematic representation illustrating the proposed mechanism by which HIF‐induced DNA damage leads to mitochondrial apoptosis and parthanatos‐mediated colorectal tumor cell death. ** p < 0.01, **** p < 0.0001.

Techniques Used: In Vivo, Immunohistochemistry, Immunofluorescence, Staining

Incubation:

Article Title: Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death
Article Snippet: .. The membranes were then blocked with a 5% non‐fat milk TBST (TBS containing 0.1% Tween‐20) for 1 h at room temperature and incubated at 4°C for overnight with primary antibodies against the following proteins: cleaved Caspase 3 (25128‐1‐AP, Proteintech), cleaved Caspase 8 (9496, CST), PARP (9542, CST), cleaved PARP (9541, CST), P21 (2947, CST), P53 (2527, CST), Cyclin A2 (91500, CST), Cyclin D1 (2978, CST), CDK1 (bs‐1341R, Bioss), CDK2 (bs‐10726R, Bioss), CDK7 (bs‐0569R, Bioss), AKT (4691, CST), p‐AKT (4060, CST), ERK (9102, CST), p‐ERK (9101, CST), MEK (9126, CST), p‐MEK (9154, CST), ATR (13934, CST), p‐ATR (2853, CST), Chk1 (2360, CST), p‐Chk1 (2348, CST), RAD51 (14961‐1‐AP, Proteintech), ATM (27156‐1‐AP, Proteintech), p‐ATM (5883, CST), γ‐H2AX (9718, CST), AIF (5318, CST), MIF (75038, CST), Cyt c (10993‐1‐AP, Proteintech), Lamin B (66095‐1‐Ig, Proteintech), VDAC1 (81538‐1‐RR, Proteintech) and GAPDH (60004‐1‐Ig, Proteintech). .. Following primary antibody incubation, the membranes were washed again with TBST and incubated with HRP‐conjugated goat anti‐mouse IgG (H+L) (SA00001‐1, Proteintech) and goat anti‐rabbit IgG (H+L) (SA00001‐2, Proteintech) for 1 h at room temperature.

Article Title: MRPL13 enhances mitochondrial function and promotes tumor progression in ovarian cancer by inhibiting mPTP opening via SLC25A6
Article Snippet: Proteins were separated via SDS-PAGE and transferred onto 0.2 μm or 0.45 μm PVDF membranes (Millipore, USA). .. Membranes were blocked in 5% non-fat milk for 1–2 h at room temperature, followed by overnight incubation at 4 °C with primary antibodies, including MRPL13 (Proteintech, 16241-1-AP, 1:1000), β-Actin (Proteintech, 66009-1-Ig, 1:5000), PCNA (CST, 2586, 1:1000), Bcl-2 (Proteintech, 12789-1-AP, 1:2000), Bax (CST, 5023, 1:1000), Caspase-3 (CST, 9662, 1:1000), SLC25A6 (Proteintech, 14841-1-AP, 1:1000), Flag-tag (Proteintech, 20543-1-AP, 1:4000), HA-tag (Proteintech, 51064-2-AP, 1:4000), Myc-tag (Proteintech, 16286-1-AP, 1:4000), Ubiquitin (CST, 3936, 1:1000), Cyt c (Proteintech, 10993-1-AP, 1:1000), and COXIV (Proteintech, 11242-1-AP, 1:2000). .. After three washes with TBST, membranes were incubated with HRP-conjugated secondary antibodies (ZSGB-BIO, ZB-2301/ZB-2305, 1:4000) at room temperature for 1 h. Protein bands were visualized using HRP chemiluminescent substrate (Millipore, USA) and imaged with the Tanon 5200 Multi System.

Article Title: MRPL13 enhances mitochondrial function and promotes tumor progression in ovarian cancer by inhibiting mPTP opening via SLC25A6.
Article Snippet: Proteins were separated via SDS-PAGE and transferred onto 0.2 μm Cell Death and Disease (2025) 16:634 or 0.45 μm PVDF membranes (Millipore, USA). .. Membranes were blocked in 5% non-fat milk for 1–2 h at room temperature, followed by overnight incubation at 4 °C with primary antibodies, including MRPL13 (Proteintech, 16241-1-AP, 1:1000), β-Actin (Proteintech, 66009-1-Ig, 1:5000), PCNA (CST, 2586, 1:1000), Bcl-2 (Proteintech, 12789-1-AP, 1:2000), Bax (CST, 5023, 1:1000), Caspase-3 (CST, 9662, 1:1000), SLC25A6 (Proteintech, 14841-1-AP, 1:1000), Flag-tag (Proteintech, 20543-1-AP, 1:4000), HA-tag (Proteintech, 51064-2-AP, 1:4000), Myc-tag (Proteintech, 16286-1-AP, 1:4000), Ubiquitin (CST, 3936, 1:1000), Cyt c (Proteintech, 10993-1-AP, 1:1000), and COXIV (Proteintech, 11242-1-AP, 1:2000). .. After three washes with TBST, membranes were incubated with HRP-conjugated secondary antibodies (ZSGBBIO, ZB-2301/ZB-2305, 1:4000) at room temperature for 1 h. Protein bands were visualized using HRP chemiluminescent substrate (Millipore, USA) and imaged with the Tanon 5200 Multi System.

Article Title: Xin-Ji-Er-Kang improves MIR injury-induced heart failure via the Calpain1/Bid signaling pathway.
Article Snippet: Ethnopharmacological relevance: Xin-Ji-Er-Kang (XJEK) is a clinically verified formula derived from the principles of Xin'an medicine, and is used for the treatment of myocarditis.. It has also demonstrated robust cardioprotective effects in various animal models of cardiovascular diseases.. However, the specific mechanism by which XJEK alleviates heart failure (HF) through the attenuation of cardiomyocyte apoptosis remains unclear.

Article Title: Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage-Induced Mitochondrial Apoptosis and Parthanatos-Like Cell Death.
Article Snippet: .. The membranes were then blocked with a 5% non-fat milk TBST (TBS containing 0.1% Tween-20) for 1 h at room temperature and incubated at 4◦C for overnight with primary antibodies against the following proteins: cleaved Caspase 3 (25128-1-AP, Proteintech), cleaved Caspase 8 (9496, CST), PARP (9542, CST), cleaved PARP (9541, CST), P21 (2947, CST), P53 (2527, CST), Cyclin A2 (91500, CST), Cyclin D1 (2978, CST), CDK1 (bs-1341R, Bioss), CDK2 (bs-10726R, Bioss), CDK7 (bs-0569R, Bioss), AKT (4691, CST), p-AKT (4060, CST), ERK (9102, CST), p-ERK (9101, CST), MEK (9126, CST), p-MEK (9154, CST), ATR (13934, CST), p-ATR (2853, CST), Chk1 (2360, CST), p-Chk1 (2348, CST), RAD51 (14961-1-AP, Proteintech), ATM (27156-1-AP, Proteintech), p-ATM (5883, CST), γ-H2AX (9718, CST), AIF (5318, CST), MIF (75038, CST), Cyt c (10993-1-AP, Proteintech), Lamin B (66095-1-Ig, Proteintech), VDAC1 (81538-1-RR, Proteintech) and GAPDH (60004-1-Ig, Proteintech). .. Following primary antibody incubation, the membranes were washed again with TBST and incubated with HRP-conjugated goat anti-mouse IgG (H + L) (SA00001-1, Proteintech) and goat anti-rabbit IgG (H + L) (SA00001-2, Proteintech) for 1 h at room temperature.

Ubiquitin Proteomics:

other:

Article Title: Mn 3 O 4 -potentiated bifunctional hydrogel for mild temperature-controlled tumor ablation and osteogenesis
Article Snippet: Antibodies used in this study included: Cleaved caspase-3, Caspase-3, Cyt-c, Bax, Bcl-2, p-ERK, ERK, p-MEK, MEK, and GAPDH (Proteintech).

Nucleic Acid Electrophoresis:

Membrane:

Image Search Results

PolG Mut mitochondria possess selective impairments to NAD-linked Respiration (A) Schematic depiction of the substrates and inhibitors added during the OxPhos kinetics assay. Mitochondrial oxygen consumption ( J O 2 ) across OxPhos kinetics assay in mitochondria isolated from (B) BAT, (C) brain, (D) colon, (E) heart, (F) kidney, (G) Liver, (H) and lung tissue. Ratio of maximal complex I (CI) versus CII-supported mitochondrial J O 2 (I). N = 4–6 per group. Data are presented as mean ± SEM and analyzed using multiple unpaired t tests ( B–5H) or unpaired t test ( I), ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Substrates utilized are indicated as follows: creatine kinase (CK; 20 U/mL), ATP (5 mM), phospho-creatine (PCr; 1 mM), cytochrome c (Cyt C; 10 μM; pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), glutamate (Glut; 5 mM), rotenone (Rot; 0.5 μM), succinate (Succ; 5 mM) oligomycin (Oligo; 0.02 μM), malonate (Malo; 20 mM), calcium chloride (CaCl 2 ; 0.6 mM) glycerol-3-phosphate (G3P; 10 mM), and antimycin A (Ant A; 0.5 μM). Graphics were generated using BioRender.

Journal: iScience

Article Title: Accumulated mtDNA mutations are linked to specific impairments in NADH-linked respiration

doi: 10.1016/j.isci.2026.115184

Figure Lengend Snippet: PolG Mut mitochondria possess selective impairments to NAD-linked Respiration (A) Schematic depiction of the substrates and inhibitors added during the OxPhos kinetics assay. Mitochondrial oxygen consumption ( J O 2 ) across OxPhos kinetics assay in mitochondria isolated from (B) BAT, (C) brain, (D) colon, (E) heart, (F) kidney, (G) Liver, (H) and lung tissue. Ratio of maximal complex I (CI) versus CII-supported mitochondrial J O 2 (I). N = 4–6 per group. Data are presented as mean ± SEM and analyzed using multiple unpaired t tests ( B–5H) or unpaired t test ( I), ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001. Substrates utilized are indicated as follows: creatine kinase (CK; 20 U/mL), ATP (5 mM), phospho-creatine (PCr; 1 mM), cytochrome c (Cyt C; 10 μM; pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), glutamate (Glut; 5 mM), rotenone (Rot; 0.5 μM), succinate (Succ; 5 mM) oligomycin (Oligo; 0.02 μM), malonate (Malo; 20 mM), calcium chloride (CaCl 2 ; 0.6 mM) glycerol-3-phosphate (G3P; 10 mM), and antimycin A (Ant A; 0.5 μM). Graphics were generated using BioRender.

Article Snippet: Following freeze fracture, 20μg of mitochondria were added to Respiration Buffer in the Oroboros O2k system followed by Cyt C (10μM).

Techniques: Isolation, Generated

Respiratory capacity within the electron transport system remains intact in PolG Mut mice (A–H) Schematic representing the maximal respiratory capacity protocol. Real-time oxygen consumption ( J O 2 ) in mitochondria isolated from (B) BAT, (C) brain, (D) colon, (E) heart, (F) kidney, (G) Liver, (H) and lung following serial titration of the mitochondrial uncoupling agent, carbonyl cyanide- p -trifluoromethoxyphenylhydrazone (FCCP, FC; 0.25 μM). (I) Maximal mitochondrial respiration achieved during FCCP titration. N = 5–6 per group, Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001 depict significant post hoc LSD by two-way ANOVA; main effect PolG ( B–4H) or unpaired t test ( I). Substrates utilized are indicated as follows: pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), succinate (Succ; 5 mM) cytochrome c (Cyt C, 10 μM). Graphics were generated using BioRender.

Journal: iScience

Article Title: Accumulated mtDNA mutations are linked to specific impairments in NADH-linked respiration

doi: 10.1016/j.isci.2026.115184

Figure Lengend Snippet: Respiratory capacity within the electron transport system remains intact in PolG Mut mice (A–H) Schematic representing the maximal respiratory capacity protocol. Real-time oxygen consumption ( J O 2 ) in mitochondria isolated from (B) BAT, (C) brain, (D) colon, (E) heart, (F) kidney, (G) Liver, (H) and lung following serial titration of the mitochondrial uncoupling agent, carbonyl cyanide- p -trifluoromethoxyphenylhydrazone (FCCP, FC; 0.25 μM). (I) Maximal mitochondrial respiration achieved during FCCP titration. N = 5–6 per group, Data are presented as mean ± SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001 depict significant post hoc LSD by two-way ANOVA; main effect PolG ( B–4H) or unpaired t test ( I). Substrates utilized are indicated as follows: pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), succinate (Succ; 5 mM) cytochrome c (Cyt C, 10 μM). Graphics were generated using BioRender.

Article Snippet: Following freeze fracture, 20μg of mitochondria were added to Respiration Buffer in the Oroboros O2k system followed by Cyt C (10μM).

Techniques: Isolation, Titration, Generated

Mitochondrial respiratory phenotypes are maintained in permeabilized tissue (A) Tissue slices were permeabilized in saponin before assessment of oxygen consumption ( J O 2 ). (B) Intact colon, (C) heart, and (D) liver J O 2 under multiple substrate conditions. (E) Ratio of complex I (CI) versus CII-supported respiration. (F) Dose-response to FCCP titration and (G) maximal respiratory capacity in intact bone marrow-derived mononuclear cells (BMMCs). (H) Mitochondrial J O 2 during OxPhos kinetics technique in permeabilized BMMCs. (I) Ratio of CI versus CII-supported respiration in permeabilized BMMCs. N = 5 per group. Data are presented as mean ± SEM, p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001,∗∗∗∗ p < 0.00001 depict significant multiple unpaired t tests ( A–6C and 6G), and unpaired t test ( D–6F and 6H). Substrates utilized are indicated as follows: creatine kinase (CK; 20 U/mL), ATP (5 mM), phospho-creatine (PCr; 1 mM), cytochrome c (Cyt C; 10 μM), pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), glutamate (Glut; 5 mM), rotenone (Rot; 0.5 μM), succinate (Succ; 5 mM) oligomycin (Oligo; 0.02 μM), malonate (Malo; 20 mM), calcium chloride (CaCl 2 ; 0.6 mM) glycerol-3-phosphate (G3P; 10 mM) antimycin A (Ant A; 0.5 μM), and carbonyl cyanide- p -trifluoromethoxyphenylhydrazone (FCCP, FC; 0.25 μM). Graphics were generated using BioRender.

Journal: iScience

Article Title: Accumulated mtDNA mutations are linked to specific impairments in NADH-linked respiration

doi: 10.1016/j.isci.2026.115184

Figure Lengend Snippet: Mitochondrial respiratory phenotypes are maintained in permeabilized tissue (A) Tissue slices were permeabilized in saponin before assessment of oxygen consumption ( J O 2 ). (B) Intact colon, (C) heart, and (D) liver J O 2 under multiple substrate conditions. (E) Ratio of complex I (CI) versus CII-supported respiration. (F) Dose-response to FCCP titration and (G) maximal respiratory capacity in intact bone marrow-derived mononuclear cells (BMMCs). (H) Mitochondrial J O 2 during OxPhos kinetics technique in permeabilized BMMCs. (I) Ratio of CI versus CII-supported respiration in permeabilized BMMCs. N = 5 per group. Data are presented as mean ± SEM, p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001,∗∗∗∗ p < 0.00001 depict significant multiple unpaired t tests ( A–6C and 6G), and unpaired t test ( D–6F and 6H). Substrates utilized are indicated as follows: creatine kinase (CK; 20 U/mL), ATP (5 mM), phospho-creatine (PCr; 1 mM), cytochrome c (Cyt C; 10 μM), pyruvate (Pyr; 5 mM), malate (Mal; 1 mM), octanoyl-carnitine (Oct; 0.2 mM), glutamate (Glut; 5 mM), rotenone (Rot; 0.5 μM), succinate (Succ; 5 mM) oligomycin (Oligo; 0.02 μM), malonate (Malo; 20 mM), calcium chloride (CaCl 2 ; 0.6 mM) glycerol-3-phosphate (G3P; 10 mM) antimycin A (Ant A; 0.5 μM), and carbonyl cyanide- p -trifluoromethoxyphenylhydrazone (FCCP, FC; 0.25 μM). Graphics were generated using BioRender.

Article Snippet: Following freeze fracture, 20μg of mitochondria were added to Respiration Buffer in the Oroboros O2k system followed by Cyt C (10μM).

Techniques: Titration, Derivative Assay, Generated

ACO2 overexpression protected against LIRI in mice. (A) Schematic of AAV9-mediated ACO2-OE in I/R mice. (B–C) ACO2 expression levels assessed by RT-qPCR and western blot. (D) Blood gas parameters (PaO 2 and PaCO 2 ) following I/R injury. (E) Representative H&E-stained lung sections (scale bars = 20/50 μm, Black arrow: Alveolar expansion; Red arrow: Hemorrhage; Green arrow: Alveolar septum thickening and inflammatory cell infiltration). (F–G) Quantitative assessment of lung injury via histopathological scoring and wet/dry weight ratio. (H) Total cells count and protein concentration in BALF. (I) The mRNA expression of pro-inflammatory cytokines ( IL-6 , IL-1β , and TNF-α ). (J–K) Oxidative stress markers: T-AOC and MDA. (L) Apoptosis-related gene expression ( caspase 9 , Bcl-2, BAX , and Cyt-c ). (M) Mitochondrial respiratory function measured by OCR. (N) Serum Cyt-c release. (O) TUNEL staining for apoptosis detection (scale bar = 20 μm). Data are presented as the mean ± SD; n = 6; ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001.

Journal: Redox Biology

Article Title: Unveiling a novel function of Aconitase-2: attenuating lung ischemia-reperfusion injury via inhibition of pulmonary endothelial apoptosis

doi: 10.1016/j.redox.2026.104016

Figure Lengend Snippet: ACO2 overexpression protected against LIRI in mice. (A) Schematic of AAV9-mediated ACO2-OE in I/R mice. (B–C) ACO2 expression levels assessed by RT-qPCR and western blot. (D) Blood gas parameters (PaO 2 and PaCO 2 ) following I/R injury. (E) Representative H&E-stained lung sections (scale bars = 20/50 μm, Black arrow: Alveolar expansion; Red arrow: Hemorrhage; Green arrow: Alveolar septum thickening and inflammatory cell infiltration). (F–G) Quantitative assessment of lung injury via histopathological scoring and wet/dry weight ratio. (H) Total cells count and protein concentration in BALF. (I) The mRNA expression of pro-inflammatory cytokines ( IL-6 , IL-1β , and TNF-α ). (J–K) Oxidative stress markers: T-AOC and MDA. (L) Apoptosis-related gene expression ( caspase 9 , Bcl-2, BAX , and Cyt-c ). (M) Mitochondrial respiratory function measured by OCR. (N) Serum Cyt-c release. (O) TUNEL staining for apoptosis detection (scale bar = 20 μm). Data are presented as the mean ± SD; n = 6; ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001.

Article Snippet: Contents of MDA (Cat. No: A003-1-2 ), MPO (Cat. No: A044-1-1), GSH (Cat. No: A006-2-1), T-AOC (Cat. No: A015-2-1), SOD (Cat. No: A001-3-2), and Cyt-c (Cat. No: H190-1-2) were quantified using commercial kits (Nanjing Jiancheng Bioengineering Institute) with a UV-VIS spectrophotometer.

Techniques: Over Expression, Expressing, Quantitative RT-PCR, Western Blot, Staining, Protein Concentration, Gene Expression, TUNEL Assay

ACO2-KO exacerbated mitochondrial damage and apoptosis in HUVECs. (A–B) Validation of ACO2-KO efficiency by RT-qPCR and western blot. (C) Representative TEM images showing mitochondrial ultrastructural changes. The red arrows indicate the disappearance of mitochondrial cristae. (D) Cellular ATP contents measured by enzymatic assay. (E) The mtDNA copy number assessed via quantification of mitochondrial genes (ND-1, COX I, and COX IV). (F) Mitochondrial superoxide production detected by MitoSOX Red staining (scale bar = 20 μm). (G) Mitochondrial respiratory function measured by OCR. (H–I) Metabolomic analysis of TCA cycle intermediates: itaconate and isocitrate. (J) The mRNA expression of apoptosis-related genes ( Bcl-2, BAX, and Caspase-9 ). (K) Cyt-c release from mitochondria. (L) Apoptosis evaluation by TUNEL staining (scale bar = 20 μm). Data are presented as the mean ± SD; n = 3; ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001.

Journal: Redox Biology

Article Title: Unveiling a novel function of Aconitase-2: attenuating lung ischemia-reperfusion injury via inhibition of pulmonary endothelial apoptosis

doi: 10.1016/j.redox.2026.104016

Figure Lengend Snippet: ACO2-KO exacerbated mitochondrial damage and apoptosis in HUVECs. (A–B) Validation of ACO2-KO efficiency by RT-qPCR and western blot. (C) Representative TEM images showing mitochondrial ultrastructural changes. The red arrows indicate the disappearance of mitochondrial cristae. (D) Cellular ATP contents measured by enzymatic assay. (E) The mtDNA copy number assessed via quantification of mitochondrial genes (ND-1, COX I, and COX IV). (F) Mitochondrial superoxide production detected by MitoSOX Red staining (scale bar = 20 μm). (G) Mitochondrial respiratory function measured by OCR. (H–I) Metabolomic analysis of TCA cycle intermediates: itaconate and isocitrate. (J) The mRNA expression of apoptosis-related genes ( Bcl-2, BAX, and Caspase-9 ). (K) Cyt-c release from mitochondria. (L) Apoptosis evaluation by TUNEL staining (scale bar = 20 μm). Data are presented as the mean ± SD; n = 3; ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, and ∗∗∗∗ P < 0.0001.

Techniques: Biomarker Discovery, Quantitative RT-PCR, Western Blot, Enzymatic Assay, Staining, Metabolomic, Expressing, TUNEL Assay

4-OI rescued mitochondrial dysfunction after ACO2-KO in HUVECs. (A) Mitochondrial mass assessed by MitoTracker staining (scale bar = 20 μm). (B) Mitochondrial respiratory function measured by OCR. (C) Mitochondrial membrane potential evaluated using JC-1 staining (scale bar = 20 μm). (D) Activities of mitochondrial ETC complexes. (E) Protein contents of ETC complex subunits. (F–G) Metabolic ratios of NAD + /NADH and ATP/ADP. (H–I) The mRNA expression of apoptosis-related genes ( caspase-9 and BAX ). (J) Apoptosis-related protein contents (cleaved caspase-3, Bcl-2, and BAX) analyzed by western blot with semi-quantitative analysis. (K) Cyt-c release from mitochondria. (L) Apoptosis evaluation by TUNEL staining (scale bar = 20 μm). Data are presented as the mean ± SD; n = 3; ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001.

Journal: Redox Biology

Article Title: Unveiling a novel function of Aconitase-2: attenuating lung ischemia-reperfusion injury via inhibition of pulmonary endothelial apoptosis

doi: 10.1016/j.redox.2026.104016

Figure Lengend Snippet: 4-OI rescued mitochondrial dysfunction after ACO2-KO in HUVECs. (A) Mitochondrial mass assessed by MitoTracker staining (scale bar = 20 μm). (B) Mitochondrial respiratory function measured by OCR. (C) Mitochondrial membrane potential evaluated using JC-1 staining (scale bar = 20 μm). (D) Activities of mitochondrial ETC complexes. (E) Protein contents of ETC complex subunits. (F–G) Metabolic ratios of NAD + /NADH and ATP/ADP. (H–I) The mRNA expression of apoptosis-related genes ( caspase-9 and BAX ). (J) Apoptosis-related protein contents (cleaved caspase-3, Bcl-2, and BAX) analyzed by western blot with semi-quantitative analysis. (K) Cyt-c release from mitochondria. (L) Apoptosis evaluation by TUNEL staining (scale bar = 20 μm). Data are presented as the mean ± SD; n = 3; ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001.

Techniques: Staining, Membrane, Expressing, Western Blot, TUNEL Assay

Journal: Advanced Science

Article Title: Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death

doi: 10.1002/advs.202511406

Figure Lengend Snippet: HIF disrupts mitochondrial homeostasis and decreases ATP production. (A–C) Representative immunofluorescence images show the subcellular localization and nuclear translocation of AIF, MIF, and Cytochrome c (Cyt c) in HCT15 and HCT116 cells following 24 h HIF treatment. (D, E) Quantification of intracellular reactive oxygen species (ROS) levels in HCT15 and HCT116 cells, respectively. (F, G) Quantification of mitochondrial ROS intensity using mitoSOX staining in HCT15 and HCT116 cells, respectively. (H, I) Oxygen consumption rate (OCR) fluorescence intensity in HCT15 and HCT116 cells, reflecting changes in mitochondrial respiration. (J, K) Relative intracellular ATP levels in HCT15 and HCT116 cells following HIF treatment. (L) Flow cytometric analysis of mitochondrial membrane potential (Δψm) in HCT15 and HCT116 cells after HIF treatment, assessed using JC‐1 staining. The red‐to‐green fluorescence intensity ratio was used to quantify alterations in membrane potential (right panels). ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: The membranes were then blocked with a 5% non‐fat milk TBST (TBS containing 0.1% Tween‐20) for 1 h at room temperature and incubated at 4°C for overnight with primary antibodies against the following proteins: cleaved Caspase 3 (25128‐1‐AP, Proteintech), cleaved Caspase 8 (9496, CST), PARP (9542, CST), cleaved PARP (9541, CST), P21 (2947, CST), P53 (2527, CST), Cyclin A2 (91500, CST), Cyclin D1 (2978, CST), CDK1 (bs‐1341R, Bioss), CDK2 (bs‐10726R, Bioss), CDK7 (bs‐0569R, Bioss), AKT (4691, CST), p‐AKT (4060, CST), ERK (9102, CST), p‐ERK (9101, CST), MEK (9126, CST), p‐MEK (9154, CST), ATR (13934, CST), p‐ATR (2853, CST), Chk1 (2360, CST), p‐Chk1 (2348, CST), RAD51 (14961‐1‐AP, Proteintech), ATM (27156‐1‐AP, Proteintech), p‐ATM (5883, CST), γ‐H2AX (9718, CST), AIF (5318, CST), MIF (75038, CST), Cyt c (10993‐1‐AP, Proteintech), Lamin B (66095‐1‐Ig, Proteintech), VDAC1 (81538‐1‐RR, Proteintech) and GAPDH (60004‐1‐Ig, Proteintech).

Techniques: Immunofluorescence, Translocation Assay, Staining, Fluorescence, Membrane

Journal: Advanced Science

Article Title: Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death

doi: 10.1002/advs.202511406

Figure Lengend Snippet: HIF suppresses CRC tumor growth in vivo. (A) Tumor growth in mouse models bearing HCT116 cells treated with HIF, 5‐FU, or the combination. (B) Final tumor weights were measured at the end of treatment across treatment groups. (C) Representative images of excised tumors from each group. (D) Body weight monitoring throughout the treatment period. (E, F) H&E and IHC analysis of tumor tissues for Ki67, Cyt c, c‐Caspase‐3, and c‐PARP, with corresponding quantification. (G) H&E and IHC staining of kidney and liver tissues to evaluate potential organ toxicity. (H–J) Immunofluorescence analysis of γ‐H2AX, AIF, and MIF localization in tumor tissues. Nuclei are stained with DAPI (blue), and target proteins appear in green. (K) Schematic representation illustrating the proposed mechanism by which HIF‐induced DNA damage leads to mitochondrial apoptosis and parthanatos‐mediated colorectal tumor cell death. ** p < 0.01, **** p < 0.0001.

Techniques: In Vivo, Immunohistochemistry, Immunofluorescence, Staining

Review

cyt c (Proteintech)

Structured Review

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1) Product Images from "Homoisoflavanone Delays Colorectal Cancer Progression via DNA Damage‐Induced Mitochondrial Apoptosis and Parthanatos‐Like Cell Death"

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