SOD2/MnSOD Antibody - #AF5144

FIGURE 3: Pro-inflammatory factors, anti-oxidant enzyme and cell signaling pathways in resveratrol (Res)- or vehicle-treated cystic kidneys. (A) TNF-α, MCP-1, CFB and SOD2 were analyzed by western blot in 9-week-old +/+ and Cy/+ kidneys. (B–E) Immunohistochemical staining for oxidative stress markers 8-OHdG and nitrotyrosine in the tubulointerstitial area. Computer-assisted morphometry was used to quantify changes of 8-OHdG and nitrotyrosine in each group. Scale bar = 50 µm. (F) NF-κB pathway ( p-p65, p65, p105 and p50) and mTOR pathway ( p-S6K and total S6K) were analyzed by western blot in 9-week-old +/+ and Cy/+ kidneys. Blots are representative of three independent experiments.

FIGURE 7 Effect of MLG on some protein levels in ethanol-induced gastric lesions mice. Some representative western blot bands (A). Protein levels of SOD1/GAPDH (B), SOD2/GAPDH (C), iNOS/GAPDH (D), nNOS/GAPDH (E), eNOS/GAPDH (F), COX2/GAPDH (G), p38/GAPDH (H) in mice gastric tissues. SOD1, Superoxide dismutase one or Cu/Zn-superoxide dismutase; SOD2/Mn SOD, superoxide dismutase 2. Control: the group administered zero ethanol; Model: the group administered ethanol intragastrically (13.25 ml/kg BW); MLG-L: low-dose (5 g/kg body weight) MLG-treated group; MLG-M: medium-dose (10 g/kg body weight) MLG-treated group; MLG-H: high-dose (20 g/kg body weight) MLG-treated group; CBP: the group receiving Colloid Bismuth Pectin (57 mg/kg body weight). Each group’s data was expressed as mean ± standard deviation (SD), n = 6. By one-way analysis of variance (ANOVA) test, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 vs. each group. Whole page of western blot can be found in Supplementary Figures S1, S3, S7, S8, S10, S14, S15, respectively.

FIGURE 7 (A,B) Western blot along with its quantification revealed that the level of P-PI3K, P-Akt and Nrf2 as treated above (C,D) Western blot along with its quantification revealed that the level of HO-1, NQO1, GCLc, GCLm and TrxR1 (E,F) The IHC result of SOD2 and HO-1 expression in skin flaps (scale bar: 50 μm) **p ≤ 0.01 compared to the control group; ##p ≤ 0.01 compared to the FMNT-H group.

FIGURE 6 IR-61 activated Nrf2 and increased antioxidant-related protein levels. (A–G) Western blot analysis of Nrf2, Keap1, HO-1, GPX-1, SOD-1, and SOD-2 in bladder tissue and quantitative analysis. Data indicate the mean ± SD (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 vs. control group, #p < 0.05, p < 0.01, ###p < 0.001, ####p < 0.0001 vs. DBD group).

Figure 5. | S58 promotes antioxidant defense of TGF-β2-induced HConFs. (A) Analysis of antioxidant capacity of cells at day 14 after GFS. (B) Intracellular ROS variation, and (C) mitochondrial superoxide variation were examined by flow cytometry. (D) Antioxidant protein SOD1/2, γ-GCS and CAT levels analyzed by western blotting in TGF-β2-treated HConFs in the presence or absence of S58 (20 nM). (E) Relative antioxidant gene levels in HConFs preconditioned with TGF-β2 in the presence or absence of S58 (20 nM) for 12h. All data indicate the mean ± SD, n=3. *p < 0.05, **p < 0.01, ***p < 0.001.

Figure 3. CPT1C overexpression attenuated oxidative stress in Aβ25-35-induced HT22 cells. Following transfection of Ov-CPT1C or Ov-NC for 24 h, HT22 cells were treated with Aβ25–35 for another 24 h (a) ROS expression was detected using ROS kits. (b) MDA levels and SOD activity were measured using MDA and SOD kits, respectively. (c) The relative mRNA and protein expression of SOD1 and SOD2 in A25-35-induced HT22 cells were measured using RT-qPCR and western blot, respectively. ***P < 0.001 vs. Control group, ##P < 0.01 and ###P < 0.001 vs A25-35 + Ov-NC.