SOD1 Antibody - #AF5198

Fig. 2 Chlorogenic acid-induced protection of brain post-hypoxic-ischemic brain injury via the down-regulation of expression of inflammatory and oxidative stress levels. a The IL-1 β level in brain tissue 24 h after HI brain injury measured by Elisa kit. ∗P < 0.05 vs. the sham group. ##P < 0.01 vs. the HI group. n=3. b The MDA level in brain tissue 24 h after HI brain injury by MDA kit. ∗∗∗P < 0.001 vs. the sham group. #P < 0.05 vs. the HI group. n=3. c The CAT level in brain tissue 24 h after HI brain injury by CAT kit. ∗∗∗P < 0.001 vs. the sham group. #P < 0.05 vs. the HI group. n=3. d Western blot detection of the protein levels of iNOS, SOD2/MnSOD, TNF-α, pre-IL-1β and mature- IL-1β 24h after HI injury. e–h Quantification of western blot data of iNOS, SOD2/MnSOD, TNF-α, and mature-IL-1 β. ∗∗P < 0.01 and ∗∗∗P < 0.001 vs. the sham group. #P < 0.05, ##P < 0.01 and ###P < 0.001 vs. the HI group. n = 3

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 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.

Fig. 6 |NBP upregulated PI3k/Akt/Nrf2 signaling pathway and downstream antioxidant enzymes, including HO-1, GSH, SOD1, and SOD2, analyzed by western blot. Data are expressed as means + SD. *P < 0.05 versus Sham group; #P < 0.05 versus MI group

Figure 2 LINC00987 inhibited cell apoptosis, oxidative stress, inflammation and autophagy in LPS-mediated 16HBE and BEAS-2B cells. (A) The transfection efficiency of LINC00987 was detected by RT-qPCR in LPS-induced 16HBE and BEAS-2B cells. (B and C) The effects of LPS treatment and LINC00987 overexpression on LINC00987 and let-7b-5p expression were demonstrated by RT-qPCR. (D) CCK-8 assay was performed to illustrate the impacts between LPS and LINC00987 on cell viability in 16HBE and BEAS-2B cells. (E and F) Caspase3 activity and apoptosis analysis assays were conducted to present the influences between LPS and LINC00987 overexpression on caspase3 activity and cell apoptosis, respectively, in 16HBE and BEAS-2B cells. (G and H) ROS detection kit and SOD activity assays were carried out to uncover the impacts between LPS and enforced LINC00987 expression on oxidative stress in 16HBE and BEAS-2B cells. (I) Western blot assay was employed to determine the impacts of LINC00987 on the protein levels of pro-c3, cleaved-c3, SOD1, SOD2 and SOD3 in LPS-induced 16HBE and BEAS-2B cells. (J and K) ELISA kit assays were employed to exhibit the effects between LPS exposure and LINC00987 on the production of IL-6 and IL-8 in 16HBE and BEAS-2B cells. (L) The effects of LPS treatment and LINC00987 overexpression on the level of IC3-II/IC3-I and the protein expression of ATG5 and P62 were demonstrated by Western blot in 16HBE and BEAS-2B cells. *P<0.05, **P<0.01 and ***P<0.001.

Figure 8.The combination of Que and 5-FU attenuated the Nrf2/HO-1 pathway-related marker levels of CC cells and 5-FU-resistant CC cells. After cells were treated with 10 μg/mL 5-FU, 40 μM Que, or 40 μM Que plus 10 μg/mL 5-FU, Western blotting was used to examine the Nrf2/HO-1 pathway-related factors level in CC cells (A) and 5-FU-resistant CC cells (B); n=3. Que, quercetin; 5-FU, 5-fluorouracil; CC, colon cancer.