anti-human nrf2 rabbit polyclonal igg sc-13032 h300  (Santa Cruz Biotechnology)

Journal: Scientific Reports

Article Title: Forensic significance of intracardiac expressions of Nrf2 in acute myocardial ischemia

doi: 10.1038/s41598-024-54530-x

Figure Lengend Snippet: Expression of Nrf2 in the human heart. ( A ) Immunohistochemical analysis using anti-Nrf2. Representative results from hearts of non-AIHD and AIHD groups are shown. Scale bar, 50μm. ( B ) Morphometrical analysis was performed to measure the number of Nrf2 + cells in each group. Mean and standard error of the number of Nrf2 + cells per high power field (hpf) in each group. ** P < 0.01 indicates a statistically significant difference. ( C ) Relationship between age, sex, or PMI and appearance of Nrf2 + cells in all cases; P values were determined using Spearman's correction coefficient by rank test as previously described .

Article Snippet: In this study, following polyclonal or monoclonal Abs (pAbs or mAbs) were used for immunohistochemical analyses in the present study: rabbit anti-human Nrf2 pAbs (bs-1074R, Bioss antibodies, Woburn, MA), rabbit anti-human fibronectin pAbs (15613-1-AP, Proteintec, Rosemont, IL), rabbit anti-human C5b-9 pAbs (bs-2673R, Bioss antibodies).

Techniques: Expressing, Immunohistochemical staining

Journal: Frontiers in Pharmacology

Article Title: Targeting Cytokine Release Through the Differential Modulation of Nrf2 and NF-κB Pathways by Electrophilic/Non-Electrophilic Compounds

doi: 10.3389/fphar.2020.01256

Figure Lengend Snippet: Nrf2 nuclear translocation and modulation of HO-1 protein content in THP-1 cells. (A) THP-1 cells were treated with compounds 1 – 4 and CURC at a concentration of 5 μM for 3 h. After isolation, nuclear extracts were examined by Western blot analysis and Nrf2 expression was determined using an anti-Nrf2 antibody. Anti-lamin A/C was used as protein loading control. Results are shown as means of Nrf2/lamin A/C ratio ± SEM. Dunnett’s multiple comparison test; ** p < 0.01 and **** p < 0.0001 versus CTR; n = 5–7. (B) Total protein extracts of THP-1 cells, treated with compounds 1 – 4 and CURC at the concentration of 5 μM for 24 h, were analyzed for HO-1 protein content by Western blot analysis. Anti-tubulin was used as protein loading control. Results are shown as means of HO-1/Tubulin ratio ± SEM. Dunnett’s multiple comparison test; ** p < 0.01 and **** p < 0.0001 versus CTR; n = 7.

Article Snippet: Rabbit polyclonal anti-human Nrf2 (NBP1-32822) and anti-human HO-1 (NBP1-31341) antibodies were purchased from Novus (Biotechne, Minneapolis USA).

Techniques: Translocation Assay, Concentration Assay, Isolation, Western Blot, Expressing, Comparison

Journal: Frontiers in Pharmacology

Article Title: Targeting Cytokine Release Through the Differential Modulation of Nrf2 and NF-κB Pathways by Electrophilic/Non-Electrophilic Compounds

doi: 10.3389/fphar.2020.01256

Figure Lengend Snippet: Optimization of Nfr2-silenced THP-1 model (A) and effect of Nrf2-knockdown on modulation of TNFα release by compounds 1, 3 and 4, upon LPS stimulation (B) . (A) THP-1 cells were treated either with vehicle (WT), scrambled or siRNA Nrf2 for 24 h. Where indicated MG132 was added 4 h before the end of the experiment to block the proteasomal degradation of Nrf2. After treatments, Nrf2 expression was determined in total protein extracts by Western blot analysis using an anti-Nrf2 antibody. Anti-α-tubulin was used as protein loading control. Results are shown as means of Nrf2/α-Tubulin ratio ± SEM. Unpaired Student t -test; ** p < 0.01; n = 3. (B) TNFα amount was measured in the supernatants of THP-1 Nrf2-knockdown cells, treated with compounds 1, 3, and 4 at a concentration of 5 μM for 24 h and then stimulated with 10 ng/mL LPS for 3 h. The protein secretion of TNFα was determined by ELISA. Data are shown as means of stimulation index ± SEM. Dunnett’s multiple comparison test; *** p < 0.001 and **** p < 0.0001 versus WT LPS; ## p < 0.01 and #### p < 0.0001 versus siRNA Nrf2 LPS; n = 3.

Article Snippet: Rabbit polyclonal anti-human Nrf2 (NBP1-32822) and anti-human HO-1 (NBP1-31341) antibodies were purchased from Novus (Biotechne, Minneapolis USA).

Techniques: Blocking Assay, Expressing, Western Blot, Concentration Assay, Enzyme-linked Immunosorbent Assay, Comparison

Journal: Frontiers in Pharmacology

Article Title: Targeting Cytokine Release Through the Differential Modulation of Nrf2 and NF-κB Pathways by Electrophilic/Non-Electrophilic Compounds

doi: 10.3389/fphar.2020.01256

Figure Lengend Snippet: Differential modulation of Nrf2 and NF-κB intracellular signaling pathways by compounds. Electrophile 1, carrying both the catechol moiety (red) and the α,β-unsaturated carbonyl group (blue), is the most active Nrf2 inducer, while being devoid of activity on NF-kB pathway. Conversely, the non-electrophilic compound 4, synthesized to exclude eventual oxidative transformation of the methoxyphenol ring (green) of 3 into reactive metabolites, is the most potent NF-kB inhibitor, with no impact on Nrf2 activation.

Article Snippet: Rabbit polyclonal anti-human Nrf2 (NBP1-32822) and anti-human HO-1 (NBP1-31341) antibodies were purchased from Novus (Biotechne, Minneapolis USA).

Techniques: Activity Assay, Synthesized, Transformation Assay, Activation Assay

Journal: Frontiers in Pharmacology

Article Title: Targeting Cytokine Release Through the Differential Modulation of Nrf2 and NF-κB Pathways by Electrophilic/Non-Electrophilic Compounds

doi: 10.3389/fphar.2020.01256

Figure Lengend Snippet: Schematic representation of the effects induced by compounds 1 – 4 on Nrf2 and NF-κB pathways.

Article Snippet: Rabbit polyclonal anti-human Nrf2 (NBP1-32822) and anti-human HO-1 (NBP1-31341) antibodies were purchased from Novus (Biotechne, Minneapolis USA).

Techniques:

Journal: Cells

Article Title: Activation of Nrf2/HO-1 Pathway and Human Atherosclerotic Plaque Vulnerability: An In Vitro and In Vivo Study

doi: 10.3390/cells8040356

Figure Lengend Snippet: Nrf2 levels in CAD patients and healthy subjects. ( a , b ) Nrf2 levels in ( a ) total cellular lysate, ( b ) nuclear and cytosolic compartments were detected by western blot analysis. β-actin was used as a control of protein loading. Densitometry is shown in the bar graph. Data are expressed as mean ± SD and derive ( a ) from MDMs obtained from 10 healthy subjects and 17 CAD patients; ( b ) from MDMs obtained from 5 healthy subjects and 5 CAD patients. ( c ) Representative images of Nrf2 in round and spindle MDMs obtained from healthy subjects and CAD patients (400× original magnification), nuclei were visualized by Hoechst 33258. ( d ) Quantitative analysis of Nrf2 in round and spindle MDMs. Data are expressed as mean ± SD of fluorescence intensity/µm 2 (at least three fields, 400× magnification, were analyzed) and derive from independent cultures obtained from 10 healthy subjects and 30 CAD patients (SA n = 10; NSTEMI n = 10; STEMI n = 10). * p < 0.05, ** p < 0.01, vs. healthy subjects.

Article Snippet: Fixed MDMs were incubated overnight at 4 °C with a monoclonal rabbit anti-human HO-1 antibody (1:100) (Abcam), or with a polyclonal rabbit anti-human Nrf2 antibody (1:200) (Santa Cruz Biotechnology).

Techniques: Western Blot, Control, Fluorescence

Journal: Molecular Medicine Reports

Article Title: Intranasal erythropoietin ameliorates neurological function impairments and neural pathology in mice with chronic alcoholism by regulating autophagy-related Nrf2 degradation

doi: 10.3892/mmr.2018.9706

Figure Lengend Snippet: Intranasal rhEPO exerts neuroprotective effects by regulating autophagy-related Nrf2 degradation in mice with chronic alcoholism. (A) Images of western blot analyses for hEPO, phosphorylated (p)-EPOR, p-ERK1/2, p-AKT, Nrf2, KEAP1, NQO1, p62 and LC3-II in brain tissue of mice in each group. (B-I) The quantitative analyses of the relative p-EPOR (B), p-ERK1/2 (C), p-AKT (D), Nrf2 (E), KEAP1 (F), NQO1 (G), p62 (H) and LC3-II (I) levels to β-actin in brain tissue of mice in each group (n=8). Error bars indicate SEM. ns, non-significant; *P<0.05; **P<0.01; ***P<0.001. Groups: Control, Chronic Alcohol Exposure (CAE), CAE + recombinant human erythropoietin (rhEPO) and CAE+rhEPO+all- trans -retinoic acid (ATRA).

Article Snippet: The following primary antibodies were used: mouse monoclonal anti-human hEPO (catalog no. SAB5300475; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat p-EPOR (catalog no. SAB4301492; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat p-ERK1/2 (catalog no. E7028; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat p-AKT (catalog no. SAB4301497; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat Nrf2 (catalog no. SAB4501984; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat KEAP1 (catalog no. AV34727; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat NQO1 (catalog no. N5288; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat p62 (catalog no. P0067; Sigma-Aldrich; Merck KGaA), rabbit polyclonal anti-human/mouse/rat LC3B (catalog no. 3868; Cell Signaling Technology, Inc.) and rabbit polyclonal anti-human/mouse/rat β-actin (catalog no. SAB2100037; Sigma-Aldrich; Merck KGaA) (IgGs; 1:1,000). β-actin expression was used as a loading control.

Techniques: Western Blot, Recombinant