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primary antibodies that targeted nrf2  (Proteintech)


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    Proteintech primary antibodies that targeted nrf2
    Orientin suppresses ferroptosis via activation of the <t>Nrf2/GPX4</t> signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.
    Primary Antibodies That Targeted Nrf2, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibodies that targeted nrf2/product/Proteintech
    Average 90 stars, based on 1 article reviews
    primary antibodies that targeted nrf2 - by Bioz Stars, 2026-02
    90/100 stars

    Images

    1) Product Images from "Orientin promotes diabetic wounds healing by suppressing ferroptosis via activation of the Nrf2/GPX4 pathway"

    Article Title: Orientin promotes diabetic wounds healing by suppressing ferroptosis via activation of the Nrf2/GPX4 pathway

    Journal: Food Science & Nutrition

    doi: 10.1002/fsn3.4360

    Orientin suppresses ferroptosis via activation of the Nrf2/GPX4 signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.
    Figure Legend Snippet: Orientin suppresses ferroptosis via activation of the Nrf2/GPX4 signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Techniques Used: Activation Assay, In Vitro, Binding Assay, Expressing, Western Blot, Fluorescence, Comparison

    Inhibition of ferroptosis and improving HUVECs function by Orientin can be regulated by Nrf2–siRNA. (a and d) Evaluation of the neovascularization of HUVECs induced by Orientin using the tube formation assay in a variety of different groups. (b and e) Evaluation of the effect of Orientin on the migration of HUVECs using the transwell system in various groups. (c and f) Comparison of the levels of Orientin‐mediated HUVECs adhesion using a cell‐matrix adhesion assay in each of the different groups. (g and i) Western blot analysis of the expression of AAMP and VEGF‐A in HUVECs. (h and j) Western blot analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. (k and l) Quantitative analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.
    Figure Legend Snippet: Inhibition of ferroptosis and improving HUVECs function by Orientin can be regulated by Nrf2–siRNA. (a and d) Evaluation of the neovascularization of HUVECs induced by Orientin using the tube formation assay in a variety of different groups. (b and e) Evaluation of the effect of Orientin on the migration of HUVECs using the transwell system in various groups. (c and f) Comparison of the levels of Orientin‐mediated HUVECs adhesion using a cell‐matrix adhesion assay in each of the different groups. (g and i) Western blot analysis of the expression of AAMP and VEGF‐A in HUVECs. (h and j) Western blot analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. (k and l) Quantitative analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Techniques Used: Inhibition, Tube Formation Assay, Migration, Comparison, Cell Adhesion Assay, Western Blot, Expressing

    Mechanisms of action of Orientin on HUVECs that have been induced by HG. Orientin promotes diabetic wound healing by activating the Nrf2/GPX4 pathway. It also decreases HG‐induced ferroptosis by reducing the accumulation of ROS and rescuing mitochondrial dysfunction in HUVECs.
    Figure Legend Snippet: Mechanisms of action of Orientin on HUVECs that have been induced by HG. Orientin promotes diabetic wound healing by activating the Nrf2/GPX4 pathway. It also decreases HG‐induced ferroptosis by reducing the accumulation of ROS and rescuing mitochondrial dysfunction in HUVECs.

    Techniques Used:



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    Orientin suppresses ferroptosis via activation of the <t>Nrf2/GPX4</t> signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.
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    Gas plasma-treated wounds showed a modulated gene expression and connective tissue stain dependent on wound healing stage. Ear wounds of mice were treated with gas plasma as described. ( a ) Gene expression levels of transforming growth factor ( TGFβ ) signaling including SMAD2, CDKN1A, and interleukin 1 ( IL1β ) on both endpoints. ( b ) Immunofluorescence analysis of TGFβ1 and staining quantification on d9 and d20. ( c ) Quantification of TGFβ1 staining on both time points. ( d ) Representative picrosirius red (PSR)-stained connective ear tissue on days 9 (left) or 20 (right) in gas plasma-treated (lower panel) compared to untreated ear wounds of mice (upper panel) showing granulation tissue with collagen fibers (red) in brightfield (left images) and fluorescence microscopy (right images). Enlarged graphs display higher magnification. ( e-f ) Quantification of PSR using ImageJ software compared to untreated ( e ) and healthy ( f ) ear tissue showing fiber intensity on d9 and d20. Data are presented as mean ± S.D. *p < 0.05, **p < 0.01, ***p < 0.001 when compared to control groups (ctrl) with Students t -test (a, c) or ANOVA (e-f). Scale bars are 200 µm (d), 100 µm (d, higher magnifications), and 50 µm (b). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Journal: Journal of Advanced Research

    Article Title: YAP/TAZ, beta-catenin, and TGFb pathway activation in medical plasma-induced wound healing in diabetic mice

    doi: 10.1016/j.jare.2024.07.004

    Figure Lengend Snippet: Gas plasma-treated wounds showed a modulated gene expression and connective tissue stain dependent on wound healing stage. Ear wounds of mice were treated with gas plasma as described. ( a ) Gene expression levels of transforming growth factor ( TGFβ ) signaling including SMAD2, CDKN1A, and interleukin 1 ( IL1β ) on both endpoints. ( b ) Immunofluorescence analysis of TGFβ1 and staining quantification on d9 and d20. ( c ) Quantification of TGFβ1 staining on both time points. ( d ) Representative picrosirius red (PSR)-stained connective ear tissue on days 9 (left) or 20 (right) in gas plasma-treated (lower panel) compared to untreated ear wounds of mice (upper panel) showing granulation tissue with collagen fibers (red) in brightfield (left images) and fluorescence microscopy (right images). Enlarged graphs display higher magnification. ( e-f ) Quantification of PSR using ImageJ software compared to untreated ( e ) and healthy ( f ) ear tissue showing fiber intensity on d9 and d20. Data are presented as mean ± S.D. *p < 0.05, **p < 0.01, ***p < 0.001 when compared to control groups (ctrl) with Students t -test (a, c) or ANOVA (e-f). Scale bars are 200 µm (d), 100 µm (d, higher magnifications), and 50 µm (b). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: After incubation with primary antibodies targeting β-catenin, E-cadherin, collagen I, Nrf2, iNOS, and TGFβ1 (all Cell Signaling Technology, Germany), cells or wound tissues were incubated with Alexa Fluor 488 or 594 conjugated secondary antibodies (Life Technologies, Germany) and DAPI to visualize nuclei.

    Techniques: Clinical Proteomics, Gene Expression, Staining, Immunofluorescence, Fluorescence, Microscopy, Software, Control

    Orientin suppresses ferroptosis via activation of the Nrf2/GPX4 signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Journal: Food Science & Nutrition

    Article Title: Orientin promotes diabetic wounds healing by suppressing ferroptosis via activation of the Nrf2/GPX4 pathway

    doi: 10.1002/fsn3.4360

    Figure Lengend Snippet: Orientin suppresses ferroptosis via activation of the Nrf2/GPX4 signaling pathway in vitro. (a and b) A 3D binding model is illustrated by using the ribbon model, which is applied to represent protein residues. When Orientin is docked with either Nrf2 or GPX4, the binding sites have affinities that are, respectively, −7.9 and −6.8 kcal/mol. In order to demonstrate the binding of Orientin in the Nrf2 and GPX4 pockets, a space‐filling model was utilized. (c–e) The expression of n‐Nrf2 and GPX4 in HUVECs was analyzed by Western blot. (f and g) Representative images and quantification analysis of GPX4 fluorescence of HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Article Snippet: Proteintech Group, which is situated in Chicago, Illinois, United States of America, was the source of the primary antibodies that targeted Nrf2 (16396‐1‐AP, 1:1000), CD31 (or platelet endothelial cell adhesion molecule‐1, PECAM‐1) (11265‐1‐AP, 1:1000), vascular endothelial growth factor (VEGF polyclonal antibody (VEGF‐A) (19003‐1‐AP, 1:1000), and Lamin B (12987‐1‐AP, 1:2000).

    Techniques: Activation Assay, In Vitro, Binding Assay, Expressing, Western Blot, Fluorescence, Comparison

    Inhibition of ferroptosis and improving HUVECs function by Orientin can be regulated by Nrf2–siRNA. (a and d) Evaluation of the neovascularization of HUVECs induced by Orientin using the tube formation assay in a variety of different groups. (b and e) Evaluation of the effect of Orientin on the migration of HUVECs using the transwell system in various groups. (c and f) Comparison of the levels of Orientin‐mediated HUVECs adhesion using a cell‐matrix adhesion assay in each of the different groups. (g and i) Western blot analysis of the expression of AAMP and VEGF‐A in HUVECs. (h and j) Western blot analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. (k and l) Quantitative analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Journal: Food Science & Nutrition

    Article Title: Orientin promotes diabetic wounds healing by suppressing ferroptosis via activation of the Nrf2/GPX4 pathway

    doi: 10.1002/fsn3.4360

    Figure Lengend Snippet: Inhibition of ferroptosis and improving HUVECs function by Orientin can be regulated by Nrf2–siRNA. (a and d) Evaluation of the neovascularization of HUVECs induced by Orientin using the tube formation assay in a variety of different groups. (b and e) Evaluation of the effect of Orientin on the migration of HUVECs using the transwell system in various groups. (c and f) Comparison of the levels of Orientin‐mediated HUVECs adhesion using a cell‐matrix adhesion assay in each of the different groups. (g and i) Western blot analysis of the expression of AAMP and VEGF‐A in HUVECs. (h and j) Western blot analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. (k and l) Quantitative analysis of the expression of n‐Nrf2 and GPX4 in HUVECs. A comparison between the two groups is indicated by an asterisk. *** p < .001. All data are from n = 3 independent experiments.

    Article Snippet: Proteintech Group, which is situated in Chicago, Illinois, United States of America, was the source of the primary antibodies that targeted Nrf2 (16396‐1‐AP, 1:1000), CD31 (or platelet endothelial cell adhesion molecule‐1, PECAM‐1) (11265‐1‐AP, 1:1000), vascular endothelial growth factor (VEGF polyclonal antibody (VEGF‐A) (19003‐1‐AP, 1:1000), and Lamin B (12987‐1‐AP, 1:2000).

    Techniques: Inhibition, Tube Formation Assay, Migration, Comparison, Cell Adhesion Assay, Western Blot, Expressing

    Mechanisms of action of Orientin on HUVECs that have been induced by HG. Orientin promotes diabetic wound healing by activating the Nrf2/GPX4 pathway. It also decreases HG‐induced ferroptosis by reducing the accumulation of ROS and rescuing mitochondrial dysfunction in HUVECs.

    Journal: Food Science & Nutrition

    Article Title: Orientin promotes diabetic wounds healing by suppressing ferroptosis via activation of the Nrf2/GPX4 pathway

    doi: 10.1002/fsn3.4360

    Figure Lengend Snippet: Mechanisms of action of Orientin on HUVECs that have been induced by HG. Orientin promotes diabetic wound healing by activating the Nrf2/GPX4 pathway. It also decreases HG‐induced ferroptosis by reducing the accumulation of ROS and rescuing mitochondrial dysfunction in HUVECs.

    Article Snippet: Proteintech Group, which is situated in Chicago, Illinois, United States of America, was the source of the primary antibodies that targeted Nrf2 (16396‐1‐AP, 1:1000), CD31 (or platelet endothelial cell adhesion molecule‐1, PECAM‐1) (11265‐1‐AP, 1:1000), vascular endothelial growth factor (VEGF polyclonal antibody (VEGF‐A) (19003‐1‐AP, 1:1000), and Lamin B (12987‐1‐AP, 1:2000).

    Techniques:

    Figure 3. AKBA reduces ROS levels and increases the nuclear translocation of Nrf2 in FLSs (A,B) Immunofluorescence staining and quantitative analysis of ROS in FLSs; scale bar: 20 μm. (C,D) Flow cytometry and quantitative analysis of ROS in FLSs. (E) Representative western blots showing the nuclear and cytoplasmic expressions of Nrf2 and Keap1 in FLSs after LPS treatment and treatment with or without AKBA. (F) Quantification of the western blot data for Nrf2 and Keap1. (G) Representative western blots showing the expressions of HO-1 and NQO1 in FLSs after LPS treatment and treatment with or without AKBA. (H) Immunofluorescence staining for Nrf2 in FLSs; scale bar: 20 μm. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the LPS group.

    Journal: Acta biochimica et biophysica Sinica

    Article Title: Acetyl-11-keto-β-boswellic acid restrains the progression of synovitis in osteoarthritis via the Nrf2/HO-1 pathway.

    doi: 10.3724/abbs.2024102

    Figure Lengend Snippet: Figure 3. AKBA reduces ROS levels and increases the nuclear translocation of Nrf2 in FLSs (A,B) Immunofluorescence staining and quantitative analysis of ROS in FLSs; scale bar: 20 μm. (C,D) Flow cytometry and quantitative analysis of ROS in FLSs. (E) Representative western blots showing the nuclear and cytoplasmic expressions of Nrf2 and Keap1 in FLSs after LPS treatment and treatment with or without AKBA. (F) Quantification of the western blot data for Nrf2 and Keap1. (G) Representative western blots showing the expressions of HO-1 and NQO1 in FLSs after LPS treatment and treatment with or without AKBA. (H) Immunofluorescence staining for Nrf2 in FLSs; scale bar: 20 μm. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the LPS group.

    Article Snippet: The sections were incubated overnight at 4°C with specific primary antibodies targeting Nrf2 (16396-1-AP, 1:200; Proteintech), HO-1 (10701-1-AP, 1:200; Proteintech), iNOS (18985-1-AP, 1:200; Proteintech), Col II (28459-1-AP, 1:200; Proteintech), and MMP-13 (18165-1-AP, 1:200; Proteintech).

    Techniques: Translocation Assay, Immunofluorescence, Staining, Flow Cytometry, Western Blot

    Figure 4. ML385 suppresses the antioxidant effects of AKBA and inhibits AKBA-mediated anti-inflammation and anti-MMP effects in FLSs (A,B) Immunofluorescence staining and quantitative analysis of ROS in FLSs; scale bar: 20 μm. (C,D) Flow cytometry and quantitative analysis of ROS in FLSs. (E) Representative western blots showing the nuclear and cytoplasmic expressions of Nrf2 in FLSs after LPS treatment or treatment with or without AKBA/ML385. (F) Representative western blots showing the expressions of HO-1 and NQO1 in FLSs after LPS treatment and treatment with or without AKBA/ML385. (G) Immunofluorescence staining for Nrf2 in FLSs; scale bar: 20 μm. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the LPS+AKBA group.

    Journal: Acta biochimica et biophysica Sinica

    Article Title: Acetyl-11-keto-β-boswellic acid restrains the progression of synovitis in osteoarthritis via the Nrf2/HO-1 pathway.

    doi: 10.3724/abbs.2024102

    Figure Lengend Snippet: Figure 4. ML385 suppresses the antioxidant effects of AKBA and inhibits AKBA-mediated anti-inflammation and anti-MMP effects in FLSs (A,B) Immunofluorescence staining and quantitative analysis of ROS in FLSs; scale bar: 20 μm. (C,D) Flow cytometry and quantitative analysis of ROS in FLSs. (E) Representative western blots showing the nuclear and cytoplasmic expressions of Nrf2 in FLSs after LPS treatment or treatment with or without AKBA/ML385. (F) Representative western blots showing the expressions of HO-1 and NQO1 in FLSs after LPS treatment and treatment with or without AKBA/ML385. (G) Immunofluorescence staining for Nrf2 in FLSs; scale bar: 20 μm. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the LPS+AKBA group.

    Article Snippet: The sections were incubated overnight at 4°C with specific primary antibodies targeting Nrf2 (16396-1-AP, 1:200; Proteintech), HO-1 (10701-1-AP, 1:200; Proteintech), iNOS (18985-1-AP, 1:200; Proteintech), Col II (28459-1-AP, 1:200; Proteintech), and MMP-13 (18165-1-AP, 1:200; Proteintech).

    Techniques: Immunofluorescence, Staining, Flow Cytometry, Western Blot

    Figure 6. AKBA ameliorates pain, synovial inflammation and fibrosis in vivo (A) The experimental design for the animal study; Figure Draw ID: WOSPA7585e. (B) Changes in the body weight of the rats every 2 weeks after surgery. (C) Changes in pain sensitivity measured by the Von Frey test every 2 weeks after surgery. (D) Knee joint diameter of the right hind limbs of the rats before surgery and 6 weeks after surgery. (E) H&E and Sirius red staining of the synovium in different groups 6 weeks after surgery; scale bar: 100 μm. (F) Krenn synovitis scores of the synovium in different groups. (G) Immunohistochemical staining for iNOS, MMP-13, Nrf2, and HO-1 in the right hind joint synovium of rats; scale bar: 100 μm. (H) Percentages of iNOS-, MMP-13-, Nrf2-, and HO-1-positive cells. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the OA group.

    Journal: Acta biochimica et biophysica Sinica

    Article Title: Acetyl-11-keto-β-boswellic acid restrains the progression of synovitis in osteoarthritis via the Nrf2/HO-1 pathway.

    doi: 10.3724/abbs.2024102

    Figure Lengend Snippet: Figure 6. AKBA ameliorates pain, synovial inflammation and fibrosis in vivo (A) The experimental design for the animal study; Figure Draw ID: WOSPA7585e. (B) Changes in the body weight of the rats every 2 weeks after surgery. (C) Changes in pain sensitivity measured by the Von Frey test every 2 weeks after surgery. (D) Knee joint diameter of the right hind limbs of the rats before surgery and 6 weeks after surgery. (E) H&E and Sirius red staining of the synovium in different groups 6 weeks after surgery; scale bar: 100 μm. (F) Krenn synovitis scores of the synovium in different groups. (G) Immunohistochemical staining for iNOS, MMP-13, Nrf2, and HO-1 in the right hind joint synovium of rats; scale bar: 100 μm. (H) Percentages of iNOS-, MMP-13-, Nrf2-, and HO-1-positive cells. Data are expressed as the mean±SD, n=3. *P<0.05 vs. the OA group.

    Article Snippet: The sections were incubated overnight at 4°C with specific primary antibodies targeting Nrf2 (16396-1-AP, 1:200; Proteintech), HO-1 (10701-1-AP, 1:200; Proteintech), iNOS (18985-1-AP, 1:200; Proteintech), Col II (28459-1-AP, 1:200; Proteintech), and MMP-13 (18165-1-AP, 1:200; Proteintech).

    Techniques: In Vivo, Staining, Immunohistochemical staining

    Figure 8. Schematic illustration of the Nrf2/HO-1 signaling activator AKBA-mediated antioxidative protection against OA

    Journal: Acta biochimica et biophysica Sinica

    Article Title: Acetyl-11-keto-β-boswellic acid restrains the progression of synovitis in osteoarthritis via the Nrf2/HO-1 pathway.

    doi: 10.3724/abbs.2024102

    Figure Lengend Snippet: Figure 8. Schematic illustration of the Nrf2/HO-1 signaling activator AKBA-mediated antioxidative protection against OA

    Article Snippet: The sections were incubated overnight at 4°C with specific primary antibodies targeting Nrf2 (16396-1-AP, 1:200; Proteintech), HO-1 (10701-1-AP, 1:200; Proteintech), iNOS (18985-1-AP, 1:200; Proteintech), Col II (28459-1-AP, 1:200; Proteintech), and MMP-13 (18165-1-AP, 1:200; Proteintech).

    Techniques: