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atf3 protein (TargetMol)

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TargetMol atf3 protein
Atf3 Protein, supplied by TargetMol, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/atf3+protein/ATF-3+Protein%2C+Human%2C+Recombinant/pm41398593-97-38-34
Average 93 stars, based on 1 article reviews

atf3 protein - by Bioz Stars, 2026-09

93/100 stars

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SPR Assay:

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma.
Article Snippet: .. 288 289 Surface plasmon resonance (SPR) analysis 290 SPR assays were performed by TopScience Co., Ltd. (Shanghai, 291 China) to detect the binding between the recombinant ATF3 protein 292 (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), 293 with the ATF3 protein and anti-ATF3 antibody combination used as AR TIC LE IN PR ES S 294 the positive control. .. The ATF3 protein was immobilized on a CM5 295 sensor chip (BR-1005-30; Cytiva, Marlborough, MA, USA).

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma
Article Snippet: .. SPR assays were performed by TopScience Co., Ltd. (Shanghai, China) to detect the binding between the recombinant ATF3 protein (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), with the ATF3 protein and anti-ATF3 antibody combination used as the positive control. .. The ATF3 protein was immobilized on a CM5 sensor chip (BR-1005-30; Cytiva, Marlborough, MA, USA).

Binding Assay:

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma
Article Snippet: .. SPR assays were performed by TopScience Co., Ltd. (Shanghai, China) to detect the binding between the recombinant ATF3 protein (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), with the ATF3 protein and anti-ATF3 antibody combination used as the positive control. .. The ATF3 protein was immobilized on a CM5 sensor chip (BR-1005-30; Cytiva, Marlborough, MA, USA).

Recombinant:

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma
Article Snippet: .. SPR assays were performed by TopScience Co., Ltd. (Shanghai, China) to detect the binding between the recombinant ATF3 protein (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), with the ATF3 protein and anti-ATF3 antibody combination used as the positive control. .. The ATF3 protein was immobilized on a CM5 sensor chip (BR-1005-30; Cytiva, Marlborough, MA, USA).

Positive Control:

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma
Article Snippet: .. SPR assays were performed by TopScience Co., Ltd. (Shanghai, China) to detect the binding between the recombinant ATF3 protein (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), with the ATF3 protein and anti-ATF3 antibody combination used as the positive control. .. The ATF3 protein was immobilized on a CM5 sensor chip (BR-1005-30; Cytiva, Marlborough, MA, USA).

Image Search Results

PAF induces ferroptosis via the ATF3/GPX4 and ATF3/SLC7A11 axes. (A) Heat map representing the significantly regulated transcription factors detected via RNA-seq analysis of AN3CA and HEC1B cells. (B , C) The mRNA expression levels of ATF3 and DDIT3 were in AN3CA and HEC1B cells treated with PAF (60 µM) for 48 h. (D , E) Protein expression of ATF3 in AN3CA and HEC1B cells treated with PAF (0, 20, 40, and 60 µM) for 48 h (D), and the quantifiable data are shown (E). (F) Confocal microscopy of AN3CA and HEC1B cells in the presence of PAF (60 µM). Cells were stained for ATF3 (green) and phalloidin (red). DAPI was used to visualize the nucleus (blue). Scale bar, 50 μm (left) or 100 μm (right). (G) The potential binding sites between ATF3 and GPX4/SLC7A11 were predicted by JASPAR. (H) Schematic diagram of ATF3 binding site-mutated SLC7A11 reporter vector (pro-SLC7A11-mut) and GPX4 reporter vector (pro-GPX4-mut). (I , J) Dual luciferase assay of the luciferase activity of AN3CA (I) and HEC1B (J) cells. (K) Immunoblotting analysis of the expression of GPX4 and SLC7A11 following ATF3 overexpression in AN3CA and HEC1B cells. (L) Immunoblotting analysis of the protein expression of SLC7A11, GPX4, and ATF3 after ATF3 silencing with siRNA coupled with PAF treatment in AN3CA cells. * p < 0.05, ** p < 0.01 and *** p < 0.001, ns . not significant

Journal: Biology Direct

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma

doi: 10.1186/s13062-025-00713-z

Figure Lengend Snippet: PAF induces ferroptosis via the ATF3/GPX4 and ATF3/SLC7A11 axes. (A) Heat map representing the significantly regulated transcription factors detected via RNA-seq analysis of AN3CA and HEC1B cells. (B , C) The mRNA expression levels of ATF3 and DDIT3 were in AN3CA and HEC1B cells treated with PAF (60 µM) for 48 h. (D , E) Protein expression of ATF3 in AN3CA and HEC1B cells treated with PAF (0, 20, 40, and 60 µM) for 48 h (D), and the quantifiable data are shown (E). (F) Confocal microscopy of AN3CA and HEC1B cells in the presence of PAF (60 µM). Cells were stained for ATF3 (green) and phalloidin (red). DAPI was used to visualize the nucleus (blue). Scale bar, 50 μm (left) or 100 μm (right). (G) The potential binding sites between ATF3 and GPX4/SLC7A11 were predicted by JASPAR. (H) Schematic diagram of ATF3 binding site-mutated SLC7A11 reporter vector (pro-SLC7A11-mut) and GPX4 reporter vector (pro-GPX4-mut). (I , J) Dual luciferase assay of the luciferase activity of AN3CA (I) and HEC1B (J) cells. (K) Immunoblotting analysis of the expression of GPX4 and SLC7A11 following ATF3 overexpression in AN3CA and HEC1B cells. (L) Immunoblotting analysis of the protein expression of SLC7A11, GPX4, and ATF3 after ATF3 silencing with siRNA coupled with PAF treatment in AN3CA cells. * p < 0.05, ** p < 0.01 and *** p < 0.001, ns . not significant

Article Snippet: SPR assays were performed by TopScience Co., Ltd. (Shanghai, China) to detect the binding between the recombinant ATF3 protein (TMPH-01164, TargetMol) and C16-PAF (74389-68-7, TargetMol), with the ATF3 protein and anti-ATF3 antibody combination used as the positive control.

Techniques: RNA Sequencing, Expressing, Confocal Microscopy, Staining, Binding Assay, Plasmid Preparation, Luciferase, Activity Assay, Western Blot, Over Expression

PAF binds to ATF3 and reduces its ubiquitination. (A , B) Molecular docking indicates the binding details between PAF and ATF3. The surface representation of the protein residues ( A ) and 2D representation of the binding interaction of PAF and ATF3 ( B ) are depicted. (C , D) Surface plasmon resonance of the affinity of anti-ATF3 antibody ( C ) and PAF ( D ) for ATF3 protein. K D , dissociation constant. (E) WB analysis shows that PAF stabilized ATF3 across different temperature gradients in the CETSA in 293T cells. (F) WB analysis indicates that PAF promoted the resistance of ATF3 to pronase digestion in the DARTS assay in 293T cells. (G) CHX chase analysis of ATF3 protein expression after treatment with PAF in AN3CA and HEC1B cells. (H) WB analysis of ATF3 in ATF3 -overexpressing AN3CA and HEC1B cells. The cells were pretreated with PAF (60 µM) for 24 h and then treated with CHX and MG132 for 24 h. (I) Representative WB images demonstrate the ubiquitination of ATF3 in 293T cells co-transfected with ATF3-Flag, HA-Ub, and plasmids for 24 h. Cellular lysates were collected after 3 h of treatment with PAF, purified with a Flag-tag protein purification kit, and then subjected to WB with anti-HA and anti-ATF3

Journal: Biology Direct

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma

doi: 10.1186/s13062-025-00713-z

Figure Lengend Snippet: PAF binds to ATF3 and reduces its ubiquitination. (A , B) Molecular docking indicates the binding details between PAF and ATF3. The surface representation of the protein residues ( A ) and 2D representation of the binding interaction of PAF and ATF3 ( B ) are depicted. (C , D) Surface plasmon resonance of the affinity of anti-ATF3 antibody ( C ) and PAF ( D ) for ATF3 protein. K D , dissociation constant. (E) WB analysis shows that PAF stabilized ATF3 across different temperature gradients in the CETSA in 293T cells. (F) WB analysis indicates that PAF promoted the resistance of ATF3 to pronase digestion in the DARTS assay in 293T cells. (G) CHX chase analysis of ATF3 protein expression after treatment with PAF in AN3CA and HEC1B cells. (H) WB analysis of ATF3 in ATF3 -overexpressing AN3CA and HEC1B cells. The cells were pretreated with PAF (60 µM) for 24 h and then treated with CHX and MG132 for 24 h. (I) Representative WB images demonstrate the ubiquitination of ATF3 in 293T cells co-transfected with ATF3-Flag, HA-Ub, and plasmids for 24 h. Cellular lysates were collected after 3 h of treatment with PAF, purified with a Flag-tag protein purification kit, and then subjected to WB with anti-HA and anti-ATF3

Techniques: Ubiquitin Proteomics, Binding Assay, SPR Assay, Expressing, Transfection, Purification, FLAG-tag, Protein Purification

Schematic overview of the present study. Treatment with PAF attenuates EC cell proliferation by inducing ferroptosis. Mechanistically, PAF interacts with ATF3, enhancing its stability through deubiquitination and consequently suppressing the expression of the ferroptosis-related proteins SLC7A11 and GPX4

Journal: Biology Direct

Article Title: Platelet-activating factor induces ferroptosis by binding to ATF3 and inhibiting the SLC7A11/GPX4 axis to suppress the progression of endometrial carcinoma

doi: 10.1186/s13062-025-00713-z

Figure Lengend Snippet: Schematic overview of the present study. Treatment with PAF attenuates EC cell proliferation by inducing ferroptosis. Mechanistically, PAF interacts with ATF3, enhancing its stability through deubiquitination and consequently suppressing the expression of the ferroptosis-related proteins SLC7A11 and GPX4

Techniques: Expressing

Fig. 1 Analysis of fluorescence intensity in HeLa and Ca Ski cells transfected with pCMV6-ATF3, a mock vector, or left untreated as controls, utilizing fluorescence microscopy and flow cytometry at 48 and 72 h post-transfection. (A) Fluorescent imaging of HeLa and Ca Ski cells was performed at 20x magnification, comparing cells transfected with pCMV6-ATF3 to mock and control groups. (B) Mean fluorescence intensity levels were measured across pCMV6-ATF3, mock, and control samples. Flow cytometry results showed transfection efficiencies of 89.41% in HeLa and 88.13% in Ca Ski cells at 72 h post-transfection, significantly higher than the mock and control groups (p < 0.0001). (C) Western blot analysis was conducted to assess ATF3 protein ex pression in HeLa and Ca Ski cell lysates, using anti-ATF3 and anti-β-actin antibodies. (D) Densitometry of ATF3 expression levels showed a marked increase in cells transfected with pCMV6-ATF3 compared to control and mock groups (p < 0.001). Results are presented as the mean ± SD from three independent experiments

Journal: Virology journal

Article Title: Activating transcription factor 3 induces oxidative stress and genotoxicity, transcriptionally modulating metastasis-related gene expression in human papillomavirus-infected cervical cancer.

doi: 10.1186/s12985-025-02675-0

Figure Lengend Snippet: Fig. 1 Analysis of fluorescence intensity in HeLa and Ca Ski cells transfected with pCMV6-ATF3, a mock vector, or left untreated as controls, utilizing fluorescence microscopy and flow cytometry at 48 and 72 h post-transfection. (A) Fluorescent imaging of HeLa and Ca Ski cells was performed at 20x magnification, comparing cells transfected with pCMV6-ATF3 to mock and control groups. (B) Mean fluorescence intensity levels were measured across pCMV6-ATF3, mock, and control samples. Flow cytometry results showed transfection efficiencies of 89.41% in HeLa and 88.13% in Ca Ski cells at 72 h post-transfection, significantly higher than the mock and control groups (p < 0.0001). (C) Western blot analysis was conducted to assess ATF3 protein ex pression in HeLa and Ca Ski cell lysates, using anti-ATF3 and anti-β-actin antibodies. (D) Densitometry of ATF3 expression levels showed a marked increase in cells transfected with pCMV6-ATF3 compared to control and mock groups (p < 0.001). Results are presented as the mean ± SD from three independent experiments

Article Snippet: ATF3 protein levels were detected using a monoclonal anti-ATF3 antibody (1:500, Santa Cruz Biotechnologies). β-actin (1:5000, Santa Cruz Biotechnologies) was used as a loading control.

Techniques: Fluorescence, Transfection, Plasmid Preparation, Microscopy, Flow Cytometry, Imaging, Control, Western Blot, Expressing

Fig. 2 Effect of ATF3 overexpression on the expression of HPV-16 and HPV-18 E6/E7, MMP1, and SHARP1 genes in HeLa (A) and Ca Ski (B) cells, analyzed by RT-qPCR. (A) In HeLa cells, overexpression of ATF3 resulted in a significant decrease in MMP1 gene expression (p < 0.01), while SHARP1 and HPV-18 E6/ E7 mRNA levels remained largely unaffected (p > 0.05) compared to mock and control groups. (B) Similarly, in Ca Ski cells, ATF3 overexpression significantly reduced MMP1 expression (p < 0.02), but SHARP1 and HPV-18 E6/E7 expression levels showed no significant difference (p > 0.05) relative to mock and control groups. Both HeLa and Ca Ski cells transfected with pCMV6-ATF3 demonstrated markedly higher ATF3 mRNA expression compared to mock and control groups (p < 0.001). Data are presented as the mean ± SD from three independent experiments

Journal: Virology journal

doi: 10.1186/s12985-025-02675-0

Figure Lengend Snippet: Fig. 2 Effect of ATF3 overexpression on the expression of HPV-16 and HPV-18 E6/E7, MMP1, and SHARP1 genes in HeLa (A) and Ca Ski (B) cells, analyzed by RT-qPCR. (A) In HeLa cells, overexpression of ATF3 resulted in a significant decrease in MMP1 gene expression (p < 0.01), while SHARP1 and HPV-18 E6/ E7 mRNA levels remained largely unaffected (p > 0.05) compared to mock and control groups. (B) Similarly, in Ca Ski cells, ATF3 overexpression significantly reduced MMP1 expression (p < 0.02), but SHARP1 and HPV-18 E6/E7 expression levels showed no significant difference (p > 0.05) relative to mock and control groups. Both HeLa and Ca Ski cells transfected with pCMV6-ATF3 demonstrated markedly higher ATF3 mRNA expression compared to mock and control groups (p < 0.001). Data are presented as the mean ± SD from three independent experiments

Techniques: Over Expression, Expressing, Quantitative RT-PCR, Gene Expression, Control, Transfection

Fig. 3 Evaluation of ROS levels in HeLa and Ca Ski cells following pCMV6-ATF3 transfection. (A) Flow cytometry histograms illustrating ROS levels in HeLa and Ca Ski cells, measured with the DCHF-DA assay. (B) Quantitative comparison shows a significant rise in ROS levels in pCMV6-ATF3-transfected cells relative to mock and control groups (p < 0.01). Results are shown as the mean ± SD from three separate experiments

Journal: Virology journal

doi: 10.1186/s12985-025-02675-0

Figure Lengend Snippet: Fig. 3 Evaluation of ROS levels in HeLa and Ca Ski cells following pCMV6-ATF3 transfection. (A) Flow cytometry histograms illustrating ROS levels in HeLa and Ca Ski cells, measured with the DCHF-DA assay. (B) Quantitative comparison shows a significant rise in ROS levels in pCMV6-ATF3-transfected cells relative to mock and control groups (p < 0.01). Results are shown as the mean ± SD from three separate experiments

Techniques: Transfection, Flow Cytometry, Comparison, Control

Fig. 4 DNA damage analysis by comet assay using alkaline single-cell gel electrophoresis. (A) Representative images from the comet assay display DNA migration patterns in HeLa and Ca Ski cells post-transfection with pCMV6-ATF3. In these images, intact DNA forms a distinct head, while fragmented DNA trails behind, forming a comet tail—longer tails signify greater DNA damage. (B) Quantification of comet assay results for HeLa and Ca Ski cells across pCMV6-ATF3-transfected, mock-transfected, and control groups. Minimal DNA damage was observed in both control and mock-transfected cells. Data are expressed as the mean ± SD from three independent replicates

Journal: Virology journal

doi: 10.1186/s12985-025-02675-0

Figure Lengend Snippet: Fig. 4 DNA damage analysis by comet assay using alkaline single-cell gel electrophoresis. (A) Representative images from the comet assay display DNA migration patterns in HeLa and Ca Ski cells post-transfection with pCMV6-ATF3. In these images, intact DNA forms a distinct head, while fragmented DNA trails behind, forming a comet tail—longer tails signify greater DNA damage. (B) Quantification of comet assay results for HeLa and Ca Ski cells across pCMV6-ATF3-transfected, mock-transfected, and control groups. Minimal DNA damage was observed in both control and mock-transfected cells. Data are expressed as the mean ± SD from three independent replicates

Techniques: Single Cell Gel Electrophoresis, Alkaline Single Cell Gel Electrophoresis, Migration, Transfection, Control

Knockdown of ATF3 alleviates symptoms and pathological knee joint damage in rats with OA. ( A ) Width of the knee joints of rats. ( B ) Knee pain was assessed by weight-bearing test; ( C – E ) Serum levels of TNF-α ( C ), IL-8 ( D ) and IL-6 ( E ) were measured by ELISA (n = 4); ( F ) Histopathological changes of the knee joint from rats (n = 2) were observed by safranin O staining. Scale bar = 100 μm. Error bars are mean ± s.d. * P < 0.05 and ** P < 0.01 vs OA+si-NC group.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: Knockdown of ATF3 alleviates symptoms and pathological knee joint damage in rats with OA. ( A ) Width of the knee joints of rats. ( B ) Knee pain was assessed by weight-bearing test; ( C – E ) Serum levels of TNF-α ( C ), IL-8 ( D ) and IL-6 ( E ) were measured by ELISA (n = 4); ( F ) Histopathological changes of the knee joint from rats (n = 2) were observed by safranin O staining. Scale bar = 100 μm. Error bars are mean ± s.d. * P < 0.05 and ** P < 0.01 vs OA+si-NC group.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Knockdown, Enzyme-linked Immunosorbent Assay, Staining

Effects of ATF3 knockdown on extracellular matrix proteins in the articular cartilage of rats with OA. ( A – D ), Expression of collagen II ( A ), aggrecan ( B ) and MMP-13 ( C ) in rat knee joints from rats (n=4) detected by immunohistochemistry and quantified by ImageJ software ( D ). Scale bar = 400 μm. Error bars are mean ± s.d. ** P < 0.01 vs OA+si-NC group.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: Effects of ATF3 knockdown on extracellular matrix proteins in the articular cartilage of rats with OA. ( A – D ), Expression of collagen II ( A ), aggrecan ( B ) and MMP-13 ( C ) in rat knee joints from rats (n=4) detected by immunohistochemistry and quantified by ImageJ software ( D ). Scale bar = 400 μm. Error bars are mean ± s.d. ** P < 0.01 vs OA+si-NC group.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Knockdown, Expressing, Immunohistochemistry, Software

ATF3 regulates the Akt signaling pathway in OA rats. ( A and B ) Western blot was used to detect the protein levels of p-Akt, Akt and ATF3 in the articular cartilage in the Sham and OA groups, Error bars are mean ± s.d. * P < 0.05; ** P < 0.01 vs Sham group; ( C and D ) Western blot was utilized to measure the protein levels of p-Akt, Akt and ATF3 in the articular cartilage in the OA + si-NC and OA + si-ATF3 groups, Error bars are mean ± s.d. ** P < 0.01 vs OA + si-NC group, n = 4.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: ATF3 regulates the Akt signaling pathway in OA rats. ( A and B ) Western blot was used to detect the protein levels of p-Akt, Akt and ATF3 in the articular cartilage in the Sham and OA groups, Error bars are mean ± s.d. * P < 0.05; ** P < 0.01 vs Sham group; ( C and D ) Western blot was utilized to measure the protein levels of p-Akt, Akt and ATF3 in the articular cartilage in the OA + si-NC and OA + si-ATF3 groups, Error bars are mean ± s.d. ** P < 0.01 vs OA + si-NC group, n = 4.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Western Blot

Effects of periodic mechanical stress on inflammation, extracellular matrix proteins and ATF3-Akt axis in osteoarthritic chondrocytes. IL-1β-induced chondrocytes were treated without (group 0) or with PMS under a device height of 1 cm (group 1), 2 cm (group 2), 4 cm (group 4), and 8 cm (group 8). ( A – C ) Levels of TNF-α ( A ), IL-6 ( B ) and IL-8 ( C ) in the supernatant of OA cells measured by ELISA; ( D and E ) Protein expression levels of extracellular matrix proteins (collagen II, aggrecan, and MMP-13) in OA cells detected by Western blot; ( F and G ) Protein expression levels of p-Akt, Akt, and ATF3 in OA cells detected by Western blot. Error bars are mean ± s.d.* P < 0.05; ** P < 0.01 vs Group 0.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: Effects of periodic mechanical stress on inflammation, extracellular matrix proteins and ATF3-Akt axis in osteoarthritic chondrocytes. IL-1β-induced chondrocytes were treated without (group 0) or with PMS under a device height of 1 cm (group 1), 2 cm (group 2), 4 cm (group 4), and 8 cm (group 8). ( A – C ) Levels of TNF-α ( A ), IL-6 ( B ) and IL-8 ( C ) in the supernatant of OA cells measured by ELISA; ( D and E ) Protein expression levels of extracellular matrix proteins (collagen II, aggrecan, and MMP-13) in OA cells detected by Western blot; ( F and G ) Protein expression levels of p-Akt, Akt, and ATF3 in OA cells detected by Western blot. Error bars are mean ± s.d.* P < 0.05; ** P < 0.01 vs Group 0.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Enzyme-linked Immunosorbent Assay, Expressing, Western Blot

Up-regulation of ATF3 reverses the effects of periodic mechanical stress on apoptosis, inflammation and extracellular matrix proteins expression in osteoarthritic chondrocytes. ( A and B ) Apoptotic rate of OA cells was detected by flow cytometry; ( B – D ) Levels of TNF-α ( B ), IL-6 ( C ) and IL-8 ( D ) in OA cells were detected by ELISA; ( E and F ) Protein expression levels of collagen II, aggrecan and MMP-13 in OA cells were detected by Western blot. Error bars are mean ± s.d. * P < 0.05 and ** P < 0.01 vs IL-1β + NC group.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: Up-regulation of ATF3 reverses the effects of periodic mechanical stress on apoptosis, inflammation and extracellular matrix proteins expression in osteoarthritic chondrocytes. ( A and B ) Apoptotic rate of OA cells was detected by flow cytometry; ( B – D ) Levels of TNF-α ( B ), IL-6 ( C ) and IL-8 ( D ) in OA cells were detected by ELISA; ( E and F ) Protein expression levels of collagen II, aggrecan and MMP-13 in OA cells were detected by Western blot. Error bars are mean ± s.d. * P < 0.05 and ** P < 0.01 vs IL-1β + NC group.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Expressing, Flow Cytometry, Enzyme-linked Immunosorbent Assay, Western Blot

Up-regulation of ATF3 reverses the regulation of the ATF3-Akt axis by periodic mechanical stress in osteoarthritic chondrocytes. ( A and B ) Protein expression levels of p-Akt, ATF3 and Akt in osteoarthritic chondrocytes were detected by Western blot. Error bars are mean ± s.d. ** P < 0.01 vs IL-1β + NC group.

Journal: Journal of Inflammation Research

Article Title: Periodic Mechanical Stress Inhibits the Development of Osteoarthritis via Regulating ATF3-Akt Axis

doi: 10.2147/JIR.S419186

Figure Lengend Snippet: Up-regulation of ATF3 reverses the regulation of the ATF3-Akt axis by periodic mechanical stress in osteoarthritic chondrocytes. ( A and B ) Protein expression levels of p-Akt, ATF3 and Akt in osteoarthritic chondrocytes were detected by Western blot. Error bars are mean ± s.d. ** P < 0.01 vs IL-1β + NC group.

Article Snippet: ATF3 antibody, NBP1-85816PEP, 1:1000, Novus Biologicals, Littleton, CO, USA.

Techniques: Expressing, Western Blot

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