bio rad ahp1797 parp Search Results


abs against ripk3 for mouse  (Bio-Rad)
93
Bio-Rad abs against ripk3 for mouse
(A) Representative immunoblot images of <t>RIPK3</t> phosphorylation (Thr231/Ser232), RIPK3, MLKL phosphorylation (Ser345), MLKL, RIPK1 phosphorylation (Ser166) protein and (B) quantification of RIPK3 phosphorylation, RIPK3, MLKL phosphorylation, RIPK1 phosphorylation protein levels in lung tissues from mice treated with oligomycin either control or LPS (n=3 per each group). β-actin or MLKL were used as loading control. Data are representative of three independent experiments. Data are mean±SD. * p<0.05; ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or ANOVA.
Abs Against Ripk3 For Mouse, supplied by Bio-Rad, 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/bio+rad+ahp1797+parp/pmc09066008-52-72-78?v=Bio-Rad
Average 93 stars, based on 1 article reviews
abs against ripk3 for mouse - by Bioz Stars, 2026-08
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Image Search Results


(A) Representative immunoblot images of RIPK3 phosphorylation (Thr231/Ser232), RIPK3, MLKL phosphorylation (Ser345), MLKL, RIPK1 phosphorylation (Ser166) protein and (B) quantification of RIPK3 phosphorylation, RIPK3, MLKL phosphorylation, RIPK1 phosphorylation protein levels in lung tissues from mice treated with oligomycin either control or LPS (n=3 per each group). β-actin or MLKL were used as loading control. Data are representative of three independent experiments. Data are mean±SD. * p<0.05; ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or ANOVA.

Journal: Immune Network

Article Title: Impairment of Mitochondrial ATP Synthesis Induces RIPK3-dependent Necroptosis in Lung Epithelial Cells During Lung Injury by Lung Inflammation

doi: 10.4110/in.2022.22.e18

Figure Lengend Snippet: (A) Representative immunoblot images of RIPK3 phosphorylation (Thr231/Ser232), RIPK3, MLKL phosphorylation (Ser345), MLKL, RIPK1 phosphorylation (Ser166) protein and (B) quantification of RIPK3 phosphorylation, RIPK3, MLKL phosphorylation, RIPK1 phosphorylation protein levels in lung tissues from mice treated with oligomycin either control or LPS (n=3 per each group). β-actin or MLKL were used as loading control. Data are representative of three independent experiments. Data are mean±SD. * p<0.05; ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or ANOVA.

Article Snippet: After electrophoresis, proteins were transferred to polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA) or Protran nitrocellulose membranes (10600001; GE Healthcare Life Science, Pittsburgh, PA, USA) and blocked in 5% non-fat milk or 5% (w/v) BSA (9048-46-8; Santa Cruz Biotechnology, Dallas, TX, USA) in Tris-buffered saline containing 0.05% Tween-20 (TBS-T) (TBS [170-6435; Bio-Rad Laboratories, Hercules, CA, USA] and Tween-20 [170-6531'; Bio-Rad Laboratories]) at 25°C for 1 h. The membranes were immunoblotted with primary Abs against RIPK3 for mouse (AHP1797; Bio-Rad Laboratories), RIPK3 for human (ab62344; Abcam, Cambridge, UK), Phospho-RIPK3 (Thr231/Ser232) for mouse (ab222320; Abcam), Phospho-RIPK3 (Ser227) for human (ab209384; Abcam), Phospho-MLKL (Ser345) (ab196436; Abcam) for mouse, Phospho-MLKL (Ser358) (ab187091; Abcam) for human, MLKL (ab243142; Abcam) for mouse, MLKL (ab184718; Abcam) for human, Phospho-RIPK1 (Ser166) (#31122; Cell Signaling Technology, Danvers, MA, USA) for mouse, Phospho-RIPK1 (Ser166) (NBP3-06877; Novus, Littleton, CO, USA) for human, and β-actin (A5316; Sigma-Aldrich) overnight at 4°C and washed five times with TBS-T for 10 min each at room temperature.

Techniques: Western Blot, Phospho-proteomics, Control

(A) Representative immunofluorescence images for MLKL phosphorylation at Ser345 (P-MLKL) staining (green) in lung epithelial cells expressing E-cadherin (red) of mice treated with oligomycin either control or LPS. Scale bars, 20 µm. DAPI-stained nuclei are shown in blue. White arrows indicate P-MLKL positive cells (n=10 images per individual subject, n=5 per each group). (B) Quantification of intensity for P-MLKL-positive staining and (C) quantification of P-MLKL and E-cadherin-positive cells from immunofluorescence images in A. (D) Representative immunoblot images of RIPK3 phosphorylation (Thr231/Ser232), RIPK3, MLKL phosphorylation (Ser345), MLKL, RIPK1 phosphorylation (Ser166) protein from lung tissue sections of A. MLKL was used as loading control. (E) Quantification of protein levels in BALF of lungs from mice treated with oligomycin either control or LPS (n=5 per each group). (F) Quantification of total inflammatory cells in BALF of lungs from mice treated with oligomycin either control or LPS (n=5 per each group). Data are representative of three independent experiments. Data are mean±SD. * p<0.05; ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or ANOVA.

Journal: Immune Network

Article Title: Impairment of Mitochondrial ATP Synthesis Induces RIPK3-dependent Necroptosis in Lung Epithelial Cells During Lung Injury by Lung Inflammation

doi: 10.4110/in.2022.22.e18

Figure Lengend Snippet: (A) Representative immunofluorescence images for MLKL phosphorylation at Ser345 (P-MLKL) staining (green) in lung epithelial cells expressing E-cadherin (red) of mice treated with oligomycin either control or LPS. Scale bars, 20 µm. DAPI-stained nuclei are shown in blue. White arrows indicate P-MLKL positive cells (n=10 images per individual subject, n=5 per each group). (B) Quantification of intensity for P-MLKL-positive staining and (C) quantification of P-MLKL and E-cadherin-positive cells from immunofluorescence images in A. (D) Representative immunoblot images of RIPK3 phosphorylation (Thr231/Ser232), RIPK3, MLKL phosphorylation (Ser345), MLKL, RIPK1 phosphorylation (Ser166) protein from lung tissue sections of A. MLKL was used as loading control. (E) Quantification of protein levels in BALF of lungs from mice treated with oligomycin either control or LPS (n=5 per each group). (F) Quantification of total inflammatory cells in BALF of lungs from mice treated with oligomycin either control or LPS (n=5 per each group). Data are representative of three independent experiments. Data are mean±SD. * p<0.05; ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or ANOVA.

Article Snippet: After electrophoresis, proteins were transferred to polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA) or Protran nitrocellulose membranes (10600001; GE Healthcare Life Science, Pittsburgh, PA, USA) and blocked in 5% non-fat milk or 5% (w/v) BSA (9048-46-8; Santa Cruz Biotechnology, Dallas, TX, USA) in Tris-buffered saline containing 0.05% Tween-20 (TBS-T) (TBS [170-6435; Bio-Rad Laboratories, Hercules, CA, USA] and Tween-20 [170-6531'; Bio-Rad Laboratories]) at 25°C for 1 h. The membranes were immunoblotted with primary Abs against RIPK3 for mouse (AHP1797; Bio-Rad Laboratories), RIPK3 for human (ab62344; Abcam, Cambridge, UK), Phospho-RIPK3 (Thr231/Ser232) for mouse (ab222320; Abcam), Phospho-RIPK3 (Ser227) for human (ab209384; Abcam), Phospho-MLKL (Ser345) (ab196436; Abcam) for mouse, Phospho-MLKL (Ser358) (ab187091; Abcam) for human, MLKL (ab243142; Abcam) for mouse, MLKL (ab184718; Abcam) for human, Phospho-RIPK1 (Ser166) (#31122; Cell Signaling Technology, Danvers, MA, USA) for mouse, Phospho-RIPK1 (Ser166) (NBP3-06877; Novus, Littleton, CO, USA) for human, and β-actin (A5316; Sigma-Aldrich) overnight at 4°C and washed five times with TBS-T for 10 min each at room temperature.

Techniques: Immunofluorescence, Phospho-proteomics, Staining, Expressing, Control, Western Blot

(A) Representative immunohistochemistry images for RIPK3 staining in lung tissues from patients with ARDS (ARDS) and non-ARDS subjects (Normal). Scale bars, 100 µm. Black arrows indicate RIPK3-positive cells. (B) Quantification of intensity for RIPK3-positive staining in cells and (C) quantification of RIPK3-positive cells from immunohistochemistry images in A (ARDS, n=7; Normal, n=2; n = 10 images per individual subject). (D) Representative immunoblot images of RIPK3 phosphorylation (Ser227), RIPK3, MLKL phosphorylation (Ser358), MLKL, RIPK1 phosphorylation (Ser166) protein (left) and quantification of RIPK3 phosphorylation, RIPK3, MLKL phosphorylation, RIPK1 phosphorylation protein levels (right) in lung tissues from ARDS and Normal (n=2 per each group). β-actin or MLKL were used as loading control. Data are representative of three independent experiments. Data are mean±SD. ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or Mann–Whitney test.

Journal: Immune Network

Article Title: Impairment of Mitochondrial ATP Synthesis Induces RIPK3-dependent Necroptosis in Lung Epithelial Cells During Lung Injury by Lung Inflammation

doi: 10.4110/in.2022.22.e18

Figure Lengend Snippet: (A) Representative immunohistochemistry images for RIPK3 staining in lung tissues from patients with ARDS (ARDS) and non-ARDS subjects (Normal). Scale bars, 100 µm. Black arrows indicate RIPK3-positive cells. (B) Quantification of intensity for RIPK3-positive staining in cells and (C) quantification of RIPK3-positive cells from immunohistochemistry images in A (ARDS, n=7; Normal, n=2; n = 10 images per individual subject). (D) Representative immunoblot images of RIPK3 phosphorylation (Ser227), RIPK3, MLKL phosphorylation (Ser358), MLKL, RIPK1 phosphorylation (Ser166) protein (left) and quantification of RIPK3 phosphorylation, RIPK3, MLKL phosphorylation, RIPK1 phosphorylation protein levels (right) in lung tissues from ARDS and Normal (n=2 per each group). β-actin or MLKL were used as loading control. Data are representative of three independent experiments. Data are mean±SD. ** p<0.01; *** p<0.001 by Student’s 2-tailed t-test or Mann–Whitney test.

Article Snippet: After electrophoresis, proteins were transferred to polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA) or Protran nitrocellulose membranes (10600001; GE Healthcare Life Science, Pittsburgh, PA, USA) and blocked in 5% non-fat milk or 5% (w/v) BSA (9048-46-8; Santa Cruz Biotechnology, Dallas, TX, USA) in Tris-buffered saline containing 0.05% Tween-20 (TBS-T) (TBS [170-6435; Bio-Rad Laboratories, Hercules, CA, USA] and Tween-20 [170-6531'; Bio-Rad Laboratories]) at 25°C for 1 h. The membranes were immunoblotted with primary Abs against RIPK3 for mouse (AHP1797; Bio-Rad Laboratories), RIPK3 for human (ab62344; Abcam, Cambridge, UK), Phospho-RIPK3 (Thr231/Ser232) for mouse (ab222320; Abcam), Phospho-RIPK3 (Ser227) for human (ab209384; Abcam), Phospho-MLKL (Ser345) (ab196436; Abcam) for mouse, Phospho-MLKL (Ser358) (ab187091; Abcam) for human, MLKL (ab243142; Abcam) for mouse, MLKL (ab184718; Abcam) for human, Phospho-RIPK1 (Ser166) (#31122; Cell Signaling Technology, Danvers, MA, USA) for mouse, Phospho-RIPK1 (Ser166) (NBP3-06877; Novus, Littleton, CO, USA) for human, and β-actin (A5316; Sigma-Aldrich) overnight at 4°C and washed five times with TBS-T for 10 min each at room temperature.

Techniques: Immunohistochemistry, Staining, Western Blot, Phospho-proteomics, Control, MANN-WHITNEY

(A) Representative immunofluorescence images for MLKL phosphorylation at Ser358 (P-MLKL) staining (green) in lung epithelial cells expressing E-cadherin (red) of lung tissues from patients with ARDS (ARDS) and non-ARDS subjects (Normal). Scale bars, 20 µm. DAPI-stained nuclei are shown in blue. (B) Quantification of intensity for P-MLKL-positive staining and (C) quantification of P-MLKL and E-cadherin-positive cells from immunofluorescence images in A (ARDS, n=7; Normal, n=2; n=10 images per individual subject). (D) Representative immunoblot images of RIPK3 phosphorylation (Ser227), RIPK3, MLKL phosphorylation (Ser358), MLKL, RIPK1 phosphorylation (Ser166) protein from lung tissue sections of A. MLKL was used as loading control. (E) A schematic diagram to summarize our new findings. Red arrow means an increase and blue arrow means a decrease in the diagram. Data are representative of 3 independent experiments. Data are mean ± SD. ** p<0.01 by Student’s 2-tailed t-test.

Journal: Immune Network

Article Title: Impairment of Mitochondrial ATP Synthesis Induces RIPK3-dependent Necroptosis in Lung Epithelial Cells During Lung Injury by Lung Inflammation

doi: 10.4110/in.2022.22.e18

Figure Lengend Snippet: (A) Representative immunofluorescence images for MLKL phosphorylation at Ser358 (P-MLKL) staining (green) in lung epithelial cells expressing E-cadherin (red) of lung tissues from patients with ARDS (ARDS) and non-ARDS subjects (Normal). Scale bars, 20 µm. DAPI-stained nuclei are shown in blue. (B) Quantification of intensity for P-MLKL-positive staining and (C) quantification of P-MLKL and E-cadherin-positive cells from immunofluorescence images in A (ARDS, n=7; Normal, n=2; n=10 images per individual subject). (D) Representative immunoblot images of RIPK3 phosphorylation (Ser227), RIPK3, MLKL phosphorylation (Ser358), MLKL, RIPK1 phosphorylation (Ser166) protein from lung tissue sections of A. MLKL was used as loading control. (E) A schematic diagram to summarize our new findings. Red arrow means an increase and blue arrow means a decrease in the diagram. Data are representative of 3 independent experiments. Data are mean ± SD. ** p<0.01 by Student’s 2-tailed t-test.

Article Snippet: After electrophoresis, proteins were transferred to polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA) or Protran nitrocellulose membranes (10600001; GE Healthcare Life Science, Pittsburgh, PA, USA) and blocked in 5% non-fat milk or 5% (w/v) BSA (9048-46-8; Santa Cruz Biotechnology, Dallas, TX, USA) in Tris-buffered saline containing 0.05% Tween-20 (TBS-T) (TBS [170-6435; Bio-Rad Laboratories, Hercules, CA, USA] and Tween-20 [170-6531'; Bio-Rad Laboratories]) at 25°C for 1 h. The membranes were immunoblotted with primary Abs against RIPK3 for mouse (AHP1797; Bio-Rad Laboratories), RIPK3 for human (ab62344; Abcam, Cambridge, UK), Phospho-RIPK3 (Thr231/Ser232) for mouse (ab222320; Abcam), Phospho-RIPK3 (Ser227) for human (ab209384; Abcam), Phospho-MLKL (Ser345) (ab196436; Abcam) for mouse, Phospho-MLKL (Ser358) (ab187091; Abcam) for human, MLKL (ab243142; Abcam) for mouse, MLKL (ab184718; Abcam) for human, Phospho-RIPK1 (Ser166) (#31122; Cell Signaling Technology, Danvers, MA, USA) for mouse, Phospho-RIPK1 (Ser166) (NBP3-06877; Novus, Littleton, CO, USA) for human, and β-actin (A5316; Sigma-Aldrich) overnight at 4°C and washed five times with TBS-T for 10 min each at room temperature.

Techniques: Immunofluorescence, Phospho-proteomics, Staining, Expressing, Western Blot, Control