nih3t3 Search Results


nih3t3  (ATCC)
93
ATCC nih3t3
Effect of exosomes from P. peruviana on cell viability. (A) RAW 264,7 cells were exposed to different concentration of exosomes. (B) <t>NIH3T3</t> cells were treated with various concentrations of exosomes. Data are expressed as mean ± SD. ( n = 4 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Ct (untreated control), using one‐way ANOVA followed by Tukey's multiple comparison test.
Nih3t3, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Novus Biologicals nih3t3 whole cell lysate
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
Nih3t3 Whole Cell Lysate, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
ATCC cell culture mouse fibroblast nih 3t3 cells
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
Cell Culture Mouse Fibroblast Nih 3t3 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC 3t3 j2 feeder cells
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
3t3 J2 Feeder Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
AcceGen Biotechnology nih 3t3
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
Nih 3t3, supplied by AcceGen Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
DSMZ nih 3t3
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
Nih 3t3, supplied by DSMZ, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nih3t3/NIH-3T3/10__7554_slash_elife__19850-326-61-78
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92
Santa Cruz Biotechnology p thr
Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. <t>NIH3T3</t> (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.
P Thr, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Santa Cruz Biotechnology nih3t3 cells
Fig. 1. Interaction of S100A6 with cofilin-1 in <t>NIH3T3</t> fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.
Nih3t3 Cells, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC mouse nih 3t3 embryonic fibroblast cells
Fig. 1. Interaction of S100A6 with cofilin-1 in <t>NIH3T3</t> fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.
Mouse Nih 3t3 Embryonic Fibroblast Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nih3t3/NIH%2F3T3%3B+Embryonic+Fibroblast%3B+Mouse/10__1523_slash_jneurosci__5954___08__2009-51-15-29
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3t3  (ATCC)
93
ATCC 3t3
Fig. 1. Interaction of S100A6 with cofilin-1 in <t>NIH3T3</t> fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.
3t3, supplied by ATCC, 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/nih3t3/K%3AMolv+NIH%2F3T3/us07074901-1545-67-68
Average 93 stars, based on 1 article reviews
3t3 - by Bioz Stars, 2026-09
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93
Santa Cruz Biotechnology cleaved caspase 3
Fig. 1. Interaction of S100A6 with cofilin-1 in <t>NIH3T3</t> fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.
Cleaved Caspase 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
Santa Cruz Biotechnology cell lysate
Fig. 1. Interaction of S100A6 with cofilin-1 in <t>NIH3T3</t> fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.
Cell Lysate, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Effect of exosomes from P. peruviana on cell viability. (A) RAW 264,7 cells were exposed to different concentration of exosomes. (B) NIH3T3 cells were treated with various concentrations of exosomes. Data are expressed as mean ± SD. ( n = 4 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Ct (untreated control), using one‐way ANOVA followed by Tukey's multiple comparison test.

Journal: Molecular Nutrition & Food Research

Article Title: Therapeutic Modulation of Inflammatory Signaling via Physalis Peruviana ‐Derived Exosomes: A Targeted Effect on IKK/NFκB/STAT1

doi: 10.1002/mnfr.70458

Figure Lengend Snippet: Effect of exosomes from P. peruviana on cell viability. (A) RAW 264,7 cells were exposed to different concentration of exosomes. (B) NIH3T3 cells were treated with various concentrations of exosomes. Data are expressed as mean ± SD. ( n = 4 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Ct (untreated control), using one‐way ANOVA followed by Tukey's multiple comparison test.

Article Snippet: NIH3T3 were acquired from ATCC (ATCC No. CRL‐1658.2) were subculture at a density of 3–5 × 10 3 cells/cm 2 in DMEM medium (Lonza) supplemented with 10% FBS, 1% penicillin‐streptomycin, and 4 mM L‐glutamine.

Techniques: Concentration Assay, Control, Comparison

Antioxidant effect of P. peruviana exosomes in NIH3T3 cells. (A) Changes in cell viability after treatment with different concentrations of H 2 O 2 , (B) Cells treated with 500 µM H 2 O 2 and different concentrations of exosomes. Data are expressed as mean ± SD. ( n = 4 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Control (A) and to H 2 O 2 500 µM group (B), using one‐way ANOVA followed by Tukey's multiple comparison test.

Journal: Molecular Nutrition & Food Research

Article Title: Therapeutic Modulation of Inflammatory Signaling via Physalis Peruviana ‐Derived Exosomes: A Targeted Effect on IKK/NFκB/STAT1

doi: 10.1002/mnfr.70458

Figure Lengend Snippet: Antioxidant effect of P. peruviana exosomes in NIH3T3 cells. (A) Changes in cell viability after treatment with different concentrations of H 2 O 2 , (B) Cells treated with 500 µM H 2 O 2 and different concentrations of exosomes. Data are expressed as mean ± SD. ( n = 4 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Control (A) and to H 2 O 2 500 µM group (B), using one‐way ANOVA followed by Tukey's multiple comparison test.

Article Snippet: NIH3T3 were acquired from ATCC (ATCC No. CRL‐1658.2) were subculture at a density of 3–5 × 10 3 cells/cm 2 in DMEM medium (Lonza) supplemented with 10% FBS, 1% penicillin‐streptomycin, and 4 mM L‐glutamine.

Techniques: Control, Comparison

Antioxidant enzymes expression levels following exposure to P. peruviana exosomes, H2O2 and exosomes + H2O2 in NIH3T3 cells. Data are expressed as mean ± SD. ( n = 3 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Control using one‐way ANOVA followed by Tukey's multiple comparison test. CAT, catalase; SOD1, superoxide dismutase 1; SOD2, superoxide dismutase 2; Cyt C ox, cytochrome c oxidase; GPx4, glutathione peroxidase 4.

Journal: Molecular Nutrition & Food Research

Article Title: Therapeutic Modulation of Inflammatory Signaling via Physalis Peruviana ‐Derived Exosomes: A Targeted Effect on IKK/NFκB/STAT1

doi: 10.1002/mnfr.70458

Figure Lengend Snippet: Antioxidant enzymes expression levels following exposure to P. peruviana exosomes, H2O2 and exosomes + H2O2 in NIH3T3 cells. Data are expressed as mean ± SD. ( n = 3 biological replicates) * p < 0.05, ** p < 0.01, *** p < 0.001 compared to Control using one‐way ANOVA followed by Tukey's multiple comparison test. CAT, catalase; SOD1, superoxide dismutase 1; SOD2, superoxide dismutase 2; Cyt C ox, cytochrome c oxidase; GPx4, glutathione peroxidase 4.

Article Snippet: NIH3T3 were acquired from ATCC (ATCC No. CRL‐1658.2) were subculture at a density of 3–5 × 10 3 cells/cm 2 in DMEM medium (Lonza) supplemented with 10% FBS, 1% penicillin‐streptomycin, and 4 mM L‐glutamine.

Techniques: Expressing, Control, Comparison

Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. NIH3T3 (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.

Journal: International Journal of Dentistry

Article Title: Acinar Cell Proliferation Promoted by BMP2 in Injured Mouse Parotid Gland: BMP2 Promotes Cell Proliferation in Parotid Gland

doi: 10.1155/2023/1765317

Figure Lengend Snippet: Mouse parotid acinar cells in primary culture. (a) Cell proliferative capacity of BMP2-added (100 ng/mL) and nonadded (control) groups after 48 hr of culture. The proliferative capacity of BMP2-added cultured cells was significantly increased compared to that in the control group. ∗∗ Indicates significance at P < 0.01, ∗ P < 0.05. Data were shown as mean ± SD. Three independent experiments were performed. (b) Protein expression of E-cadherin (an epithelial marker) and vimentin (a mesenchymal marker) in cultured cells of each group at 48 hr after the addition of BMP2. NIH3T3 (3T3) was used as a positive control for mesenchymal markers. RS: rat serum.

Article Snippet: NIH3T3 whole cell lysate (Novus Biologicals, Centennial, CO, USA) was used as a positive control for mesenchymal markers.

Techniques: Control, Cell Culture, Expressing, Marker, Positive Control

Fig. 1. Interaction of S100A6 with cofilin-1 in NIH3T3 fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.

Journal: Cell calcium

Article Title: Ca 2+ -dependent binding of S100A6 to cofilin-1 regulates actin filament polymerization-depolymerization dynamics.

doi: 10.1016/j.ceca.2021.102457

Figure Lengend Snippet: Fig. 1. Interaction of S100A6 with cofilin-1 in NIH3T3 fibroblasts. (A) Pull-down assay with the use of protein lysate from NIH3T3 cells and S100A6 affinity resin (upper panel) or empty resin (lower panel). Lanes: 1-input, 2-unbound fraction, 3-last wash, 4-first wash with 0.5 M NaCl, 5-last wash with 0.5 M NaCl, 6-first wash with 1 M NaCl, 7- last wash with 1 M NaCl, 8- elution in buffer containing EGTA. Fractions were analyzed by SDS-PAGE (15% gel) fol lowed by immunoblotting developed with anti- cofilin-1 antibody. (B) Co-immunoprecipitation of S100A6 with cofilin-1 from NIH3T3 cell lysate. 30 μg of protein lysate was used directly for immunoblotting (input; lane 1 in both upper and lower panel) and 2.5 mg of protein lysate was incubated with (upper panel) or without (control, lower panel) anti-S100A6 monoclonal antibody and then with protein A/G agarose. In both panels, lane 2 shows unbound fraction, lane 3-last wash and lane 4-elution. Proteins were identified by immunoblotting using anti- cofilin-1 antibody. (C) Presence of S100A6- cofilin-1 complexes in NIH3T3 cells studied by PLA. Complexes of examined proteins are visualized in red; cell nuclei, stained with DAPI, are in blue. Scale bar is 20 μm.

Article Snippet: For co-immunoprecipitation assays 2.5 mg of protein lysate from NIH3T3 cells, obtained using the Plasma Membrane Protein Extraction Kit (Abcam) according to the manufacturer’s instruction was incubated with protein A/G-Agarose (Santa Cruz Biotechnology) for 1 h at 4◦C, as described by Jurewicz et al. [31].

Techniques: Pull Down Assay, SDS Page, Western Blot, Immunoprecipitation, Incubation, Control, Staining