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image lab 5 2 1  (Bio-Rad)
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Bio-Rad image lab 5 2 1
SUMOylation and phosphorylation of Elk-1 in heat stressed HeLa cells. Elk-1 SUMOylation in heat stressed HeLa cells. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells that were either exposed to 42 °C or 45 °C for 1 h or left untreated (untreated control) with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Arrowheads indicate heat induced SUMOylated species of Elk-1. C unexposed control and GA ginkgolic acid. Input, 10% of the total protein used for immunoprecipitation. M/kD, migration of pre-stained molecular weight markers (Thermo Scientific Page Ruler prestained protein ladder; Cat. No. 26616) is indicated. b Same as a except that immunoprecipitation was carried out with anti-HA Ab and immunodetection with anti-Elk-1 and anti-HA Abs. c Elk-1 phosphorylation levels. Elk-1 phosphorylation levels in HeLaS1 cells exposed to conditions as indicated in the figure was determined in 30 μg whole cell extract by western blotting using anti-phospho-Elk-1 and anti-Elk-1 Abs. All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001 relative to control and heat exposed groups was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test
Image Lab 5 2 1, supplied by Bio-Rad, 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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chemidoc mp imaging system  (Bio-Rad)
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Bio-Rad chemidoc mp imaging system
SUMOylation and phosphorylation of Elk-1 in heat stressed HeLa cells. Elk-1 SUMOylation in heat stressed HeLa cells. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells that were either exposed to 42 °C or 45 °C for 1 h or left untreated (untreated control) with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Arrowheads indicate heat induced SUMOylated species of Elk-1. C unexposed control and GA ginkgolic acid. Input, 10% of the total protein used for immunoprecipitation. M/kD, migration of pre-stained molecular weight markers (Thermo Scientific Page Ruler prestained protein ladder; Cat. No. 26616) is indicated. b Same as a except that immunoprecipitation was carried out with anti-HA Ab and immunodetection with anti-Elk-1 and anti-HA Abs. c Elk-1 phosphorylation levels. Elk-1 phosphorylation levels in HeLaS1 cells exposed to conditions as indicated in the figure was determined in 30 μg whole cell extract by western blotting using anti-phospho-Elk-1 and anti-Elk-1 Abs. All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001 relative to control and heat exposed groups was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test
Chemidoc Mp Imaging System, supplied by Bio-Rad, 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/image+lab+5+2+biorad+laboratories+imagequant/pm30625344-109-7-6?v=Bio-Rad
Average 99 stars, based on 1 article reviews
chemidoc mp imaging system - by Bioz Stars, 2026-08
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Image Search Results


SUMOylation and phosphorylation of Elk-1 in heat stressed HeLa cells. Elk-1 SUMOylation in heat stressed HeLa cells. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells that were either exposed to 42 °C or 45 °C for 1 h or left untreated (untreated control) with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Arrowheads indicate heat induced SUMOylated species of Elk-1. C unexposed control and GA ginkgolic acid. Input, 10% of the total protein used for immunoprecipitation. M/kD, migration of pre-stained molecular weight markers (Thermo Scientific Page Ruler prestained protein ladder; Cat. No. 26616) is indicated. b Same as a except that immunoprecipitation was carried out with anti-HA Ab and immunodetection with anti-Elk-1 and anti-HA Abs. c Elk-1 phosphorylation levels. Elk-1 phosphorylation levels in HeLaS1 cells exposed to conditions as indicated in the figure was determined in 30 μg whole cell extract by western blotting using anti-phospho-Elk-1 and anti-Elk-1 Abs. All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001 relative to control and heat exposed groups was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test

Journal: Cell Stress & Chaperones

Article Title: p38 MAPK pathway-dependent SUMOylation of Elk-1 and phosphorylation of PIAS2 correlate with the downregulation of Elk-1 activity in heat-stressed HeLa cells

doi: 10.1007/s12192-019-00974-4

Figure Lengend Snippet: SUMOylation and phosphorylation of Elk-1 in heat stressed HeLa cells. Elk-1 SUMOylation in heat stressed HeLa cells. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells that were either exposed to 42 °C or 45 °C for 1 h or left untreated (untreated control) with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Arrowheads indicate heat induced SUMOylated species of Elk-1. C unexposed control and GA ginkgolic acid. Input, 10% of the total protein used for immunoprecipitation. M/kD, migration of pre-stained molecular weight markers (Thermo Scientific Page Ruler prestained protein ladder; Cat. No. 26616) is indicated. b Same as a except that immunoprecipitation was carried out with anti-HA Ab and immunodetection with anti-Elk-1 and anti-HA Abs. c Elk-1 phosphorylation levels. Elk-1 phosphorylation levels in HeLaS1 cells exposed to conditions as indicated in the figure was determined in 30 μg whole cell extract by western blotting using anti-phospho-Elk-1 and anti-Elk-1 Abs. All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001 relative to control and heat exposed groups was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test

Article Snippet: All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software.

Techniques: Immunoprecipitation, Immunodetection, Migration, Staining, Molecular Weight, Western Blot, Software

Elk-1 is SUMOylated by p38 MAPK-dependent mechanisms. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells exposed to conditions as indicated below with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Prior to exposure to heat stress cells were treated with MAPK pathway inhibitors (SB, U0 and SP) as described in legend to Fig. ​Fig.2,2, PMA was used as negative control. Input: 10% of the total protein incubated for IP. b Same as a except that IP was carried out with anti-HA Ab and immuno-blotting with anti-Elk-1 and anti-HA Abs. C unexposed control and H Heat stress at 45 °C for 1 h. Band intensities were estimated using BioRad Image Lab 5.2.1 and ImageJ software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001, relative to control was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test. M/kD, migration of pre-stained molecular weight markers is indicated

Journal: Cell Stress & Chaperones

Article Title: p38 MAPK pathway-dependent SUMOylation of Elk-1 and phosphorylation of PIAS2 correlate with the downregulation of Elk-1 activity in heat-stressed HeLa cells

doi: 10.1007/s12192-019-00974-4

Figure Lengend Snippet: Elk-1 is SUMOylated by p38 MAPK-dependent mechanisms. a Elk-1 was immunoprecipitated from 1 mg extract prepared from HeLaS1 cells exposed to conditions as indicated below with 1 μg anti-Elk-1 Ab followed by blotting and immunodetection using Abs as indicated in the fig. Prior to exposure to heat stress cells were treated with MAPK pathway inhibitors (SB, U0 and SP) as described in legend to Fig. ​Fig.2,2, PMA was used as negative control. Input: 10% of the total protein incubated for IP. b Same as a except that IP was carried out with anti-HA Ab and immuno-blotting with anti-Elk-1 and anti-HA Abs. C unexposed control and H Heat stress at 45 °C for 1 h. Band intensities were estimated using BioRad Image Lab 5.2.1 and ImageJ software. Data are represented as mean ± SEM of triplicate experiments. ***p < 0.001, relative to control was determined by one-way ANOVA followed by adjustment for multiple comparisons using Tukey’s test. M/kD, migration of pre-stained molecular weight markers is indicated

Article Snippet: All experiments were performed in triplicates and band intensities were estimated using BioRad Image Lab 5.2.1 and Image J software.

Techniques: Immunoprecipitation, Immunodetection, Negative Control, Incubation, Software, Migration, Staining, Molecular Weight