p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit monoclonal anti p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti p erk1 2
    Rabbit Monoclonal Anti P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    Myocardial expression and activation of MAPK signaling proteins. ( A ) Western blottings were used to examine the protein levels of total p38, phosphorylated p38, total JNK, phosphorylated JNK, total <t>ERK1/2,</t> phosphorylated ERK1/2, and actin. ( B-E ) Comparisons of protein expressions among different treatment groups. In both normal and AMI conditions, ratios of phosphorylated p38 to total p38 and phosphorylated JNK to total JNK showed no statistical significance between WT mice and MYH6-Flag-GPR22 mice ( B-D ). In AMI condition, myocardial levels of phosphorylated ERK1/2 in MYH6-Flag-GPR22 mice were lower than that without GPR22 overexpression. WT, wild-type mice. GPR22Tg, MYH6-Flag-GPR22 transgenic mice. n = 6 for each group. * indicates a statistical significance compared with the WT group. † indicates a statistical significance compared with the WT-AMI group. Full-length blots are presented in Supplementary Fig. 2
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Cardiomyocyte-specific overexpression of GPR22 ameliorates cardiac injury in mice with acute myocardial infarction"

    Article Title: Cardiomyocyte-specific overexpression of GPR22 ameliorates cardiac injury in mice with acute myocardial infarction

    Journal: BMC Cardiovascular Disorders

    doi: 10.1186/s12872-024-03953-5

    Myocardial expression and activation of MAPK signaling proteins. ( A ) Western blottings were used to examine the protein levels of total p38, phosphorylated p38, total JNK, phosphorylated JNK, total ERK1/2, phosphorylated ERK1/2, and actin. ( B-E ) Comparisons of protein expressions among different treatment groups. In both normal and AMI conditions, ratios of phosphorylated p38 to total p38 and phosphorylated JNK to total JNK showed no statistical significance between WT mice and MYH6-Flag-GPR22 mice ( B-D ). In AMI condition, myocardial levels of phosphorylated ERK1/2 in MYH6-Flag-GPR22 mice were lower than that without GPR22 overexpression. WT, wild-type mice. GPR22Tg, MYH6-Flag-GPR22 transgenic mice. n = 6 for each group. * indicates a statistical significance compared with the WT group. † indicates a statistical significance compared with the WT-AMI group. Full-length blots are presented in Supplementary Fig. 2
    Figure Legend Snippet: Myocardial expression and activation of MAPK signaling proteins. ( A ) Western blottings were used to examine the protein levels of total p38, phosphorylated p38, total JNK, phosphorylated JNK, total ERK1/2, phosphorylated ERK1/2, and actin. ( B-E ) Comparisons of protein expressions among different treatment groups. In both normal and AMI conditions, ratios of phosphorylated p38 to total p38 and phosphorylated JNK to total JNK showed no statistical significance between WT mice and MYH6-Flag-GPR22 mice ( B-D ). In AMI condition, myocardial levels of phosphorylated ERK1/2 in MYH6-Flag-GPR22 mice were lower than that without GPR22 overexpression. WT, wild-type mice. GPR22Tg, MYH6-Flag-GPR22 transgenic mice. n = 6 for each group. * indicates a statistical significance compared with the WT group. † indicates a statistical significance compared with the WT-AMI group. Full-length blots are presented in Supplementary Fig. 2

    Techniques Used: Expressing, Activation Assay, Western Blot, Over Expression, Transgenic Assay

    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    Loss of miR‐31 represses PTC development in transgenic mice. (A) In situ hybridisation of miR‐31 in thyroid tissues from Tpo‐cre (WT) and Tpo‐cre/Braf V600E (mPTC) litter‐mates at 4 and 8w. Scale bar, 100 µm. (B) miR‐31 expression was measured by qRT‐PCR in thyroid tissues from WT and mPTC litter‐mates at 5w, U6 was used as the loading control, n = 10. (C) Representative images of GFP (green) and DAPI (blue) staining of tumour tissue from mPTC GFP mouse at 5w, white dotted line marked the tumour area. Scale bar, 100 µm. (D) BRAF/MAPK signalling factors were analysed by western blot in mPTC GFP primary cells treated with BRAF inhibitor PLX4032 and <t>ERK1/2</t> inhibitor SCH772984 for 24 h. (E) miR‐31 expression was measured by qRT‐PCR in mPTC GFP primary cells treated with PLX4032 and SCH772984 at 0, 12, 24 and 36 h. (F) Representative picture of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. (G) Representative H&E and Ki67 staining of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. Red arrow pointed to tall cells and black arrow pointed to nuclear pseudoinclusion. The percentage of tall cells and Ki67 positive cells in whole pictures were counted, n = 5. Scale bar, 50 µm. (H and I) Tumour weight (H) and mouse weight (I) of mPTC ( n = 8), mPTC/miR‐31 +/− ( n = 12) and mPTC/miR‐31 −/− ( n = 8) were plotted, the comparisons were between mPTC and mPTC/miR‐31 +/− or mPTC/miR‐31 −/− . A representative of three independent experiments was shown (A, C and D). All statistical analyses were performed using two‐tailed unpaired Student's t ‐test. Data represent mean ± SD. * p < .05, ** p < .01, *** p < .001, ns (not significant).
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Targeting miR‐31 represses tumourigenesis and dedifferentiation of BRAF V600E ‐associated thyroid carcinoma"

    Article Title: Targeting miR‐31 represses tumourigenesis and dedifferentiation of BRAF V600E ‐associated thyroid carcinoma

    Journal: Clinical and Translational Medicine

    doi: 10.1002/ctm2.1694

    Loss of miR‐31 represses PTC development in transgenic mice. (A) In situ hybridisation of miR‐31 in thyroid tissues from Tpo‐cre (WT) and Tpo‐cre/Braf V600E (mPTC) litter‐mates at 4 and 8w. Scale bar, 100 µm. (B) miR‐31 expression was measured by qRT‐PCR in thyroid tissues from WT and mPTC litter‐mates at 5w, U6 was used as the loading control, n = 10. (C) Representative images of GFP (green) and DAPI (blue) staining of tumour tissue from mPTC GFP mouse at 5w, white dotted line marked the tumour area. Scale bar, 100 µm. (D) BRAF/MAPK signalling factors were analysed by western blot in mPTC GFP primary cells treated with BRAF inhibitor PLX4032 and ERK1/2 inhibitor SCH772984 for 24 h. (E) miR‐31 expression was measured by qRT‐PCR in mPTC GFP primary cells treated with PLX4032 and SCH772984 at 0, 12, 24 and 36 h. (F) Representative picture of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. (G) Representative H&E and Ki67 staining of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. Red arrow pointed to tall cells and black arrow pointed to nuclear pseudoinclusion. The percentage of tall cells and Ki67 positive cells in whole pictures were counted, n = 5. Scale bar, 50 µm. (H and I) Tumour weight (H) and mouse weight (I) of mPTC ( n = 8), mPTC/miR‐31 +/− ( n = 12) and mPTC/miR‐31 −/− ( n = 8) were plotted, the comparisons were between mPTC and mPTC/miR‐31 +/− or mPTC/miR‐31 −/− . A representative of three independent experiments was shown (A, C and D). All statistical analyses were performed using two‐tailed unpaired Student's t ‐test. Data represent mean ± SD. * p < .05, ** p < .01, *** p < .001, ns (not significant).
    Figure Legend Snippet: Loss of miR‐31 represses PTC development in transgenic mice. (A) In situ hybridisation of miR‐31 in thyroid tissues from Tpo‐cre (WT) and Tpo‐cre/Braf V600E (mPTC) litter‐mates at 4 and 8w. Scale bar, 100 µm. (B) miR‐31 expression was measured by qRT‐PCR in thyroid tissues from WT and mPTC litter‐mates at 5w, U6 was used as the loading control, n = 10. (C) Representative images of GFP (green) and DAPI (blue) staining of tumour tissue from mPTC GFP mouse at 5w, white dotted line marked the tumour area. Scale bar, 100 µm. (D) BRAF/MAPK signalling factors were analysed by western blot in mPTC GFP primary cells treated with BRAF inhibitor PLX4032 and ERK1/2 inhibitor SCH772984 for 24 h. (E) miR‐31 expression was measured by qRT‐PCR in mPTC GFP primary cells treated with PLX4032 and SCH772984 at 0, 12, 24 and 36 h. (F) Representative picture of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. (G) Representative H&E and Ki67 staining of thyroid tumours from mPTC, mPTC/miR‐31 +/− and mPTC/miR‐31 −/− litter‐mates at 5w. Red arrow pointed to tall cells and black arrow pointed to nuclear pseudoinclusion. The percentage of tall cells and Ki67 positive cells in whole pictures were counted, n = 5. Scale bar, 50 µm. (H and I) Tumour weight (H) and mouse weight (I) of mPTC ( n = 8), mPTC/miR‐31 +/− ( n = 12) and mPTC/miR‐31 −/− ( n = 8) were plotted, the comparisons were between mPTC and mPTC/miR‐31 +/− or mPTC/miR‐31 −/− . A representative of three independent experiments was shown (A, C and D). All statistical analyses were performed using two‐tailed unpaired Student's t ‐test. Data represent mean ± SD. * p < .05, ** p < .01, *** p < .001, ns (not significant).

    Techniques Used: Transgenic Assay, In Situ, Hybridization, Expressing, Quantitative RT-PCR, Staining, Western Blot, Two Tailed Test

    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    Capsaicin-induced calcium influx and modulation of LPS-induced signaling cascades. The kinetics of capsaicin-induced calcium mobilization in J774 cells were measured by the fluorescence of FLUO4-NW ( a ). Data represent mean values ± SEM. The level of statistical significance was determined using 2-way ANOVA followed by Tukey’s test for multiple comparisons (**** p < 0.0001). For detection of LPS-induced signaling cascades J774 were preincubated for 4 h and stimulated with capsaicin (C) or LPS (L) for 5–10 min. The ratio between phosphorylated and unphosphorylated p-38 ( b ) and ERK 1/2 ( c ) was obtained by Western blotting after normalizing the intensities of the p-p38 <t>and</t> <t>p-ERK1/2</t> bands to those of total p38 and ERK1/2, respectively. Uncropped images of the western blot membranes are also shown in Supplementary Fig. and . Data are shown as boxes and whiskers. The lines within the boxes represent the median, and the whiskers represent the minimum and maximum values. n = 6 ( a-c ). Representative western blots are shown. The percentage of cells in which ERK1/2 translocated to the nucleus was determined by image flow cytometry. n = 3 ( d ). Data are shown as means ± SD. The level of statistical significance was determined using one-way ANOVA followed by Tukey’s test for multiple comparisons ( n p < 0.05, nn p < 0.01, nnn p < 0.001, nnnn p < 0.0001). # indicates the significance from (– –) group. + indicates significance from (C –) group. Other statistical significances between groups are indicated by *
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Lipopolysaccharide pretreatment increases the sensitivity of the TRPV1 channel and promotes an anti-inflammatory phenotype of capsaicin-activated macrophages"

    Article Title: Lipopolysaccharide pretreatment increases the sensitivity of the TRPV1 channel and promotes an anti-inflammatory phenotype of capsaicin-activated macrophages

    Journal: Journal of Inflammation (London, England)

    doi: 10.1186/s12950-024-00391-0

    Capsaicin-induced calcium influx and modulation of LPS-induced signaling cascades. The kinetics of capsaicin-induced calcium mobilization in J774 cells were measured by the fluorescence of FLUO4-NW ( a ). Data represent mean values ± SEM. The level of statistical significance was determined using 2-way ANOVA followed by Tukey’s test for multiple comparisons (**** p < 0.0001). For detection of LPS-induced signaling cascades J774 were preincubated for 4 h and stimulated with capsaicin (C) or LPS (L) for 5–10 min. The ratio between phosphorylated and unphosphorylated p-38 ( b ) and ERK 1/2 ( c ) was obtained by Western blotting after normalizing the intensities of the p-p38 and p-ERK1/2 bands to those of total p38 and ERK1/2, respectively. Uncropped images of the western blot membranes are also shown in Supplementary Fig. and . Data are shown as boxes and whiskers. The lines within the boxes represent the median, and the whiskers represent the minimum and maximum values. n = 6 ( a-c ). Representative western blots are shown. The percentage of cells in which ERK1/2 translocated to the nucleus was determined by image flow cytometry. n = 3 ( d ). Data are shown as means ± SD. The level of statistical significance was determined using one-way ANOVA followed by Tukey’s test for multiple comparisons ( n p < 0.05, nn p < 0.01, nnn p < 0.001, nnnn p < 0.0001). # indicates the significance from (– –) group. + indicates significance from (C –) group. Other statistical significances between groups are indicated by *
    Figure Legend Snippet: Capsaicin-induced calcium influx and modulation of LPS-induced signaling cascades. The kinetics of capsaicin-induced calcium mobilization in J774 cells were measured by the fluorescence of FLUO4-NW ( a ). Data represent mean values ± SEM. The level of statistical significance was determined using 2-way ANOVA followed by Tukey’s test for multiple comparisons (**** p < 0.0001). For detection of LPS-induced signaling cascades J774 were preincubated for 4 h and stimulated with capsaicin (C) or LPS (L) for 5–10 min. The ratio between phosphorylated and unphosphorylated p-38 ( b ) and ERK 1/2 ( c ) was obtained by Western blotting after normalizing the intensities of the p-p38 and p-ERK1/2 bands to those of total p38 and ERK1/2, respectively. Uncropped images of the western blot membranes are also shown in Supplementary Fig. and . Data are shown as boxes and whiskers. The lines within the boxes represent the median, and the whiskers represent the minimum and maximum values. n = 6 ( a-c ). Representative western blots are shown. The percentage of cells in which ERK1/2 translocated to the nucleus was determined by image flow cytometry. n = 3 ( d ). Data are shown as means ± SD. The level of statistical significance was determined using one-way ANOVA followed by Tukey’s test for multiple comparisons ( n p < 0.05, nn p < 0.01, nnn p < 0.001, nnnn p < 0.0001). # indicates the significance from (– –) group. + indicates significance from (C –) group. Other statistical significances between groups are indicated by *

    Techniques Used: Fluorescence, Western Blot, Flow Cytometry

    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; <t>(b)</t> <t>p-ERK1/2,</t> ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Complex interactions with several arms of the complement system dictate innate and humoral immunity to adenoviral vectors"

    Article Title: Complex interactions with several arms of the complement system dictate innate and humoral immunity to adenoviral vectors

    Journal: Gene therapy

    doi: 10.1038/gt.2008.114

    The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; (b) p-ERK1/2, ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).
    Figure Legend Snippet: The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; (b) p-ERK1/2, ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).

    Techniques Used: Recombinant, Plasmid Preparation, Injection, Western Blot

    p erk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p erk1 2
    The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; <t>(b)</t> <t>p-ERK1/2,</t> ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).
    P Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p erk1 2/product/Cell Signaling Technology Inc
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    p erk1 2 - by Bioz Stars, 2024-06
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    Images

    1) Product Images from "Complex interactions with several arms of the complement system dictate innate and humoral immunity to adenoviral vectors"

    Article Title: Complex interactions with several arms of the complement system dictate innate and humoral immunity to adenoviral vectors

    Journal: Gene therapy

    doi: 10.1038/gt.2008.114

    The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; (b) p-ERK1/2, ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).
    Figure Legend Snippet: The role of C3 in recombinant adenovirus (rAd) vector-induced ERK phosphorylation and IκBα degradation. Wild-type C57BL/6 and C3-KO mice were injected intravenously with rAd5-LacZ (1.5 × 1011 viral particles per mouse). Livers were collected at the indicated time points, snap-frozen and lysates extracted as described in the Materials and methods section. (a) IκBα and tubulin; (b) p-ERK1/2, ERK2 were determined by western blot analysis using LI-COR. Quantification was performed by normalizing the p-ERK1/2 levels to total ERK2 and IκBα levels to tubulin to control for loading (N = 3 for all time points). For each analysis, quantification is shown on the top, and a representative blot on the bottom. Bars represent mean ± s.d. A homoscedastic t-test was used to determine statistical differences between levels in C57BL/6 livers compared with levels in C3-KO mouse livers at each indicated time point (*P<0.05).

    Techniques Used: Recombinant, Plasmid Preparation, Injection, Western Blot

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