egr1 primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc egr1 primary antibody
    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and <t>Egr1</t> protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.
    Egr1 Primary Antibody, supplied by Cell Signaling Technology Inc, 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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    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    egr1 primary antibody - by Bioz Stars, 2023-03
    93/100 stars

    Images

    1) Product Images from "A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription"

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0116825

    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.
    Figure Legend Snippet: A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.

    Techniques Used: Variant Assay, Real-time Polymerase Chain Reaction, Agarose Gel Electrophoresis, Expressing, Western Blot, Chromatin Immunoprecipitation, Binding Assay

    A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.
    Figure Legend Snippet: A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.

    Techniques Used: Variant Assay, Reverse Transcription Polymerase Chain Reaction, Negative Control, SDS Page, Western Blot

    LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.
    Figure Legend Snippet: LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.

    Techniques Used: Incubation, Real-time Polymerase Chain Reaction, Binding Assay

    LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.
    Figure Legend Snippet: LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.

    Techniques Used: Transfection, Incubation, RNA Extraction, Western Blot, Expressing, Variant Assay

    WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.
    Figure Legend Snippet: WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.

    Techniques Used: Activity Assay, Expressing

    egr1 primary antibody  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Structured Review

    Cell Signaling Technology Inc egr1 primary antibody
    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and <t>Egr1</t> protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.
    Egr1 Primary Antibody, supplied by Cell Signaling Technology Inc, 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/result/egr1 primary antibody/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    egr1 primary antibody - by Bioz Stars, 2023-03
    93/100 stars

    Images

    1) Product Images from "A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription"

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0116825

    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.
    Figure Legend Snippet: A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.

    Techniques Used: Variant Assay, Real-time Polymerase Chain Reaction, Agarose Gel Electrophoresis, Expressing, Western Blot, Chromatin Immunoprecipitation, Binding Assay

    A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.
    Figure Legend Snippet: A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.

    Techniques Used: Variant Assay, Reverse Transcription Polymerase Chain Reaction, Negative Control, SDS Page, Western Blot

    LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.
    Figure Legend Snippet: LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.

    Techniques Used: Incubation, Real-time Polymerase Chain Reaction, Binding Assay

    LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.
    Figure Legend Snippet: LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.

    Techniques Used: Transfection, Incubation, RNA Extraction, Western Blot, Expressing, Variant Assay

    WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.
    Figure Legend Snippet: WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.

    Techniques Used: Activity Assay, Expressing

    primary antibodies against egr1  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Structured Review

    Cell Signaling Technology Inc primary antibodies against egr1
    <t>Egr1</t> was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).
    Primary Antibodies Against Egr1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibodies against egr1/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    primary antibodies against egr1 - by Bioz Stars, 2023-03
    94/100 stars

    Images

    1) Product Images from "Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2"

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    Journal: International Journal of Biological Sciences

    doi: 10.7150/ijbs.71781

    Egr1 was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).
    Figure Legend Snippet: Egr1 was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).

    Techniques Used: RNA Sequencing Assay, Western Blot, Immunohistochemical staining, Staining, Fluorescence

    Egr1 overexpression ameliorated acute AILI. Egr1 fl/fl and Egr1 LKO mice were injected with Ad-Egr1 or Ad-GFP via tail vein prior to 300 mg/kg APAP administration. After 12 h, liver and serum samples were collected. a. The survival rate analysis in Egr1 fl/fl and Egr1 LKO mice after 750 mg/kg APAP treatment (n = 12 mice/ Egr1 fl/fl group, n = 17 mice/ Egr1 LKO group, Log-rank (Mantel-Cox) test). b. Relative Egr1 mRNA levels in Ad-Egr1 or Ad-GFP pretreated mice (n = 3 mice/group, t test). c. Immunohistochemical staining images of Egr1 in the liver tissue of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice (scale bar = 100 μm), followed by quantified the numbers of Egr1 positive cells per HPF (n = 3 mice/group, one-way ANOVA). Red arrows represent positive staining. d. Western blot analysis of Egr1 levels of total protein in the liver tissues of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice, followed by quantified protein levels (n = 3 mice/group, one-way ANOVA). e. Hepatic GSH levels in Egr1 fl/fl and Egr1 LKO mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test), and in Ad-Egr1 or Ad-GFP pretreated mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test). f. Western blot analysis of CYP2E1 levels in the liver tissues of Egr1 fl/fl and Egr1 LKO mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). g. Western blot analysis of CYP2E1 levels in the liver tissues of Ad-Egr1 and Ad-GFP mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). h. Serum ALT, AST, and LDH levels in Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were measured ( n = 4-5 mice/group, one-way ANOVA). i. Serum CK18-M30 and CK18-M65 levels in Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were measured ( n = 4-5 mice/group, one-way ANOVA). j. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were stained with H&E, followed by quantified the area of hepatocyte necrosis (scale bars = 500 μm, one-way ANOVA). k. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were stained with TUNEL, followed by quantified the numbers of TUNEL positive cells per HFP (scale bars = 500 μm, one-way ANOVA).
    Figure Legend Snippet: Egr1 overexpression ameliorated acute AILI. Egr1 fl/fl and Egr1 LKO mice were injected with Ad-Egr1 or Ad-GFP via tail vein prior to 300 mg/kg APAP administration. After 12 h, liver and serum samples were collected. a. The survival rate analysis in Egr1 fl/fl and Egr1 LKO mice after 750 mg/kg APAP treatment (n = 12 mice/ Egr1 fl/fl group, n = 17 mice/ Egr1 LKO group, Log-rank (Mantel-Cox) test). b. Relative Egr1 mRNA levels in Ad-Egr1 or Ad-GFP pretreated mice (n = 3 mice/group, t test). c. Immunohistochemical staining images of Egr1 in the liver tissue of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice (scale bar = 100 μm), followed by quantified the numbers of Egr1 positive cells per HPF (n = 3 mice/group, one-way ANOVA). Red arrows represent positive staining. d. Western blot analysis of Egr1 levels of total protein in the liver tissues of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice, followed by quantified protein levels (n = 3 mice/group, one-way ANOVA). e. Hepatic GSH levels in Egr1 fl/fl and Egr1 LKO mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test), and in Ad-Egr1 or Ad-GFP pretreated mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test). f. Western blot analysis of CYP2E1 levels in the liver tissues of Egr1 fl/fl and Egr1 LKO mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). g. Western blot analysis of CYP2E1 levels in the liver tissues of Ad-Egr1 and Ad-GFP mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). h. Serum ALT, AST, and LDH levels in Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were measured ( n = 4-5 mice/group, one-way ANOVA). i. Serum CK18-M30 and CK18-M65 levels in Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were measured ( n = 4-5 mice/group, one-way ANOVA). j. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were stained with H&E, followed by quantified the area of hepatocyte necrosis (scale bars = 500 μm, one-way ANOVA). k. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were stained with TUNEL, followed by quantified the numbers of TUNEL positive cells per HFP (scale bars = 500 μm, one-way ANOVA).

    Techniques Used: Over Expression, Injection, Immunohistochemical staining, Staining, Western Blot, TUNEL Assay

    Genome-wide analysis of Egr1 binding sites and analysis of Egr1 induced transcriptomic changes in APAP-injured mouse liver. Mice were treated with saline, 300 mg/kg APAP for 6 h and 12 h APAP, and liver samples were collected for ChIP-seq. Egr1 fl/fl and Egr1 LKO mice were injected with 300 mg/kg APAP for 12 h, and liver samples were collected for RNA-seq. Egr1 LKO mice were pretreated with Ad-Egr1 or Ad-GFP prior to challenge with 300 mg/kg APAP, after 12 h the liver samples were collected for RNA-seq. a. Bar-plot showed genomic distribution of peaks. b. Venn diagram showing the corresponding numbers of Egr1 -bound genes analyzed from ChIP-seq. c. Venn diagram showed the distinct genes that were transcriptionally regulated by Egr1, down-regulated by Egr1 deletion, up-regulated by Egr1 overexpression (fold change ≥ 1.5, P < 0.05, t test). d. Significantly enriched biological process categories in the GO analysis concerning the 161 transcriptionally upregulated genes. e. Heatmaps representing the Z score changes of genes in FAO between Egr1 fl/fl AILI mice and Egr1 LKO AILI mice, and Z score changes of genes in FAO between Ad-Egr1 or Ad-GFP pretreated AILI mice (n = 3 mice/group, fold change ≥ 1.5, P < 0.05, t test). f. Genome-browser screenshots of Acaa2 occupancy at Egr1 gene loci. g. Relative Acaa2 mRNA levels in AML12 cells of Ad-Egr1 or Ad-GFP group after 10mM APAP challenge for 6 h ( t test). h. Relative Acaa2 mRNA levels in Egr1 fl/fl and Egr1 LKO mice of Ad-Egr1 or Ad-GFP group after 300mg/kg APAP challenge for 12 h (n = 4 mice/group, one-way ANOVA).
    Figure Legend Snippet: Genome-wide analysis of Egr1 binding sites and analysis of Egr1 induced transcriptomic changes in APAP-injured mouse liver. Mice were treated with saline, 300 mg/kg APAP for 6 h and 12 h APAP, and liver samples were collected for ChIP-seq. Egr1 fl/fl and Egr1 LKO mice were injected with 300 mg/kg APAP for 12 h, and liver samples were collected for RNA-seq. Egr1 LKO mice were pretreated with Ad-Egr1 or Ad-GFP prior to challenge with 300 mg/kg APAP, after 12 h the liver samples were collected for RNA-seq. a. Bar-plot showed genomic distribution of peaks. b. Venn diagram showing the corresponding numbers of Egr1 -bound genes analyzed from ChIP-seq. c. Venn diagram showed the distinct genes that were transcriptionally regulated by Egr1, down-regulated by Egr1 deletion, up-regulated by Egr1 overexpression (fold change ≥ 1.5, P < 0.05, t test). d. Significantly enriched biological process categories in the GO analysis concerning the 161 transcriptionally upregulated genes. e. Heatmaps representing the Z score changes of genes in FAO between Egr1 fl/fl AILI mice and Egr1 LKO AILI mice, and Z score changes of genes in FAO between Ad-Egr1 or Ad-GFP pretreated AILI mice (n = 3 mice/group, fold change ≥ 1.5, P < 0.05, t test). f. Genome-browser screenshots of Acaa2 occupancy at Egr1 gene loci. g. Relative Acaa2 mRNA levels in AML12 cells of Ad-Egr1 or Ad-GFP group after 10mM APAP challenge for 6 h ( t test). h. Relative Acaa2 mRNA levels in Egr1 fl/fl and Egr1 LKO mice of Ad-Egr1 or Ad-GFP group after 300mg/kg APAP challenge for 12 h (n = 4 mice/group, one-way ANOVA).

    Techniques Used: Genome Wide, Binding Assay, ChIP-sequencing, Injection, RNA Sequencing Assay, Over Expression

    The levels of Egr1 affected mitochondrial function in APAP-injured hepatocytes. a. PMHs were isolated from Egr1 fl/fl and Egr1 LKO mice and then treated with 20 mM APAP for different times. Cell viability was measured by CellTiter-Glo® luminescent cell viability assay ( t test). b. Western blot analysis of CYP2E1 levels in PMHs from Egr1 fl/fl and Egr1 LKO mice treated with 20 mM APAP for different times, followed by quantified protein levels ( t test). c. The ND-1 levels of PMHs treated with different doses of APAP for 12 h in Egr1 fl/fl and Egr1 LKO groups ( t test). d. Cell mito stress OCRs cause by Egr1 deficiency in PMHs were measure by Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction. Red arrows indicated the times when oligomycin, FCCP, and antimycin/rotenone were added to PMHs ( n = 4/group, one-way ANOVA). e. Representative TEM images of PMHs in Egr-1 LKO and Egr-1 fl/fl groups after DMEM (for control) and APAP treatment. Corresponding relative mitochondrial counts and surfaces were analyzed (one-way ANOVA). f. Western blot analysis of CYP2E1 levels in AML12 cells treated with 20 mM APAP at different times, followed by quantified protein levels (one-way ANOVA). g. AML12 cells were treated with Ad-Egr1 or Ad-CON for 48 h and then challenged with 10 mM APAP for 6 h, followed by PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction (n = 4/group, one-way ANOVA). BSA was used as a control for PA-BSA.
    Figure Legend Snippet: The levels of Egr1 affected mitochondrial function in APAP-injured hepatocytes. a. PMHs were isolated from Egr1 fl/fl and Egr1 LKO mice and then treated with 20 mM APAP for different times. Cell viability was measured by CellTiter-Glo® luminescent cell viability assay ( t test). b. Western blot analysis of CYP2E1 levels in PMHs from Egr1 fl/fl and Egr1 LKO mice treated with 20 mM APAP for different times, followed by quantified protein levels ( t test). c. The ND-1 levels of PMHs treated with different doses of APAP for 12 h in Egr1 fl/fl and Egr1 LKO groups ( t test). d. Cell mito stress OCRs cause by Egr1 deficiency in PMHs were measure by Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction. Red arrows indicated the times when oligomycin, FCCP, and antimycin/rotenone were added to PMHs ( n = 4/group, one-way ANOVA). e. Representative TEM images of PMHs in Egr-1 LKO and Egr-1 fl/fl groups after DMEM (for control) and APAP treatment. Corresponding relative mitochondrial counts and surfaces were analyzed (one-way ANOVA). f. Western blot analysis of CYP2E1 levels in AML12 cells treated with 20 mM APAP at different times, followed by quantified protein levels (one-way ANOVA). g. AML12 cells were treated with Ad-Egr1 or Ad-CON for 48 h and then challenged with 10 mM APAP for 6 h, followed by PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction (n = 4/group, one-way ANOVA). BSA was used as a control for PA-BSA.

    Techniques Used: Isolation, Cell Viability Assay, Western Blot

    Egr1 deficiency increased lipid droplets accumulation and FFAs levels in AILI. a. Oil Red O staining of PMHs in Egr1 fl/fl and Egr1 LKO groups after DMEM or 10 mM APAP treatment and the quantification of the ratio relative to the DMEM of Egr1 fl/fl group (one-way ANOVA). b-c. The levels of total fatty acids ( b ) and each fatty acid ( c ) of PMHs in Egr1 fl/fl and Egr1 LKO groups after 10 mM APAP treatment for 12 h determined by GC-MS-based FFA analysis (one-way ANOVA).
    Figure Legend Snippet: Egr1 deficiency increased lipid droplets accumulation and FFAs levels in AILI. a. Oil Red O staining of PMHs in Egr1 fl/fl and Egr1 LKO groups after DMEM or 10 mM APAP treatment and the quantification of the ratio relative to the DMEM of Egr1 fl/fl group (one-way ANOVA). b-c. The levels of total fatty acids ( b ) and each fatty acid ( c ) of PMHs in Egr1 fl/fl and Egr1 LKO groups after 10 mM APAP treatment for 12 h determined by GC-MS-based FFA analysis (one-way ANOVA).

    Techniques Used: Staining, Gas Chromatography-Mass Spectrometry

    Egr1 protect mice and hepatocytes against AILI by transcriptionally up-regulating Acaa2. a. AML12 cells were knocked down of Acaa2 for 24 h, then overexpressed Egr1 for 24 h, finally challenged with 20 mM APAP treatment for 24 h. Cell viability was measured by CCK8 assay (one-way ANOVA). Cell viability of DMEM groups was used as normalization control groups. b. Acaa2 was knocked down in Hepa1-6 cells at 24 h, then overexpressed Egr1 for 48 h and followed by 10 mM APAP treatment for 3 h, finally PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Maximal respiration was calculated according to instruction (n = 5-6/group, one-way ANOVA). BSA was used as a control for PA-BSA. c - j. Mice were knocked down of Acaa2 at 24 h, then overexpressed Egr1 for 48 h via tail vein prior to 300 mg/kg APAP administration. After 6 h, liver and serum samples were collected. (c) Western blot analysis of Acaa2 levels in liver tissues of all groups, followed by quantified protein levels (n=3 mice/group, one-way ANOVA). Serum ALT, AST, LDH ( d ) levels, liver TG ( e ), HE ( f and g ), Oil Red O staining ( h ) and TUNEL staining ( i and j ) in all mice groups (n = 6 mice/group, one-way ANOVA). k. Luciferase activity assay of Acaa2 N-terminal promoter and truncated N-terminal promoters (N-1-5) in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test). l. Luciferase activity assay of WT and mutant N-2 promoters in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test).
    Figure Legend Snippet: Egr1 protect mice and hepatocytes against AILI by transcriptionally up-regulating Acaa2. a. AML12 cells were knocked down of Acaa2 for 24 h, then overexpressed Egr1 for 24 h, finally challenged with 20 mM APAP treatment for 24 h. Cell viability was measured by CCK8 assay (one-way ANOVA). Cell viability of DMEM groups was used as normalization control groups. b. Acaa2 was knocked down in Hepa1-6 cells at 24 h, then overexpressed Egr1 for 48 h and followed by 10 mM APAP treatment for 3 h, finally PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Maximal respiration was calculated according to instruction (n = 5-6/group, one-way ANOVA). BSA was used as a control for PA-BSA. c - j. Mice were knocked down of Acaa2 at 24 h, then overexpressed Egr1 for 48 h via tail vein prior to 300 mg/kg APAP administration. After 6 h, liver and serum samples were collected. (c) Western blot analysis of Acaa2 levels in liver tissues of all groups, followed by quantified protein levels (n=3 mice/group, one-way ANOVA). Serum ALT, AST, LDH ( d ) levels, liver TG ( e ), HE ( f and g ), Oil Red O staining ( h ) and TUNEL staining ( i and j ) in all mice groups (n = 6 mice/group, one-way ANOVA). k. Luciferase activity assay of Acaa2 N-terminal promoter and truncated N-terminal promoters (N-1-5) in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test). l. Luciferase activity assay of WT and mutant N-2 promoters in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test).

    Techniques Used: CCK-8 Assay, Western Blot, Staining, TUNEL Assay, Luciferase, Activity Assay, Mutagenesis

    Levels of EGR1 were increased in the liver and serum samples of patients with DILI. a. Representative EGR1 staining patterns in liver samples from DILI patients and healthy controls (scale bars = 200 μm or 50 μm). EGR1 H-scores in liver samples obtained from 24 patients with DILI and 16 healthy controls ( t test). Red arrows indicated positive staining. b. Distribution of liver histopathologic features and corresponding EGR1 H-scores in patients with DILI ( t test). c. The levels of EGR1 in serum samples from 21 patients with DILI and 17 healthy controls were measured by ELISA ( t test). d. Pearson correlation was performed between serum AST levels in 21 DILI patients and EGR1 serum levels. e. Pearson correlation was performed between latency less than 90 days in 18 DILI patients and EGR1 serum levels. f. Graphical abstract.
    Figure Legend Snippet: Levels of EGR1 were increased in the liver and serum samples of patients with DILI. a. Representative EGR1 staining patterns in liver samples from DILI patients and healthy controls (scale bars = 200 μm or 50 μm). EGR1 H-scores in liver samples obtained from 24 patients with DILI and 16 healthy controls ( t test). Red arrows indicated positive staining. b. Distribution of liver histopathologic features and corresponding EGR1 H-scores in patients with DILI ( t test). c. The levels of EGR1 in serum samples from 21 patients with DILI and 17 healthy controls were measured by ELISA ( t test). d. Pearson correlation was performed between serum AST levels in 21 DILI patients and EGR1 serum levels. e. Pearson correlation was performed between latency less than 90 days in 18 DILI patients and EGR1 serum levels. f. Graphical abstract.

    Techniques Used: Staining, Enzyme-linked Immunosorbent Assay

    speci c primary antibodies anti egr antibody  (Cell Signaling Technology Inc)


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    egr1 primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc egr1 primary antibody
    Oligonucleotides used for generation of <t> EGR1−/− </t> U87MG cells.
    Egr1 Primary Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    1) Product Images from "EGR1 Upregulation during Encephalitic Viral Infections Contributes to Inflammation and Cell Death"

    Article Title: EGR1 Upregulation during Encephalitic Viral Infections Contributes to Inflammation and Cell Death

    Journal: Viruses

    doi: 10.3390/v14061210

    Oligonucleotides used for generation of EGR1−/− U87MG cells.
    Figure Legend Snippet: Oligonucleotides used for generation of EGR1−/− U87MG cells.

    Techniques Used: Sequencing

    Differentially expressed genes consistent with neuronal cell death, inflammation, encephalitis, and/or EGR1 upregulation. Upregulated genes are displayed in shades of red. The darker the shade, the greater the differential gene expression. Genes with a yellow star contain predicted EGR1 binding sites within their promoter.
    Figure Legend Snippet: Differentially expressed genes consistent with neuronal cell death, inflammation, encephalitis, and/or EGR1 upregulation. Upregulated genes are displayed in shades of red. The darker the shade, the greater the differential gene expression. Genes with a yellow star contain predicted EGR1 binding sites within their promoter.

    Techniques Used: Expressing, Binding Assay

    Differentially expressed genes consistent with neuronal cell death, inflammation, encephalitis, and/or EGR1 upregulation.
    Figure Legend Snippet: Differentially expressed genes consistent with neuronal cell death, inflammation, encephalitis, and/or EGR1 upregulation.

    Techniques Used:

    Transcription factors ATF3, FOS, JUN, and KLF4 and inflammatory genes CXCL8, PTGS2, and TNF-α transcription are partially dependent on EGR1 following VEEV infection after knockdown of EGR1 with siRNA. ( A ) U87MG cells were transfected with siNeg or siEGR1 for 48 h prior to infection with VEEV. Knockdown of EGR1 was confirmed via Western blot with β-actin used as the loading control. ( B , C ) U87MG cells were transfected in triplicate with either siNeg or siEGR1 for 48 h and then infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression for transcription factors ( B ) and inflammatory genes ( C ) was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. ## p -Value ≤ 0.01, ### p -Value ≤ 0.001 (comparison between mock siNeg and VEEV siNeg), * p -Value < 0.05, ** p -Value ≤ 0.01, (comparison between VEEV siNeg and VEEV siEGR1), $ p -Value < 0.05, $$ p -Value ≤ 0.01 (comparison between mock siNeg and mock siEGR1).
    Figure Legend Snippet: Transcription factors ATF3, FOS, JUN, and KLF4 and inflammatory genes CXCL8, PTGS2, and TNF-α transcription are partially dependent on EGR1 following VEEV infection after knockdown of EGR1 with siRNA. ( A ) U87MG cells were transfected with siNeg or siEGR1 for 48 h prior to infection with VEEV. Knockdown of EGR1 was confirmed via Western blot with β-actin used as the loading control. ( B , C ) U87MG cells were transfected in triplicate with either siNeg or siEGR1 for 48 h and then infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression for transcription factors ( B ) and inflammatory genes ( C ) was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. ## p -Value ≤ 0.01, ### p -Value ≤ 0.001 (comparison between mock siNeg and VEEV siNeg), * p -Value < 0.05, ** p -Value ≤ 0.01, (comparison between VEEV siNeg and VEEV siEGR1), $ p -Value < 0.05, $$ p -Value ≤ 0.01 (comparison between mock siNeg and mock siEGR1).

    Techniques Used: Infection, Transfection, Western Blot, Expressing, Quantitative RT-PCR

    Increased transcription of transcription factors ATF3, FOS, and JUN, as well as inflammatory genes CXCL3 and CXCL8, are at least partially dependent on EGR1 following VEEV infection in EGR1 knockout U87MG cells. ( A ) U87MG WT or EGR1−/−cells were infected with VEEV TC-83 at an MOI of 5 for 1 h. Lysates were collected at 16h post-infection and Western blot analysis performed for EGR1, VEEV GP, and actin. ( B , C ) U87MG WT or EGR1−/− cells were infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression for transcription factors ( B ) and inflammatory genes ( C ) was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. ### p -Value ≤ 0.001, #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), * p -Value < 0.05, ** p -Value ≤ 0.01, *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1 −/− VEEV), $ p -Value < 0.05, $$$ p -Value ≤ 0.001, $$$$ p -Value ≤ 0.0001 (comparison between WT mock and EGR1−/− mock).
    Figure Legend Snippet: Increased transcription of transcription factors ATF3, FOS, and JUN, as well as inflammatory genes CXCL3 and CXCL8, are at least partially dependent on EGR1 following VEEV infection in EGR1 knockout U87MG cells. ( A ) U87MG WT or EGR1−/−cells were infected with VEEV TC-83 at an MOI of 5 for 1 h. Lysates were collected at 16h post-infection and Western blot analysis performed for EGR1, VEEV GP, and actin. ( B , C ) U87MG WT or EGR1−/− cells were infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression for transcription factors ( B ) and inflammatory genes ( C ) was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. ### p -Value ≤ 0.001, #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), * p -Value < 0.05, ** p -Value ≤ 0.01, *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1 −/− VEEV), $ p -Value < 0.05, $$$ p -Value ≤ 0.001, $$$$ p -Value ≤ 0.0001 (comparison between WT mock and EGR1−/− mock).

    Techniques Used: Infection, Knock-Out, Western Blot, Expressing, Quantitative RT-PCR

    EGR family members are at least partially regulated by EGR1. ( A ) Schematic of EGR family members gene regions. Figure adapted from . ( B ) Alignment of EGR family member DNA binding domains. ( C ) Wildtype or EGR1−/− U87MG cells were infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1−/− VEEV), $$ p -Value ≤ 0.01, $$$ p -Value ≤ 0.001, $$$$ p -Value ≤ 0.0001 (comparison between WT mock and EGR1−/− mock).
    Figure Legend Snippet: EGR family members are at least partially regulated by EGR1. ( A ) Schematic of EGR family members gene regions. Figure adapted from . ( B ) Alignment of EGR family member DNA binding domains. ( C ) Wildtype or EGR1−/− U87MG cells were infected with VEEV TrD at an MOI of 5 for 1 h. RNA was extracted from samples collected at 16 hpi. Gene expression was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1−/− VEEV), $$ p -Value ≤ 0.01, $$$ p -Value ≤ 0.001, $$$$ p -Value ≤ 0.0001 (comparison between WT mock and EGR1−/− mock).

    Techniques Used: Binding Assay, Infection, Expressing, Quantitative RT-PCR

    Viruses utilized to elucidate the influence of EGR1 in other encephalitic viral infections.
    Figure Legend Snippet: Viruses utilized to elucidate the influence of EGR1 in other encephalitic viral infections.

    Techniques Used:

    EGR1 is upregulated in VEEV-, EEEV-, SINV-, CHIKV-, ZIKV-, and RVFV-infected cells. WT U87MG cells were seeded at 1 × 10 5 cells/well. The following day, cells were infected with alphaviruses, including ( A ) VEEV, EEEV, SINV, or CHIKV, ( B ) ZIKV, a flavivirus, or ( C ) RVFV, a phlebovirus, at an MOI of 5 in serum-free media for 1 h. After 1 h incubation, cells were washed 2× with PBS and replenished with fresh serum-free media. Cell lysates were collected 16 hpi and RNA was extracted and normalized to 10 ng/uL. Gene expression was measured using TaqMan assays for EGR1 and 18s. Data were normalized to 18s and mock was set to 1. *—indicates significance as compared to mock, * p -value < 0.05, ** p -value < 0.007, *** p -value < 0.0005, **** p -value < 0.0001.
    Figure Legend Snippet: EGR1 is upregulated in VEEV-, EEEV-, SINV-, CHIKV-, ZIKV-, and RVFV-infected cells. WT U87MG cells were seeded at 1 × 10 5 cells/well. The following day, cells were infected with alphaviruses, including ( A ) VEEV, EEEV, SINV, or CHIKV, ( B ) ZIKV, a flavivirus, or ( C ) RVFV, a phlebovirus, at an MOI of 5 in serum-free media for 1 h. After 1 h incubation, cells were washed 2× with PBS and replenished with fresh serum-free media. Cell lysates were collected 16 hpi and RNA was extracted and normalized to 10 ng/uL. Gene expression was measured using TaqMan assays for EGR1 and 18s. Data were normalized to 18s and mock was set to 1. *—indicates significance as compared to mock, * p -value < 0.05, ** p -value < 0.007, *** p -value < 0.0005, **** p -value < 0.0001.

    Techniques Used: Infection, Incubation, Expressing

    Loss of EGR1 has minimal impact on VEEV, EEEV, CHIKV, SINV, RVFV, and ZIKV viral titers. WT U87MG or EGR1−/− U87MG cells were seeded at 1 × 10 5 cells/well. The following day, cells were infected with either ( A ) VEEV, ( B ) EEEV, ( C ) RVFV, ( D ) SINV, ( E ) CHIKV, or ( F ) ZIKV at an MOI 5 in serum-free media for 1 h. After 1 h incubation, cells were washed 2× with PBS and replenished with fresh serum-free media. At 16 hpi, the supernatant was collected, and viral titers were determined via plaque assay. ** p -value: 0.0011 (VEEV); 0.0082 (SINV).
    Figure Legend Snippet: Loss of EGR1 has minimal impact on VEEV, EEEV, CHIKV, SINV, RVFV, and ZIKV viral titers. WT U87MG or EGR1−/− U87MG cells were seeded at 1 × 10 5 cells/well. The following day, cells were infected with either ( A ) VEEV, ( B ) EEEV, ( C ) RVFV, ( D ) SINV, ( E ) CHIKV, or ( F ) ZIKV at an MOI 5 in serum-free media for 1 h. After 1 h incubation, cells were washed 2× with PBS and replenished with fresh serum-free media. At 16 hpi, the supernatant was collected, and viral titers were determined via plaque assay. ** p -value: 0.0011 (VEEV); 0.0082 (SINV).

    Techniques Used: Infection, Incubation, Plaque Assay

    EGR1-dependent gene expression in EEEV-, SINV-, CHIKV-, ZIKV-, and RVFV-infected cells. WT and EGR1−/− U87MG cells were infected with either mock, ( A ) EEEV, ( B ) SINV, ( C ) CHIKV, ( D ) ZIKV, or ( E ) RVFV at an MOI of 5 for 1 h. RNA was extracted from samples collected 16 hpi. Gene expression for transcription factors and inflammatory genes was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. # p -Value < 0.05, ## p -Value ≤ 0.01, ### p -Value ≤ 0.001, #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), * p -Value < 0.05, ** p -Value ≤ 0.01, *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1−/− VEEV).
    Figure Legend Snippet: EGR1-dependent gene expression in EEEV-, SINV-, CHIKV-, ZIKV-, and RVFV-infected cells. WT and EGR1−/− U87MG cells were infected with either mock, ( A ) EEEV, ( B ) SINV, ( C ) CHIKV, ( D ) ZIKV, or ( E ) RVFV at an MOI of 5 for 1 h. RNA was extracted from samples collected 16 hpi. Gene expression for transcription factors and inflammatory genes was determined by RT-qPCR using TaqMan assays. Data were normalized to mock-infected cells and 18S RNA by the ∆∆CT method. # p -Value < 0.05, ## p -Value ≤ 0.01, ### p -Value ≤ 0.001, #### p -Value ≤ 0.0001 (comparison between WT mock and WT VEEV), * p -Value < 0.05, ** p -Value ≤ 0.01, *** p -Value ≤ 0.001, **** p -Value ≤ 0.0001 (comparison between WT VEEV and EGR1−/− VEEV).

    Techniques Used: Expressing, Infection, Quantitative RT-PCR

    EGR1 may work directly or indirectly with target genes to induce transcription of inflammatory cytokines and chemokines and apoptotic transcriptional machinery. ( A ) Overview of proposed direct mechanism of action. Susceptible cells become virally infected, resulting in EGR1 activation and translocation to the nucleus. Once in the nucleus, EGR1 binds directly to promoters of target genes and induces their transcription, thereby contributing to inflammation and cell death associated with viral infection. ( B ) Overview of proposed indirect mechanism of action. Susceptible cells become virally infected, resulting in EGR1 activation and translocation to the nucleus. Once in the nucleus, EGR1 binds to target genes, such as transcription factor x, resulting in their upregulation. Transcription factor(s) X then binds to promoter regions of inflammatory genes and apoptotic machinery, inducing their transcription and subsequent release of inflammatory cytokines and chemokines, ultimately contributing to neuronal cell death within the brain. Figures were created with BioRender.com.
    Figure Legend Snippet: EGR1 may work directly or indirectly with target genes to induce transcription of inflammatory cytokines and chemokines and apoptotic transcriptional machinery. ( A ) Overview of proposed direct mechanism of action. Susceptible cells become virally infected, resulting in EGR1 activation and translocation to the nucleus. Once in the nucleus, EGR1 binds directly to promoters of target genes and induces their transcription, thereby contributing to inflammation and cell death associated with viral infection. ( B ) Overview of proposed indirect mechanism of action. Susceptible cells become virally infected, resulting in EGR1 activation and translocation to the nucleus. Once in the nucleus, EGR1 binds to target genes, such as transcription factor x, resulting in their upregulation. Transcription factor(s) X then binds to promoter regions of inflammatory genes and apoptotic machinery, inducing their transcription and subsequent release of inflammatory cytokines and chemokines, ultimately contributing to neuronal cell death within the brain. Figures were created with BioRender.com.

    Techniques Used: Infection, Activation Assay, Translocation Assay

    egr 1 rabbit primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc egr 1 rabbit primary antibody
    KORD-mediated inactivation decreased <t>EGR-1</t> expression in RE. (A) Schematic of SALB injection, object training, and tissue collection. Panel created using BioRender.com . (B) Representative area of EGR-1 quantification . (C) Representative EGR-1 expression (red) against DAPI (blue) in RE in Control and KORD groups, 20x magnification. (D) Treatment with SALB 10 min prior to training decreased EGR-1 expression.
    Egr 1 Rabbit Primary Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Chemogenetic inactivation of the nucleus reuniens impairs object placement memory in female mice"

    Article Title: Chemogenetic inactivation of the nucleus reuniens impairs object placement memory in female mice

    Journal: Neurobiology of learning and memory

    doi: 10.1016/j.nlm.2021.107521

    KORD-mediated inactivation decreased EGR-1 expression in RE. (A) Schematic of SALB injection, object training, and tissue collection. Panel created using BioRender.com . (B) Representative area of EGR-1 quantification . (C) Representative EGR-1 expression (red) against DAPI (blue) in RE in Control and KORD groups, 20x magnification. (D) Treatment with SALB 10 min prior to training decreased EGR-1 expression.
    Figure Legend Snippet: KORD-mediated inactivation decreased EGR-1 expression in RE. (A) Schematic of SALB injection, object training, and tissue collection. Panel created using BioRender.com . (B) Representative area of EGR-1 quantification . (C) Representative EGR-1 expression (red) against DAPI (blue) in RE in Control and KORD groups, 20x magnification. (D) Treatment with SALB 10 min prior to training decreased EGR-1 expression.

    Techniques Used: Expressing, Injection

    egr1 primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc egr1 primary antibody
    <t>Transcription</t> <t>factor</t> <t>EGR1</t> is required for SAHH inhibition-induced TXNIP expression . (A) Podocytes were incubated with ADA (20 μmol/L) for 24 h. The enrichment of H3K27me3 at TXNIP promoter in podocytes was assayed by chromatin immunoprecipitation (ChIP). (B) ChIP sequencing showed the enrichment of H3K27me3 at EGR1 promoter were decreased in ADA-treated mice compared with control. (C) Protein expression of EGR1 was assayed by Western blot in podocytes. (D) Representative immunofluorescence images and quantitation of H3K27me3 and EGR1 expression in podocytes. Scale bar, 2 μm. (E) The protein expression of H3K27me3 and EGR1 were assayed by Western blot in kidney tissues. (F) The enrichment of EGR1 at TXNIP promoter was assayed by ChIP in podocytes. (G) The motif of EGR1 from JASPAR database was used to predict the binding sites on TXNIP promoter. The luciferase activity of TXNIP promoter was measured by a reporter assay system. (H) The protein and mRNA expression of TXNIP and its promoter activity were measured in podocytes treated by ADA with or without EGR1 siRNA transfection. Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P < 0.05 vs. control; # P < 0.05 vs.ADA (determined by one-way ANOVA or unpaired Student's t -test).
    Egr1 Primary Antibody, supplied by Cell Signaling Technology Inc, 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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    1) Product Images from "Epigenetic regulation of TXNIP-mediated oxidative stress and NLRP3 inflammasome activation contributes to SAHH inhibition-aggravated diabetic nephropathy"

    Article Title: Epigenetic regulation of TXNIP-mediated oxidative stress and NLRP3 inflammasome activation contributes to SAHH inhibition-aggravated diabetic nephropathy

    Journal: Redox Biology

    doi: 10.1016/j.redox.2021.102033

    Transcription factor EGR1 is required for SAHH inhibition-induced TXNIP expression . (A) Podocytes were incubated with ADA (20 μmol/L) for 24 h. The enrichment of H3K27me3 at TXNIP promoter in podocytes was assayed by chromatin immunoprecipitation (ChIP). (B) ChIP sequencing showed the enrichment of H3K27me3 at EGR1 promoter were decreased in ADA-treated mice compared with control. (C) Protein expression of EGR1 was assayed by Western blot in podocytes. (D) Representative immunofluorescence images and quantitation of H3K27me3 and EGR1 expression in podocytes. Scale bar, 2 μm. (E) The protein expression of H3K27me3 and EGR1 were assayed by Western blot in kidney tissues. (F) The enrichment of EGR1 at TXNIP promoter was assayed by ChIP in podocytes. (G) The motif of EGR1 from JASPAR database was used to predict the binding sites on TXNIP promoter. The luciferase activity of TXNIP promoter was measured by a reporter assay system. (H) The protein and mRNA expression of TXNIP and its promoter activity were measured in podocytes treated by ADA with or without EGR1 siRNA transfection. Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P < 0.05 vs. control; # P < 0.05 vs.ADA (determined by one-way ANOVA or unpaired Student's t -test).
    Figure Legend Snippet: Transcription factor EGR1 is required for SAHH inhibition-induced TXNIP expression . (A) Podocytes were incubated with ADA (20 μmol/L) for 24 h. The enrichment of H3K27me3 at TXNIP promoter in podocytes was assayed by chromatin immunoprecipitation (ChIP). (B) ChIP sequencing showed the enrichment of H3K27me3 at EGR1 promoter were decreased in ADA-treated mice compared with control. (C) Protein expression of EGR1 was assayed by Western blot in podocytes. (D) Representative immunofluorescence images and quantitation of H3K27me3 and EGR1 expression in podocytes. Scale bar, 2 μm. (E) The protein expression of H3K27me3 and EGR1 were assayed by Western blot in kidney tissues. (F) The enrichment of EGR1 at TXNIP promoter was assayed by ChIP in podocytes. (G) The motif of EGR1 from JASPAR database was used to predict the binding sites on TXNIP promoter. The luciferase activity of TXNIP promoter was measured by a reporter assay system. (H) The protein and mRNA expression of TXNIP and its promoter activity were measured in podocytes treated by ADA with or without EGR1 siRNA transfection. Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P < 0.05 vs. control; # P < 0.05 vs.ADA (determined by one-way ANOVA or unpaired Student's t -test).

    Techniques Used: Inhibition, Expressing, Incubation, Chromatin Immunoprecipitation, ChIP-sequencing, Western Blot, Immunofluorescence, Quantitation Assay, Binding Assay, Luciferase, Activity Assay, Reporter Assay, Transfection, In Vitro, In Vivo

    Knockdown of EGR1 alleviates SAHH inhibition-increased inflammation and diabetic nephropathy . (A) The basic characteristics of C57BL/6 mice injected with ADA in the presence or absence of tail vein injection of EGR1 shRNA, (B) Representative images and quantitation of PAS staining, TEM examination, WT1, F-actin, and Masson staining, (C) The levels of caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (D) Urine albumin and creatinine was measured using commercial kits. (E) Urinary levels of 8-OHdG were measured by an ELISA kit. (F) Protein expression of EGR1, TXNIP, and NLRP3 was assayed by Western blot. Values are mean ± SEM; n = 6–8, * P < 0.05 vs. control; # P < 0.05 vs. scrambled shRNA (determined by one-way ANOVA).
    Figure Legend Snippet: Knockdown of EGR1 alleviates SAHH inhibition-increased inflammation and diabetic nephropathy . (A) The basic characteristics of C57BL/6 mice injected with ADA in the presence or absence of tail vein injection of EGR1 shRNA, (B) Representative images and quantitation of PAS staining, TEM examination, WT1, F-actin, and Masson staining, (C) The levels of caspase-1 activity and IL-1β production in kidney tissues was measured by commercial kits. (D) Urine albumin and creatinine was measured using commercial kits. (E) Urinary levels of 8-OHdG were measured by an ELISA kit. (F) Protein expression of EGR1, TXNIP, and NLRP3 was assayed by Western blot. Values are mean ± SEM; n = 6–8, * P < 0.05 vs. control; # P < 0.05 vs. scrambled shRNA (determined by one-way ANOVA).

    Techniques Used: Inhibition, Injection, shRNA, Quantitation Assay, Staining, Activity Assay, Enzyme-linked Immunosorbent Assay, Expressing, Western Blot

    Knockdown of SAHH increases oxidative stress and inflammation and diabetic nephropathy . (A) The basic characteristics and plasma methionine metabolites levels of SAHH -/- and wild type mice, (B–C) Representative images and quantitation of SAHH immunofluorescence staining, PAS staining, TEM examination, WT1, F-actin, and Masson staining, (D) The levels of caspase-1 activity and IL-1β production, urine albumin and creatinine, and urinary levels of 8-OHdG was measured by commercial kits. (E) Representative images and quantitation of F-actin staining and ROS levels in podocytes treated with SAHH shRNA. (F) Protein expression of SAHH, EZH2, EGR1, TXNIP, and NLRP3 was assayed by Western blot in vitro and in vivo . Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P < 0.05 vs. WT (determined by unpaired Student's t -test).
    Figure Legend Snippet: Knockdown of SAHH increases oxidative stress and inflammation and diabetic nephropathy . (A) The basic characteristics and plasma methionine metabolites levels of SAHH -/- and wild type mice, (B–C) Representative images and quantitation of SAHH immunofluorescence staining, PAS staining, TEM examination, WT1, F-actin, and Masson staining, (D) The levels of caspase-1 activity and IL-1β production, urine albumin and creatinine, and urinary levels of 8-OHdG was measured by commercial kits. (E) Representative images and quantitation of F-actin staining and ROS levels in podocytes treated with SAHH shRNA. (F) Protein expression of SAHH, EZH2, EGR1, TXNIP, and NLRP3 was assayed by Western blot in vitro and in vivo . Values are mean ± SEM; n = 3 for in vitro , 6–8 for in vivo assays, * P < 0.05 vs. WT (determined by unpaired Student's t -test).

    Techniques Used: Quantitation Assay, Immunofluorescence, Staining, Activity Assay, shRNA, Expressing, Western Blot, In Vitro, In Vivo

    rabbit monoclonal primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal primary antibody
    Rabbit Monoclonal Primary Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    primary antibodies against egr1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc primary antibodies against egr1
    Characterization of the Yangyinjiedu (YYJD) induced differential gene expression in lung cancer cells. A, Scatter plot showed the differential gene expression pattern in A549 with YYJD treatment or with no YYJD treatment. Expression was shown as log10 of the FPKM+1, including up‐regulated (red) and down‐regulated (green) genes. B, Gene ontology analysis of the significantly differentially expressed genes in YYJD‐treated A549. C, Heatmap showed the 50 most up‐regulated and down‐regulated in YYJD‐treated A549. D, The alteration in early growth response 1 protein levels in YYJD‐treated lung cancer cell lines was examined by Western blot
    Primary Antibodies Against Egr1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Herbal formula Yangyinjiedu induces lung cancer cell apoptosis via activation of early growth response 1"

    Article Title: Herbal formula Yangyinjiedu induces lung cancer cell apoptosis via activation of early growth response 1

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.14501

    Characterization of the Yangyinjiedu (YYJD) induced differential gene expression in lung cancer cells. A, Scatter plot showed the differential gene expression pattern in A549 with YYJD treatment or with no YYJD treatment. Expression was shown as log10 of the FPKM+1, including up‐regulated (red) and down‐regulated (green) genes. B, Gene ontology analysis of the significantly differentially expressed genes in YYJD‐treated A549. C, Heatmap showed the 50 most up‐regulated and down‐regulated in YYJD‐treated A549. D, The alteration in early growth response 1 protein levels in YYJD‐treated lung cancer cell lines was examined by Western blot
    Figure Legend Snippet: Characterization of the Yangyinjiedu (YYJD) induced differential gene expression in lung cancer cells. A, Scatter plot showed the differential gene expression pattern in A549 with YYJD treatment or with no YYJD treatment. Expression was shown as log10 of the FPKM+1, including up‐regulated (red) and down‐regulated (green) genes. B, Gene ontology analysis of the significantly differentially expressed genes in YYJD‐treated A549. C, Heatmap showed the 50 most up‐regulated and down‐regulated in YYJD‐treated A549. D, The alteration in early growth response 1 protein levels in YYJD‐treated lung cancer cell lines was examined by Western blot

    Techniques Used: Expressing, Western Blot

    Knockdown of early growth response 1 (EGR1) attenuated the Yangyinjiedu induced pro‐apoptosis effect in A549. A, The expression levels of EGR1 mRNA were detected by quantitative real‐time PCR. B, The expression levels of EGR1 protein were measured by Western blot. C, Cell viabilities were examined by CCK8 assay. D, Apoptotic cells were measured by flow cytometric assay. Ratios of early apoptosis and total apoptosis were analysed with flowjo software (** P < 0.01, *** P < 0.001 compared with control group)
    Figure Legend Snippet: Knockdown of early growth response 1 (EGR1) attenuated the Yangyinjiedu induced pro‐apoptosis effect in A549. A, The expression levels of EGR1 mRNA were detected by quantitative real‐time PCR. B, The expression levels of EGR1 protein were measured by Western blot. C, Cell viabilities were examined by CCK8 assay. D, Apoptotic cells were measured by flow cytometric assay. Ratios of early apoptosis and total apoptosis were analysed with flowjo software (** P < 0.01, *** P < 0.001 compared with control group)

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, CCK-8 Assay, Flow Cytometry, Software

    Characterization of early growth response 1 (EGR1) directed transcriptional network in A549. A, A snapshot of the IGV genome browser showed the sequencing read signals of EGR1 binding sites. B, Genomic distribution of EGR1 binding sites across the Yangyinjiedu (YYJD) treated A549 genome. C, Venn diagram of differentially expressed genes and EGR1‐bound genes in YYJD‐treated A549. D, Gene ontology analysis of the up‐regulated EGR1 target genes ( P < 0.05)
    Figure Legend Snippet: Characterization of early growth response 1 (EGR1) directed transcriptional network in A549. A, A snapshot of the IGV genome browser showed the sequencing read signals of EGR1 binding sites. B, Genomic distribution of EGR1 binding sites across the Yangyinjiedu (YYJD) treated A549 genome. C, Venn diagram of differentially expressed genes and EGR1‐bound genes in YYJD‐treated A549. D, Gene ontology analysis of the up‐regulated EGR1 target genes ( P < 0.05)

    Techniques Used: Sequencing, Binding Assay

    Tumour inhibitory effect of Yangyinjiedu in vivo. A, The tumour volumes were measured once every day. * P < 0.05, ** P < 0.01 and *** P < 0.001. B, The comparison of tumour weights of four groups. * P < 0.05, ** P < 0.01 and *** P < 0.001. C, Haematoxylin eosin staining of the tumour tissues (100× and 400× magnification). Representative images were shown from six mice in each group. D, The expression of early growth response 1 and KLF11 in tumour xenograft tissues was detected by immunohistochemistry (400×). Scale bars: 200 μm
    Figure Legend Snippet: Tumour inhibitory effect of Yangyinjiedu in vivo. A, The tumour volumes were measured once every day. * P < 0.05, ** P < 0.01 and *** P < 0.001. B, The comparison of tumour weights of four groups. * P < 0.05, ** P < 0.01 and *** P < 0.001. C, Haematoxylin eosin staining of the tumour tissues (100× and 400× magnification). Representative images were shown from six mice in each group. D, The expression of early growth response 1 and KLF11 in tumour xenograft tissues was detected by immunohistochemistry (400×). Scale bars: 200 μm

    Techniques Used: In Vivo, Staining, Expressing, Immunohistochemistry

    primary anti egr-1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc primary anti egr-1
    Primary Anti Egr 1, 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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    egr1 primary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc egr1 primary antibody
    (A) Representative photomicrograph of <t>EGR1</t> staining in the NAc, (B) areas quantified in the NAc, (C) areas quantified in the anterior BNST, and (D) areas quantified in the posterior BNST. LV = lateral ventricle, ac = anterior commissure, core = NAc core, ShD = dorsal shell of NAc, ShV = ventral shell of NAc, BNSTam = anterior medial BNST, BNSTal = anterior lateral BNST, BNSTdl = dorsal lateral BNST, BNSTdm = dorsal medial BNST, BNSTvl = ventral lateral BNST, BNSTvm = ventral medial BNST, f = fornix. Scale bars = 200 μm.
    Egr1 Primary Antibody, 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 "The long-term effects of stress and kappa opioid receptor activation on conditioned place aversion in male and female California mice"

    Article Title: The long-term effects of stress and kappa opioid receptor activation on conditioned place aversion in male and female California mice

    Journal: Behavioural brain research

    doi: 10.1016/j.bbr.2017.06.015

    (A) Representative photomicrograph of EGR1 staining in the NAc, (B) areas quantified in the NAc, (C) areas quantified in the anterior BNST, and (D) areas quantified in the posterior BNST. LV = lateral ventricle, ac = anterior commissure, core = NAc core, ShD = dorsal shell of NAc, ShV = ventral shell of NAc, BNSTam = anterior medial BNST, BNSTal = anterior lateral BNST, BNSTdl = dorsal lateral BNST, BNSTdm = dorsal medial BNST, BNSTvl = ventral lateral BNST, BNSTvm = ventral medial BNST, f = fornix. Scale bars = 200 μm.
    Figure Legend Snippet: (A) Representative photomicrograph of EGR1 staining in the NAc, (B) areas quantified in the NAc, (C) areas quantified in the anterior BNST, and (D) areas quantified in the posterior BNST. LV = lateral ventricle, ac = anterior commissure, core = NAc core, ShD = dorsal shell of NAc, ShV = ventral shell of NAc, BNSTam = anterior medial BNST, BNSTal = anterior lateral BNST, BNSTdl = dorsal lateral BNST, BNSTdm = dorsal medial BNST, BNSTvl = ventral lateral BNST, BNSTvm = ventral medial BNST, f = fornix. Scale bars = 200 μm.

    Techniques Used: Staining

    Cell counts for EGR1 in the NAc. * p < 0.05, ** p < 0.01, † p < 0.05 vs. vehicle treated animals of same stress group, n=5-9 per group.
    Figure Legend Snippet: Cell counts for EGR1 in the NAc. * p < 0.05, ** p < 0.01, † p < 0.05 vs. vehicle treated animals of same stress group, n=5-9 per group.

    Techniques Used:

    3.2. Effects of U50,488 on EGR1 immunoreactivity in the nucleus accumbens and the bed nucleus of the stria terminalis
    Figure Legend Snippet: 3.2. Effects of U50,488 on EGR1 immunoreactivity in the nucleus accumbens and the bed nucleus of the stria terminalis

    Techniques Used:

    3.3. Correlations between place aversion behavior and EGR1 immunoreactivity
    Figure Legend Snippet: 3.3. Correlations between place aversion behavior and EGR1 immunoreactivity

    Techniques Used:

    Correlations between aversion score (post-test minus pre-test) and EGR1 counts in the NAc for (A) control females treated with vehicle (Spearman's ρ= .964, FDR adjusted p<.001), (B) control females treated with 2.5 mg/kg U50,488 (Spearman's ρ= -.943, FDR adjusted p=.045), n=6-7 per group.
    Figure Legend Snippet: Correlations between aversion score (post-test minus pre-test) and EGR1 counts in the NAc for (A) control females treated with vehicle (Spearman's ρ= .964, FDR adjusted p<.001), (B) control females treated with 2.5 mg/kg U50,488 (Spearman's ρ= -.943, FDR adjusted p=.045), n=6-7 per group.

    Techniques Used:

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    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and <t>Egr1</t> protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.
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    <t>Egr1</t> was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).
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    <t>Egr1</t> was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).
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    A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.

    Journal: PLoS ONE

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    doi: 10.1371/journal.pone.0116825

    Figure Lengend Snippet: A. WT1 mRNA (+KTS and –KTS) splice variant PCR products expressed in LβT2 cells. Whole cell RNA was extracted from LβT2 cells, reverse transcribed to cDNA and quantified by real-time PCR, using specific primers to detect +KTS and –KTS splice variants, then displayed on a 1% agarose gel. Bands corresponding to the products for +KTS (301bp) and –KTS (292 bp) WT1 were detected in 4 independent samples of mRNA. B. WT1 and Egr1 protein expression in LβT2 cells. Cell proteins (30μg) were separated on 10% polyacrylamide-SDS gels, then analyzed by immunoblotting with specific antibodies for WT1, Egr1 and β-actin. Specific proteins were detected in the same samples of untreated LβT2 cells. C. Chromatin association of WT1 with the endogenous LHβ promoter in LβT2 cells. The association of WT1 and RNA Polymerase II with the LHβ promoter in untreated LβT2 cells was measured by Chromatin immunoprecipitation assays with antibodies against WT1 and phosphorylated RNApol II, as well as control (no Antibody). LHβ promoter occupancy was measured by quantitative real time PCR using primers specific for the LHβ promoter, and normalized for chromatin input in each sample. In this study, background binding (no Antibody) was set at 100% and association of RNA Polymerase II and WT1 are expressed relative to background values. Association was measured in 3 independent experiments with duplicate samples.

    Article Snippet: Membranes were then incubated with a WT1 primary antibody (C-19:SC-192 Santa Cruz Biotechnologies, Santa Cruz CA) overnight (1:500) or Egr1 primary antibody (Cell Signaling Technology) overnight (1:1000) at 4C followed by three 5 min washes with TBST and another incubation with secondary antibody, horseradish peroxidase-conjugated donkey anti-rabbit Fab fragment IgG (1:5000;GE HealthCare; Piscataway, New Jersey) for 2h.

    Techniques: Variant Assay, Real-time Polymerase Chain Reaction, Agarose Gel Electrophoresis, Expressing, Western Blot, Chromatin Immunoprecipitation, Binding Assay

    A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.

    Journal: PLoS ONE

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    doi: 10.1371/journal.pone.0116825

    Figure Lengend Snippet: A. WT1 (-KTS) and (+ KTS) mRNA variant levels in LβT2 cells treated with 50nM GnRH for 90min. RNA was extracted and mRNAs levels measured by RT-PCR and normalized against GAPDH mRNA. Values for WT1 mRNAs are shown for both Reverse Transcriptase (RT) and no RT (negative control) conditions. Note that for no RT, the Y axis is interrupted and expanded to show the low values. Data is the mean ± SEM from 5–7 experiments. * = P<0.05, -GnRH vs +GnRH; ** = P<0.001, -GnRH vs +GnRH B. WT1 and Egr1 protein levels in LβT2 cells treated with 50nM GnRH for 0 to 3.5 h. The experiment was performed three times. Upper panel: Cells were lysed after GnRH treatment and proteins (30μg) were separated by 10% SDS-PAGE, then detected with antibodies against WT1 or Egr1. Immunoblotting for β-actin was performed on the same blots as WT1 and Egr1, and used for normalization of these proteins quantified by densitometry analysis. A representative blot is shown. Lower panel: Quantification of protein bands was performed with densitometry, and normalized protein levels are shown from combined experiments. Bands for Egr1 proteins were not detected (ND) in any blot at time zero without GnRH.

    Article Snippet: Membranes were then incubated with a WT1 primary antibody (C-19:SC-192 Santa Cruz Biotechnologies, Santa Cruz CA) overnight (1:500) or Egr1 primary antibody (Cell Signaling Technology) overnight (1:1000) at 4C followed by three 5 min washes with TBST and another incubation with secondary antibody, horseradish peroxidase-conjugated donkey anti-rabbit Fab fragment IgG (1:5000;GE HealthCare; Piscataway, New Jersey) for 2h.

    Techniques: Variant Assay, Reverse Transcription Polymerase Chain Reaction, Negative Control, SDS Page, Western Blot

    LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.

    Journal: PLoS ONE

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    doi: 10.1371/journal.pone.0116825

    Figure Lengend Snippet: LβT2 cells were incubated with or without 50 nM GnRH and collected every 10 min for 120 min. ChIP assays were performed using antibody against WT1, Egr1 and phosphorylated pRNA Pol II. LHβ promoter occupancy was measured by quantitative real time PCR using primers for the LHβ promoter. The experiment was performed three times with duplicate samples and replicate PCR measurements in each sample. Data are presented as the mean + SEM and expressed as LHβ promoter occupancy relative to basal (no GnRH at time zero) binding.

    Article Snippet: Membranes were then incubated with a WT1 primary antibody (C-19:SC-192 Santa Cruz Biotechnologies, Santa Cruz CA) overnight (1:500) or Egr1 primary antibody (Cell Signaling Technology) overnight (1:1000) at 4C followed by three 5 min washes with TBST and another incubation with secondary antibody, horseradish peroxidase-conjugated donkey anti-rabbit Fab fragment IgG (1:5000;GE HealthCare; Piscataway, New Jersey) for 2h.

    Techniques: Incubation, Real-time Polymerase Chain Reaction, Binding Assay

    LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.

    Journal: PLoS ONE

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    doi: 10.1371/journal.pone.0116825

    Figure Lengend Snippet: LβT2 cells were transfected with siRNA against WT1 and a non-targeting siRNA as a control. After 72 h of incubation, cells were treated with or without GnRH for 1.5 h, followed by cell lysate collection, RNA extraction and western blot analysis (30 μg protein) on 10% PAGE-SDS gels. WT1 protein was detected by immunoblotting with specific antibodies for WT1, and normalized for β-actin on the same blot. A. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where the WT1 (-KTS) variant mRNA was reduced. B. Expression of the endogenous LHβ primary transcript, Egr1 primary transcript mRNA, and WT1 protein under conditions where both the WT1 (-KTS) and WT1 (+KTS) variant mRNAs were reduced. For each condition, the experiment was performed twice with 5 replicates. LHβ and Egr1 primary transcript mRNAs were normalized for GAPDH mRNA in the same sample. Control samples contained non-targeting siRNA. * p<.05 -GnRH vs +GnRH, in either Control siRNA or WT1 siRNA treatments. Values are mean ± SEM for 5 replicates. # = p<.05 -GnRH Control siRNA vs –GnRH WT1 siRNA, or p<.05+GnRH Control siRNA vs +GnRH WT1 siRNA.

    Article Snippet: Membranes were then incubated with a WT1 primary antibody (C-19:SC-192 Santa Cruz Biotechnologies, Santa Cruz CA) overnight (1:500) or Egr1 primary antibody (Cell Signaling Technology) overnight (1:1000) at 4C followed by three 5 min washes with TBST and another incubation with secondary antibody, horseradish peroxidase-conjugated donkey anti-rabbit Fab fragment IgG (1:5000;GE HealthCare; Piscataway, New Jersey) for 2h.

    Techniques: Transfection, Incubation, RNA Extraction, Western Blot, Expressing, Variant Assay

    WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.

    Journal: PLoS ONE

    Article Title: A New Role for Wilms Tumor Protein 1: Differential Activities of + KTS and –KTS Variants to Regulate LHβ Transcription

    doi: 10.1371/journal.pone.0116825

    Figure Lengend Snippet: WT1 (-KTS) may associate directly with the 3’Egr1 site of the LHβ promoter to stimulate basal promoter activity, but in the presence of GnRH stimulates Egr1 expression. Egr1 then binds to both the 3’- and 5’-Egr1 sites on the promoter and further increases LHβ transcription. WT1 (+KTS) may associate with the 3’-Egr1 site, but also requires the SF1 site for biological activity. Decreased expression of WT1 (+KTS) would stimulate basal LHβ expression as the suppressor is reduced. The isoforms likely compete for association to the LHβ promoter at the same sites.

    Article Snippet: Membranes were then incubated with a WT1 primary antibody (C-19:SC-192 Santa Cruz Biotechnologies, Santa Cruz CA) overnight (1:500) or Egr1 primary antibody (Cell Signaling Technology) overnight (1:1000) at 4C followed by three 5 min washes with TBST and another incubation with secondary antibody, horseradish peroxidase-conjugated donkey anti-rabbit Fab fragment IgG (1:5000;GE HealthCare; Piscataway, New Jersey) for 2h.

    Techniques: Activity Assay, Expressing

    Egr1 was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Egr1 was significantly upregulated in acute AILI models. a. Volcano plots of transcriptional factors from liver tissue RNA sequencing data of saline group, 3 h AILI group and 6 h AILI group ( P < 0.05, n = 3 mice/group, t test). b. Relative Egr1 mRNA levels of liver tissue in saline and APAP groups at 1, 3, 6, and 12 h (n = 6 mice/group, t test). c. Western blot analysis of Egr1 levels of cytoplasmic and nuclear protein in the liver tissue of saline and APAP groups at 1, 3, 6, and 12 h, followed by quantified protein levels (one-way ANOVA). d. Immunohistochemical staining images of Egr1 in the liver tissue of saline group and 300 mg/kg APAP groups at 12h (scale bar = 250 μm). Black arrows represent positive staining. e. Relative Egr1 mRNA levels of PMHs treated with different doses of APAP (one-way ANOVA). f. Relative Egr1 mRNA levels of PMHs treated with DMEM and 10 mM APAP at different time points ( t test). g. Representative images of Egr1 fluorescence in PMHs treated with 10 mM APAP for 0, 3, 6, and 12 h (scale bar = 200 μm), followed by quantified the numbers of Egr1 positive cells per high-power field (HPF) (one-way ANOVA).

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: RNA Sequencing Assay, Western Blot, Immunohistochemical staining, Staining, Fluorescence

    Egr1 overexpression ameliorated acute AILI. Egr1 fl/fl and Egr1 LKO mice were injected with Ad-Egr1 or Ad-GFP via tail vein prior to 300 mg/kg APAP administration. After 12 h, liver and serum samples were collected. a. The survival rate analysis in Egr1 fl/fl and Egr1 LKO mice after 750 mg/kg APAP treatment (n = 12 mice/ Egr1 fl/fl group, n = 17 mice/ Egr1 LKO group, Log-rank (Mantel-Cox) test). b. Relative Egr1 mRNA levels in Ad-Egr1 or Ad-GFP pretreated mice (n = 3 mice/group, t test). c. Immunohistochemical staining images of Egr1 in the liver tissue of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice (scale bar = 100 μm), followed by quantified the numbers of Egr1 positive cells per HPF (n = 3 mice/group, one-way ANOVA). Red arrows represent positive staining. d. Western blot analysis of Egr1 levels of total protein in the liver tissues of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice, followed by quantified protein levels (n = 3 mice/group, one-way ANOVA). e. Hepatic GSH levels in Egr1 fl/fl and Egr1 LKO mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test), and in Ad-Egr1 or Ad-GFP pretreated mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test). f. Western blot analysis of CYP2E1 levels in the liver tissues of Egr1 fl/fl and Egr1 LKO mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). g. Western blot analysis of CYP2E1 levels in the liver tissues of Ad-Egr1 and Ad-GFP mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). h. Serum ALT, AST, and LDH levels in Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were measured ( n = 4-5 mice/group, one-way ANOVA). i. Serum CK18-M30 and CK18-M65 levels in Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were measured ( n = 4-5 mice/group, one-way ANOVA). j. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were stained with H&E, followed by quantified the area of hepatocyte necrosis (scale bars = 500 μm, one-way ANOVA). k. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were stained with TUNEL, followed by quantified the numbers of TUNEL positive cells per HFP (scale bars = 500 μm, one-way ANOVA).

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Egr1 overexpression ameliorated acute AILI. Egr1 fl/fl and Egr1 LKO mice were injected with Ad-Egr1 or Ad-GFP via tail vein prior to 300 mg/kg APAP administration. After 12 h, liver and serum samples were collected. a. The survival rate analysis in Egr1 fl/fl and Egr1 LKO mice after 750 mg/kg APAP treatment (n = 12 mice/ Egr1 fl/fl group, n = 17 mice/ Egr1 LKO group, Log-rank (Mantel-Cox) test). b. Relative Egr1 mRNA levels in Ad-Egr1 or Ad-GFP pretreated mice (n = 3 mice/group, t test). c. Immunohistochemical staining images of Egr1 in the liver tissue of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice (scale bar = 100 μm), followed by quantified the numbers of Egr1 positive cells per HPF (n = 3 mice/group, one-way ANOVA). Red arrows represent positive staining. d. Western blot analysis of Egr1 levels of total protein in the liver tissues of Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice, followed by quantified protein levels (n = 3 mice/group, one-way ANOVA). e. Hepatic GSH levels in Egr1 fl/fl and Egr1 LKO mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test), and in Ad-Egr1 or Ad-GFP pretreated mice after challenge with saline and APAP for 2 h (n = 5 mice/group, t test). f. Western blot analysis of CYP2E1 levels in the liver tissues of Egr1 fl/fl and Egr1 LKO mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). g. Western blot analysis of CYP2E1 levels in the liver tissues of Ad-Egr1 and Ad-GFP mice after injection with saline for 2 h, followed by quantified protein levels (n = 5 mice/group, t test). h. Serum ALT, AST, and LDH levels in Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were measured ( n = 4-5 mice/group, one-way ANOVA). i. Serum CK18-M30 and CK18-M65 levels in Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were measured ( n = 4-5 mice/group, one-way ANOVA). j. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated Egr1 fl/fl and Egr1 LKO AILI mice were stained with H&E, followed by quantified the area of hepatocyte necrosis (scale bars = 500 μm, one-way ANOVA). k. Liver sample obtained from Ad-Egr1 or Ad-GFP pretreated AILI Egr1 fl/fl and Egr1 LKO mice were stained with TUNEL, followed by quantified the numbers of TUNEL positive cells per HFP (scale bars = 500 μm, one-way ANOVA).

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: Over Expression, Injection, Immunohistochemical staining, Staining, Western Blot, TUNEL Assay

    Genome-wide analysis of Egr1 binding sites and analysis of Egr1 induced transcriptomic changes in APAP-injured mouse liver. Mice were treated with saline, 300 mg/kg APAP for 6 h and 12 h APAP, and liver samples were collected for ChIP-seq. Egr1 fl/fl and Egr1 LKO mice were injected with 300 mg/kg APAP for 12 h, and liver samples were collected for RNA-seq. Egr1 LKO mice were pretreated with Ad-Egr1 or Ad-GFP prior to challenge with 300 mg/kg APAP, after 12 h the liver samples were collected for RNA-seq. a. Bar-plot showed genomic distribution of peaks. b. Venn diagram showing the corresponding numbers of Egr1 -bound genes analyzed from ChIP-seq. c. Venn diagram showed the distinct genes that were transcriptionally regulated by Egr1, down-regulated by Egr1 deletion, up-regulated by Egr1 overexpression (fold change ≥ 1.5, P < 0.05, t test). d. Significantly enriched biological process categories in the GO analysis concerning the 161 transcriptionally upregulated genes. e. Heatmaps representing the Z score changes of genes in FAO between Egr1 fl/fl AILI mice and Egr1 LKO AILI mice, and Z score changes of genes in FAO between Ad-Egr1 or Ad-GFP pretreated AILI mice (n = 3 mice/group, fold change ≥ 1.5, P < 0.05, t test). f. Genome-browser screenshots of Acaa2 occupancy at Egr1 gene loci. g. Relative Acaa2 mRNA levels in AML12 cells of Ad-Egr1 or Ad-GFP group after 10mM APAP challenge for 6 h ( t test). h. Relative Acaa2 mRNA levels in Egr1 fl/fl and Egr1 LKO mice of Ad-Egr1 or Ad-GFP group after 300mg/kg APAP challenge for 12 h (n = 4 mice/group, one-way ANOVA).

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Genome-wide analysis of Egr1 binding sites and analysis of Egr1 induced transcriptomic changes in APAP-injured mouse liver. Mice were treated with saline, 300 mg/kg APAP for 6 h and 12 h APAP, and liver samples were collected for ChIP-seq. Egr1 fl/fl and Egr1 LKO mice were injected with 300 mg/kg APAP for 12 h, and liver samples were collected for RNA-seq. Egr1 LKO mice were pretreated with Ad-Egr1 or Ad-GFP prior to challenge with 300 mg/kg APAP, after 12 h the liver samples were collected for RNA-seq. a. Bar-plot showed genomic distribution of peaks. b. Venn diagram showing the corresponding numbers of Egr1 -bound genes analyzed from ChIP-seq. c. Venn diagram showed the distinct genes that were transcriptionally regulated by Egr1, down-regulated by Egr1 deletion, up-regulated by Egr1 overexpression (fold change ≥ 1.5, P < 0.05, t test). d. Significantly enriched biological process categories in the GO analysis concerning the 161 transcriptionally upregulated genes. e. Heatmaps representing the Z score changes of genes in FAO between Egr1 fl/fl AILI mice and Egr1 LKO AILI mice, and Z score changes of genes in FAO between Ad-Egr1 or Ad-GFP pretreated AILI mice (n = 3 mice/group, fold change ≥ 1.5, P < 0.05, t test). f. Genome-browser screenshots of Acaa2 occupancy at Egr1 gene loci. g. Relative Acaa2 mRNA levels in AML12 cells of Ad-Egr1 or Ad-GFP group after 10mM APAP challenge for 6 h ( t test). h. Relative Acaa2 mRNA levels in Egr1 fl/fl and Egr1 LKO mice of Ad-Egr1 or Ad-GFP group after 300mg/kg APAP challenge for 12 h (n = 4 mice/group, one-way ANOVA).

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: Genome Wide, Binding Assay, ChIP-sequencing, Injection, RNA Sequencing Assay, Over Expression

    The levels of Egr1 affected mitochondrial function in APAP-injured hepatocytes. a. PMHs were isolated from Egr1 fl/fl and Egr1 LKO mice and then treated with 20 mM APAP for different times. Cell viability was measured by CellTiter-Glo® luminescent cell viability assay ( t test). b. Western blot analysis of CYP2E1 levels in PMHs from Egr1 fl/fl and Egr1 LKO mice treated with 20 mM APAP for different times, followed by quantified protein levels ( t test). c. The ND-1 levels of PMHs treated with different doses of APAP for 12 h in Egr1 fl/fl and Egr1 LKO groups ( t test). d. Cell mito stress OCRs cause by Egr1 deficiency in PMHs were measure by Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction. Red arrows indicated the times when oligomycin, FCCP, and antimycin/rotenone were added to PMHs ( n = 4/group, one-way ANOVA). e. Representative TEM images of PMHs in Egr-1 LKO and Egr-1 fl/fl groups after DMEM (for control) and APAP treatment. Corresponding relative mitochondrial counts and surfaces were analyzed (one-way ANOVA). f. Western blot analysis of CYP2E1 levels in AML12 cells treated with 20 mM APAP at different times, followed by quantified protein levels (one-way ANOVA). g. AML12 cells were treated with Ad-Egr1 or Ad-CON for 48 h and then challenged with 10 mM APAP for 6 h, followed by PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction (n = 4/group, one-way ANOVA). BSA was used as a control for PA-BSA.

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: The levels of Egr1 affected mitochondrial function in APAP-injured hepatocytes. a. PMHs were isolated from Egr1 fl/fl and Egr1 LKO mice and then treated with 20 mM APAP for different times. Cell viability was measured by CellTiter-Glo® luminescent cell viability assay ( t test). b. Western blot analysis of CYP2E1 levels in PMHs from Egr1 fl/fl and Egr1 LKO mice treated with 20 mM APAP for different times, followed by quantified protein levels ( t test). c. The ND-1 levels of PMHs treated with different doses of APAP for 12 h in Egr1 fl/fl and Egr1 LKO groups ( t test). d. Cell mito stress OCRs cause by Egr1 deficiency in PMHs were measure by Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction. Red arrows indicated the times when oligomycin, FCCP, and antimycin/rotenone were added to PMHs ( n = 4/group, one-way ANOVA). e. Representative TEM images of PMHs in Egr-1 LKO and Egr-1 fl/fl groups after DMEM (for control) and APAP treatment. Corresponding relative mitochondrial counts and surfaces were analyzed (one-way ANOVA). f. Western blot analysis of CYP2E1 levels in AML12 cells treated with 20 mM APAP at different times, followed by quantified protein levels (one-way ANOVA). g. AML12 cells were treated with Ad-Egr1 or Ad-CON for 48 h and then challenged with 10 mM APAP for 6 h, followed by PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Basal and maximal respiration were calculated according to instruction (n = 4/group, one-way ANOVA). BSA was used as a control for PA-BSA.

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: Isolation, Cell Viability Assay, Western Blot

    Egr1 deficiency increased lipid droplets accumulation and FFAs levels in AILI. a. Oil Red O staining of PMHs in Egr1 fl/fl and Egr1 LKO groups after DMEM or 10 mM APAP treatment and the quantification of the ratio relative to the DMEM of Egr1 fl/fl group (one-way ANOVA). b-c. The levels of total fatty acids ( b ) and each fatty acid ( c ) of PMHs in Egr1 fl/fl and Egr1 LKO groups after 10 mM APAP treatment for 12 h determined by GC-MS-based FFA analysis (one-way ANOVA).

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Egr1 deficiency increased lipid droplets accumulation and FFAs levels in AILI. a. Oil Red O staining of PMHs in Egr1 fl/fl and Egr1 LKO groups after DMEM or 10 mM APAP treatment and the quantification of the ratio relative to the DMEM of Egr1 fl/fl group (one-way ANOVA). b-c. The levels of total fatty acids ( b ) and each fatty acid ( c ) of PMHs in Egr1 fl/fl and Egr1 LKO groups after 10 mM APAP treatment for 12 h determined by GC-MS-based FFA analysis (one-way ANOVA).

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: Staining, Gas Chromatography-Mass Spectrometry

    Egr1 protect mice and hepatocytes against AILI by transcriptionally up-regulating Acaa2. a. AML12 cells were knocked down of Acaa2 for 24 h, then overexpressed Egr1 for 24 h, finally challenged with 20 mM APAP treatment for 24 h. Cell viability was measured by CCK8 assay (one-way ANOVA). Cell viability of DMEM groups was used as normalization control groups. b. Acaa2 was knocked down in Hepa1-6 cells at 24 h, then overexpressed Egr1 for 48 h and followed by 10 mM APAP treatment for 3 h, finally PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Maximal respiration was calculated according to instruction (n = 5-6/group, one-way ANOVA). BSA was used as a control for PA-BSA. c - j. Mice were knocked down of Acaa2 at 24 h, then overexpressed Egr1 for 48 h via tail vein prior to 300 mg/kg APAP administration. After 6 h, liver and serum samples were collected. (c) Western blot analysis of Acaa2 levels in liver tissues of all groups, followed by quantified protein levels (n=3 mice/group, one-way ANOVA). Serum ALT, AST, LDH ( d ) levels, liver TG ( e ), HE ( f and g ), Oil Red O staining ( h ) and TUNEL staining ( i and j ) in all mice groups (n = 6 mice/group, one-way ANOVA). k. Luciferase activity assay of Acaa2 N-terminal promoter and truncated N-terminal promoters (N-1-5) in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test). l. Luciferase activity assay of WT and mutant N-2 promoters in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test).

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Egr1 protect mice and hepatocytes against AILI by transcriptionally up-regulating Acaa2. a. AML12 cells were knocked down of Acaa2 for 24 h, then overexpressed Egr1 for 24 h, finally challenged with 20 mM APAP treatment for 24 h. Cell viability was measured by CCK8 assay (one-way ANOVA). Cell viability of DMEM groups was used as normalization control groups. b. Acaa2 was knocked down in Hepa1-6 cells at 24 h, then overexpressed Egr1 for 48 h and followed by 10 mM APAP treatment for 3 h, finally PA-BSA or BSA treated for 1 h. Palmitate oxidation stress OCRs were measured using Seahorse XF96 analyzer. Maximal respiration was calculated according to instruction (n = 5-6/group, one-way ANOVA). BSA was used as a control for PA-BSA. c - j. Mice were knocked down of Acaa2 at 24 h, then overexpressed Egr1 for 48 h via tail vein prior to 300 mg/kg APAP administration. After 6 h, liver and serum samples were collected. (c) Western blot analysis of Acaa2 levels in liver tissues of all groups, followed by quantified protein levels (n=3 mice/group, one-way ANOVA). Serum ALT, AST, LDH ( d ) levels, liver TG ( e ), HE ( f and g ), Oil Red O staining ( h ) and TUNEL staining ( i and j ) in all mice groups (n = 6 mice/group, one-way ANOVA). k. Luciferase activity assay of Acaa2 N-terminal promoter and truncated N-terminal promoters (N-1-5) in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test). l. Luciferase activity assay of WT and mutant N-2 promoters in AML12 cells after Ad-Egr1 or Ad-CON treatment ( t test).

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: CCK-8 Assay, Western Blot, Staining, TUNEL Assay, Luciferase, Activity Assay, Mutagenesis

    Levels of EGR1 were increased in the liver and serum samples of patients with DILI. a. Representative EGR1 staining patterns in liver samples from DILI patients and healthy controls (scale bars = 200 μm or 50 μm). EGR1 H-scores in liver samples obtained from 24 patients with DILI and 16 healthy controls ( t test). Red arrows indicated positive staining. b. Distribution of liver histopathologic features and corresponding EGR1 H-scores in patients with DILI ( t test). c. The levels of EGR1 in serum samples from 21 patients with DILI and 17 healthy controls were measured by ELISA ( t test). d. Pearson correlation was performed between serum AST levels in 21 DILI patients and EGR1 serum levels. e. Pearson correlation was performed between latency less than 90 days in 18 DILI patients and EGR1 serum levels. f. Graphical abstract.

    Journal: International Journal of Biological Sciences

    Article Title: Egr1 confers protection against acetaminophen‑induced hepatotoxicity via transcriptional upregulating of Acaa2

    doi: 10.7150/ijbs.71781

    Figure Lengend Snippet: Levels of EGR1 were increased in the liver and serum samples of patients with DILI. a. Representative EGR1 staining patterns in liver samples from DILI patients and healthy controls (scale bars = 200 μm or 50 μm). EGR1 H-scores in liver samples obtained from 24 patients with DILI and 16 healthy controls ( t test). Red arrows indicated positive staining. b. Distribution of liver histopathologic features and corresponding EGR1 H-scores in patients with DILI ( t test). c. The levels of EGR1 in serum samples from 21 patients with DILI and 17 healthy controls were measured by ELISA ( t test). d. Pearson correlation was performed between serum AST levels in 21 DILI patients and EGR1 serum levels. e. Pearson correlation was performed between latency less than 90 days in 18 DILI patients and EGR1 serum levels. f. Graphical abstract.

    Article Snippet: The sheared chromatin (250 μg) was immunoprecipitated using primary antibodies against Egr1 (Cell Signaling Technology Cat# 4154) and IgG (Cell Signaling Technology Cat# 3900).

    Techniques: Staining, Enzyme-linked Immunosorbent Assay

    KORD-mediated inactivation decreased EGR-1 expression in RE. (A) Schematic of SALB injection, object training, and tissue collection. Panel created using BioRender.com . (B) Representative area of EGR-1 quantification . (C) Representative EGR-1 expression (red) against DAPI (blue) in RE in Control and KORD groups, 20x magnification. (D) Treatment with SALB 10 min prior to training decreased EGR-1 expression.

    Journal: Neurobiology of learning and memory

    Article Title: Chemogenetic inactivation of the nucleus reuniens impairs object placement memory in female mice

    doi: 10.1016/j.nlm.2021.107521

    Figure Lengend Snippet: KORD-mediated inactivation decreased EGR-1 expression in RE. (A) Schematic of SALB injection, object training, and tissue collection. Panel created using BioRender.com . (B) Representative area of EGR-1 quantification . (C) Representative EGR-1 expression (red) against DAPI (blue) in RE in Control and KORD groups, 20x magnification. (D) Treatment with SALB 10 min prior to training decreased EGR-1 expression.

    Article Snippet: To label EGR-1 expression, three sections of tissue containing RE between −0.4 mm and −0.96 mm relative to Bregma were washed in 25 mM PBS to remove cryoprotectant, blocked with 5% NGS in 25 mM PBS with 0.3% TritonX-100, and incubated overnight at 4 °C in EGR-1 rabbit primary antibody (1:500 in block solution, Cell Signaling #4153).

    Techniques: Expressing, Injection