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    Santa Cruz Biotechnology ets c 275
    Ets C 275, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ets c 275/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ets c 275 - by Bioz Stars, 2023-01
    86/100 stars
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    86
    Haynes International Inc hastelloy c 275
    Hastelloy C 275, supplied by Haynes International Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hastelloy c 275/product/Haynes International Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hastelloy c 275 - by Bioz Stars, 2023-01
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    86
    Santa Cruz Biotechnology c 275 anti ets1 antibody
    Schematic of the structure of the human <t>Ets1</t> protein. The positions of the CaMK II target serines in exon VII are indicated by an asterisk. Three mutants were constructed in which different combinations of these serines were replaced with alanine. Amino acid sequence is shown in single-letter code.
    C 275 Anti Ets1 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c 275 anti ets1 antibody/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c 275 anti ets1 antibody - by Bioz Stars, 2023-01
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    86
    Unitron Inc c 275 98 unitron scandinavia v ministeriet
    Schematic of the structure of the human <t>Ets1</t> protein. The positions of the CaMK II target serines in exon VII are indicated by an asterisk. Three mutants were constructed in which different combinations of these serines were replaced with alanine. Amino acid sequence is shown in single-letter code.
    C 275 98 Unitron Scandinavia V Ministeriet, supplied by Unitron Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c 275 98 unitron scandinavia v ministeriet/product/Unitron Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c 275 98 unitron scandinavia v ministeriet - by Bioz Stars, 2023-01
    86/100 stars
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    86
    Unitron Inc case c 275 98 unitron scandinavia a s
    Schematic of the structure of the human <t>Ets1</t> protein. The positions of the CaMK II target serines in exon VII are indicated by an asterisk. Three mutants were constructed in which different combinations of these serines were replaced with alanine. Amino acid sequence is shown in single-letter code.
    Case C 275 98 Unitron Scandinavia A S, supplied by Unitron Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/case c 275 98 unitron scandinavia a s/product/Unitron Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    case c 275 98 unitron scandinavia a s - by Bioz Stars, 2023-01
    86/100 stars
      Buy from Supplier

    Image Search Results


    Schematic of the structure of the human Ets1 protein. The positions of the CaMK II target serines in exon VII are indicated by an asterisk. Three mutants were constructed in which different combinations of these serines were replaced with alanine. Amino acid sequence is shown in single-letter code.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Schematic of the structure of the human Ets1 protein. The positions of the CaMK II target serines in exon VII are indicated by an asterisk. Three mutants were constructed in which different combinations of these serines were replaced with alanine. Amino acid sequence is shown in single-letter code.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Construct, Sequencing

    Phosphorylation of Ets1 wild-type and Ets1-m3 mutant by CaMK II in vitro. Ets1 proteins were separated by 10% SDS-PAGE, and the phosphorylated form was detected by autoradiography (top), whereas both forms were detected by Coomassie blue staining (bottom). The amounts of baculovirus-produced CaMK II (New England Biolabs) used were 125 U in lanes 3 and 6, 250 U in lanes 2, 4, and 7, and 500 U in lanes 5 and 8.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Phosphorylation of Ets1 wild-type and Ets1-m3 mutant by CaMK II in vitro. Ets1 proteins were separated by 10% SDS-PAGE, and the phosphorylated form was detected by autoradiography (top), whereas both forms were detected by Coomassie blue staining (bottom). The amounts of baculovirus-produced CaMK II (New England Biolabs) used were 125 U in lanes 3 and 6, 250 U in lanes 2, 4, and 7, and 500 U in lanes 5 and 8.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Mutagenesis, In Vitro, SDS Page, Autoradiography, Staining, Produced

    Effects of Ets1 wild-type and mutants on the GM-CSF promoter/enhancer in DG75 cells in the absence and presence of the phorbol ester PMA, the Ca2+ ionophore ionomycin, and the calcineurin inhibitor CsA. (A) Effects of treatment with PMA plus ionomycin and (B) effects of treatment with ionomycin plus CsA. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Effects of Ets1 wild-type and mutants on the GM-CSF promoter/enhancer in DG75 cells in the absence and presence of the phorbol ester PMA, the Ca2+ ionophore ionomycin, and the calcineurin inhibitor CsA. (A) Effects of treatment with PMA plus ionomycin and (B) effects of treatment with ionomycin plus CsA. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Luciferase, Activity Assay, Transfection, Expressing, Plasmid Preparation, Western Blot

    Effects of ionomycin plus CsA on activation of the GM-CSF promoter/enhancer by Ets1 wild type and mutants when the largest splice form of mouse Runx1 is overexpressed in DG75 cells. Assay conditions were as described in the legend to Figure ​Figure44.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Effects of ionomycin plus CsA on activation of the GM-CSF promoter/enhancer by Ets1 wild type and mutants when the largest splice form of mouse Runx1 is overexpressed in DG75 cells. Assay conditions were as described in the legend to Figure ​Figure44.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Activation Assay

    Decreased inhibition of the GM-CSF promoter/enhancer by constitutively active CaMK II on mutation of Ets1. (A) Cotransfection of constitutively active CaMK II T286D, inactive CaMK II T286A, or vector control with Ets1 wild type, mutant Ets1, or vector control in DG75 cells. (B) Same as A except that Runx1 was also cotransfected. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Decreased inhibition of the GM-CSF promoter/enhancer by constitutively active CaMK II on mutation of Ets1. (A) Cotransfection of constitutively active CaMK II T286D, inactive CaMK II T286A, or vector control with Ets1 wild type, mutant Ets1, or vector control in DG75 cells. (B) Same as A except that Runx1 was also cotransfected. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Inhibition, Mutagenesis, Cotransfection, Plasmid Preparation, Luciferase, Activity Assay, Transfection, Expressing

    Effects of Ets1 wild-type and mutants on the GM-CSF promoter/enhancer in (A) Raji cells and (B) K562 cells in the absence and presence of ionomycin plus CsA. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. The results from cotransfections of Ets1 wild type, mutant Ets1, or vector control with constitutively active CaMK II T286D compared with vector control are shown below the bars in B. These numbers are the average inhibitions in per cent from three independent transfections ± SD.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Effects of Ets1 wild-type and mutants on the GM-CSF promoter/enhancer in (A) Raji cells and (B) K562 cells in the absence and presence of ionomycin plus CsA. Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. The results from cotransfections of Ets1 wild type, mutant Ets1, or vector control with constitutively active CaMK II T286D compared with vector control are shown below the bars in B. These numbers are the average inhibitions in per cent from three independent transfections ± SD.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Luciferase, Activity Assay, Transfection, Expressing, Plasmid Preparation, Mutagenesis

    Binding of wild-type and mutant Ets1 to the GM-CSF promoter in vivo: decreased binding of wild-type Ets1 but not the Ets1-m3 mutant on ionomycin plus CsA treatment or expression of constitutively active CaMK II. (A) Schematic drawing of the GM-CSF reporter plasmid. The 716-bp human GM-CSF enhancer and the 647-bp human GM-CSF promoter segments (Cockerill et al., 1993 ; Jenkins et al., 1995 ; Shannon et al., 1997 ) are indicated. The positions of the primers used in ChIP, ChIP1 and ChIP2, relative to the weak (gray) and strong (black) Ets1 binding sites (Thomas et al., 1995 ) are indicated. (B) The amounts of the PCR product after ChIP with wild-type and mutant Ets1. Where indicated, either the cells were treated with ionomycin plus CsA, or constitutively active CaMK II was expressed (MATERIALS AND METHODS).

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Binding of wild-type and mutant Ets1 to the GM-CSF promoter in vivo: decreased binding of wild-type Ets1 but not the Ets1-m3 mutant on ionomycin plus CsA treatment or expression of constitutively active CaMK II. (A) Schematic drawing of the GM-CSF reporter plasmid. The 716-bp human GM-CSF enhancer and the 647-bp human GM-CSF promoter segments (Cockerill et al., 1993 ; Jenkins et al., 1995 ; Shannon et al., 1997 ) are indicated. The positions of the primers used in ChIP, ChIP1 and ChIP2, relative to the weak (gray) and strong (black) Ets1 binding sites (Thomas et al., 1995 ) are indicated. (B) The amounts of the PCR product after ChIP with wild-type and mutant Ets1. Where indicated, either the cells were treated with ionomycin plus CsA, or constitutively active CaMK II was expressed (MATERIALS AND METHODS).

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Binding Assay, Mutagenesis, In Vivo, Expressing, Plasmid Preparation

    Schematic illustrating the discussed models for regulation of GM-CSF transcription. The binding of NF-AT, NF-κB, Ets1, AP-1, and Runx1 transcription factors to the promoter is shown. For simplicity, only one NF-AT site and one Ets1 site are drawn, although the GM-CSF promoter/enhancer contains multiple binding sites for these factors (Thomas et al., 1995 ; Shannon et al., 1997 ; Thomas et al., 1997 ; McKinlay et al., 1998 ; Shang et al., 1999 ). The autoinhibitory domain of Ets1 (gray) and the Ets domain are also shown. Nonphosphorylated serines at positions 251, 257, 282, and 285 in the autoinhibitory domain are indicated with S and phosphorylation of these serines with P. Ca2+ signaling, which can be induced by TCR or BCR activation or by ionomycin treatment, positively regulates transcription from the GM-CSF promoter/enhancer through calcineurin activation of the transcription factors NF-AT, NF-κB, and AP-1 (Shannon et al., 1997 ). In the present study, we show that Ca2+ signaling can also negatively regulate the GM-CSF promoter/enhancer through CaMK II phosphorylation of serines in the autoinhibitory domain for DNA binding of Ets1. Serine phosphorylation in the autoinhibitory domain stabilizes the conformation that inhibits the DNA binding of the Ets domain (Cowley and Graves, 2000 ). The negative effect of wild-type Ets1 suggests that it functions as a dominant inhibitory protein that decreases transactivation by a functionally related protein(s), such as the p42 splice form of Ets1, that lacks the autoinhibitory domain or another Ets family member(s) that is less inhibited by CaMK II. The finding that the mutations also increased the Ets1 activity in the absence of Ca2+/CaMK II–activating treatment may, as illustrated, indicate that another kinase can mediate a partial phosphorylation in the absence of Ca2+ signaling. The circular arrow indicates a possible dynamic balance between Ca2+-dependent CaMK II and autophosphorylation that makes CaMK II independent of Ca2+ (Lukas et al., 1998 ). The intermediate nucleotides between the Runx1 and Ets1 sites in the GM-CSF promoter constitute a binding site for AP-1. The results suggest that when Ets1 functions in cooperation with nearby AP-1, at least a large part of the autoinhibition through phosphorylation of the autoinhibitory domain remains and is not relieved by interaction between Ets1 and Runx1.

    Journal:

    Article Title: Calcium Regulation of GM-CSF by Calmodulin-Dependent Kinase II Phosphorylation of Ets1

    doi: 10.1091/mbc.E02-03-0149

    Figure Lengend Snippet: Schematic illustrating the discussed models for regulation of GM-CSF transcription. The binding of NF-AT, NF-κB, Ets1, AP-1, and Runx1 transcription factors to the promoter is shown. For simplicity, only one NF-AT site and one Ets1 site are drawn, although the GM-CSF promoter/enhancer contains multiple binding sites for these factors (Thomas et al., 1995 ; Shannon et al., 1997 ; Thomas et al., 1997 ; McKinlay et al., 1998 ; Shang et al., 1999 ). The autoinhibitory domain of Ets1 (gray) and the Ets domain are also shown. Nonphosphorylated serines at positions 251, 257, 282, and 285 in the autoinhibitory domain are indicated with S and phosphorylation of these serines with P. Ca2+ signaling, which can be induced by TCR or BCR activation or by ionomycin treatment, positively regulates transcription from the GM-CSF promoter/enhancer through calcineurin activation of the transcription factors NF-AT, NF-κB, and AP-1 (Shannon et al., 1997 ). In the present study, we show that Ca2+ signaling can also negatively regulate the GM-CSF promoter/enhancer through CaMK II phosphorylation of serines in the autoinhibitory domain for DNA binding of Ets1. Serine phosphorylation in the autoinhibitory domain stabilizes the conformation that inhibits the DNA binding of the Ets domain (Cowley and Graves, 2000 ). The negative effect of wild-type Ets1 suggests that it functions as a dominant inhibitory protein that decreases transactivation by a functionally related protein(s), such as the p42 splice form of Ets1, that lacks the autoinhibitory domain or another Ets family member(s) that is less inhibited by CaMK II. The finding that the mutations also increased the Ets1 activity in the absence of Ca2+/CaMK II–activating treatment may, as illustrated, indicate that another kinase can mediate a partial phosphorylation in the absence of Ca2+ signaling. The circular arrow indicates a possible dynamic balance between Ca2+-dependent CaMK II and autophosphorylation that makes CaMK II independent of Ca2+ (Lukas et al., 1998 ). The intermediate nucleotides between the Runx1 and Ets1 sites in the GM-CSF promoter constitute a binding site for AP-1. The results suggest that when Ets1 functions in cooperation with nearby AP-1, at least a large part of the autoinhibition through phosphorylation of the autoinhibitory domain remains and is not relieved by interaction between Ets1 and Runx1.

    Article Snippet: Bars represent average ratio of luciferase/β-galactosidase activity in arbitrary units from three independent transfections ± SD, using β-galactosidase expression from an hCMV-β-gal plasmid for normalization. (C) Quantification of the expression level of Ets1 wild-type and the mutants in the transfected DG75 cells by Western blot using the C-275 anti-Ets1 antibody (Santa Cruz).

    Techniques: Binding Assay, Activation Assay, Activity Assay