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    Ventana Medical ventana discovery xt slide staining system
    Ventana Discovery Xt Slide Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 6 article reviews
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    ventana discovery xt slide staining system - by Bioz Stars, 2020-07
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    90
    Ventana Medical ventana discovery xt automated slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Automated Slide Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 90/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ventana discovery xt automated slide staining system/product/Ventana Medical
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    ventana discovery xt automated slide staining system - by Bioz Stars, 2020-07
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    94
    Ventana Medical ventana discovery xt automated slide stainer
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Automated Slide Stainer, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche ventana discovery xt automated ihc ish research slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Automated Ihc Ish Research Slide Staining System, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical ventana discovery xt slide autostaining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Slide Autostaining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 89/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical discovery xt staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 89/100, based on 262 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche discovery xt automated slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Automated Slide Staining System, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical ihc slide staining system discovery xt
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ihc Slide Staining System Discovery Xt, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical immunohistochemistry slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Immunohistochemistry Slide Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 88/100, based on 98 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical discovery xt automated ihc ish slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Automated Ihc Ish Slide Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical discovery xt automated ihc ish research slide staining system
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Automated Ihc Ish Research Slide Staining System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical discovery xt autostainer
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Autostainer, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 90/100, based on 309 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical ventana discovery xt automated immunostainer
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Automated Immunostainer, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 85/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Ventana Discovery Xt Automated System, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 91/100, based on 426 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt System Slide Stainer, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical discovery xt processors
    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false <t>discovery</t> rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step
    Discovery Xt Processors, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 88/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false discovery rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step

    Journal: Nature Communications

    Article Title: In vivo phosphoproteomics reveals kinase activity profiles that predict treatment outcome in triple-negative breast cancer

    doi: 10.1038/s41467-018-05742-z

    Figure Lengend Snippet: Kinases driving the profiles of the relapsed cases. a Example of a chart of normalized enrichment scores (NESs) (left) obtained for CLK1 from the relative abundance of its phosphorylated substrates in either the relapsed or the non-relapsed cases (right)—or kinase set enrichment analysis (KSEAS). Each substrate (phosphopeptide) is represented in the KSEA as a vertical black line. The proteins to which they map are represented in the right column by their encoding genes, adjacent to the site at which phosphorylation was detected. In this column, a larger or shorter horizontal bar depicts, for each substrate, the Log 2 -fold regulation in the relapsed (blue) versus non-relapsed (red) cases. b Two phosphatase (DUSP6 and PP2C-δ) and 9 kinase domains were enriched in the relapsed cases. The finding of an enriched phosphatase domain can be accounted for by the presence of a high concentration of a substrate for that phosphatase in a specific subgroup of patient tumors or cell lines. The in silico tool cannot predict whether a phosphatase is functional based on the absence of phosphorylation of its putative substrates; however, it can predict which upstream kinases or phosphatases can bind (and phosphorylate or cleave) an identified substrate. P -values and false discovery rates (FDR) are depicted for each kinase or phosphatase. Although most KSEAS show a low FDR, a relaxed FDR boundary (up to 0.25) was allowed to ensure as little information loss as possible in the mass spectrometry-to-immunohistochemistry translation step

    Article Snippet: Deparafinization and antigen retrieval (cell conditioning) were performed on DISCOVERY XT automated slide staining system using validated reagents (Ventana Medical Systems, Inc.).

    Techniques: Concentration Assay, In Silico, Functional Assay, Mass Spectrometry, Immunohistochemistry