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  • 94
    Enzo Biochem ac yvad amc
    Zinc-dependent mechanism. (A) Nigericin (20 μM, 10 min)-induced IL-1β release (i) and pro-IL-1β processing (ii) in LPS-treated (1 μg/mL, 2 h) peritoneal macrophages was inhibited by TPEN. (B) In vitro inflammasome assembly and caspase-1 activity, induced by hypotonic lysis of LPS-treated peritoneal macrophages was measured by <t>Ac-YVAD-AMC</t> cleavage, and was not inhibited by TPEN. RFU, relative fluorescence units. (C) The effects of a 20 min incubation of 50 μM TPEN on the Fura-2 (F340/F360), [Ca 2+ ] i response to 1 mM ATP in P2X7 expressing HEK-293 cells (i). Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in P2X7 expressing HEK-293 cells (ii). A summary of the slope of ethidium dye uptake in P2X7 expressing HEK-293 cells (iii). (D) Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in LPS-treated primary mouse peritoneal macrophages (i). A summary of the slope of ethidium dye uptake in primary mouse peritoneal macrophages (ii). Data show the mean±SD of at least three independent experiments. Fluorescence traces are representative of at least three separate experiments. *** p
    Ac Yvad Amc, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 94/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Pharmingen ac yvad amc
    Caspase-1 is activated early in differentiated mouse neuroblastoma N2a cells. Immunoblots showing caspase-1 activation in differentiated G37R ( a ) or G85R ( b ) positive N2a exposed to X/XO for 0, 1, 3, or 4 h. ( c ) Immunoblot of lysates from wt hSOD1-expressing cells (left) or G85R-positive cells (right) 4 h after X/XO treatment. ( d ) <t>YVAD-AMC</t> cleavage was measured as described and is reported relative to the cleavage induced by lysates of untreated (time 0) wt hSOD1-positive cultures. Data are the mean ± SD of three independent experiments for the G85R-positive cells and of two independent experiments assayed in duplicate for the G37R and wt hSOD1 expressing cells. Asterisks (*, P
    Ac Yvad Amc, supplied by Pharmingen, used in various techniques. Bioz Stars score: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Biomol GmbH ac yvad amc
    Caspase inhibition assay, group I and III caspases. A , Inhibition of caspase-1, a representative member of the group I caspases. The tetrapeptide <t>Ac-YVAD-AMC</t> (10 μ m ) served as the substrate. Enzyme concentration was held constant at 1 n m . The
    Ac Yvad Amc, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ac yvad amc
    Caspase inhibition assay, group I and III caspases. A , Inhibition of caspase-1, a representative member of the group I caspases. The tetrapeptide <t>Ac-YVAD-AMC</t> (10 μ m ) served as the substrate. Enzyme concentration was held constant at 1 n m . The
    Ac Yvad Amc, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson ac yvad amc substrate
    Caspase inhibition assay, group I and III caspases. A , Inhibition of caspase-1, a representative member of the group I caspases. The tetrapeptide <t>Ac-YVAD-AMC</t> (10 μ m ) served as the substrate. Enzyme concentration was held constant at 1 n m . The
    Ac Yvad Amc Substrate, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bachem ac yvad amc
    CRCP activity of cytosolic protein extracts from CGCs after 1, 4, or 12 hr of treatment with K25+S, K25−S, K5+S, or K5−S media. A, Cleavage of <t>Ac-DEVD-AMC</t> or <t>Ac-YVAD-AMC,</t> substrates for CPP32- or ICE-like proteases, respectively, were assayed fluorometrically by measuring the accumulation of free aminomethylcoumarin ( AMC ). Activities are represented as the rate of AMC accumulation in pmol/min. Closed symbols represent CPP32-like activity; open symbols represent ICE-like activity (at 0 pmol/min for all time points and conditions assayed). The dashed line indicates the level of CPP32-like protease activity in K25+S treated cultures after 12 hr (control). B, CPP32-like activity was confirmed by incubating protein extracts with 35 S-labeled recombinant PARP and analyzing the reaction products by SDS-PAGE and phosphorimagery. Bands running at 113 kDa represent uncleaved PARP; 89 and 24 kDa bands represent PARP cleavage products generated by CPP32-like protease activity. Ctrl = K25+S treated cultures after 12 hr.
    Ac Yvad Amc, supplied by Bachem, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Pharmingen fluorogenic substrate ac yvad amc
    CRCP activity of cytosolic protein extracts from CGCs after 1, 4, or 12 hr of treatment with K25+S, K25−S, K5+S, or K5−S media. A, Cleavage of <t>Ac-DEVD-AMC</t> or <t>Ac-YVAD-AMC,</t> substrates for CPP32- or ICE-like proteases, respectively, were assayed fluorometrically by measuring the accumulation of free aminomethylcoumarin ( AMC ). Activities are represented as the rate of AMC accumulation in pmol/min. Closed symbols represent CPP32-like activity; open symbols represent ICE-like activity (at 0 pmol/min for all time points and conditions assayed). The dashed line indicates the level of CPP32-like protease activity in K25+S treated cultures after 12 hr (control). B, CPP32-like activity was confirmed by incubating protein extracts with 35 S-labeled recombinant PARP and analyzing the reaction products by SDS-PAGE and phosphorimagery. Bands running at 113 kDa represent uncleaved PARP; 89 and 24 kDa bands represent PARP cleavage products generated by CPP32-like protease activity. Ctrl = K25+S treated cultures after 12 hr.
    Fluorogenic Substrate Ac Yvad Amc, supplied by Pharmingen, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Enzo Biochem caspase 1 substrate ac yvad amc
    Analysis of IL-1β release, <t>caspase-1</t> activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor <t>AC-YVAD-CHO</t> (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p
    Caspase 1 Substrate Ac Yvad Amc, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Peptide Institute fluorogenic caspase 3 substrate ac yvad amc
    Analysis of IL-1β release, <t>caspase-1</t> activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor <t>AC-YVAD-CHO</t> (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p
    Fluorogenic Caspase 3 Substrate Ac Yvad Amc, supplied by Peptide Institute, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Enzo Biochem fluorogenic substrate ac yvad amc
    Analysis of IL-1β release, <t>caspase-1</t> activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor <t>AC-YVAD-CHO</t> (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p
    Fluorogenic Substrate Ac Yvad Amc, supplied by Enzo Biochem, 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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    Peptide Institute caspase 3 activity assay fluorogenic caspase 3 substrate ac yvad amc
    Analysis of IL-1β release, <t>caspase-1</t> activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor <t>AC-YVAD-CHO</t> (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p
    Caspase 3 Activity Assay Fluorogenic Caspase 3 Substrate Ac Yvad Amc, supplied by Peptide Institute, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Zinc-dependent mechanism. (A) Nigericin (20 μM, 10 min)-induced IL-1β release (i) and pro-IL-1β processing (ii) in LPS-treated (1 μg/mL, 2 h) peritoneal macrophages was inhibited by TPEN. (B) In vitro inflammasome assembly and caspase-1 activity, induced by hypotonic lysis of LPS-treated peritoneal macrophages was measured by Ac-YVAD-AMC cleavage, and was not inhibited by TPEN. RFU, relative fluorescence units. (C) The effects of a 20 min incubation of 50 μM TPEN on the Fura-2 (F340/F360), [Ca 2+ ] i response to 1 mM ATP in P2X7 expressing HEK-293 cells (i). Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in P2X7 expressing HEK-293 cells (ii). A summary of the slope of ethidium dye uptake in P2X7 expressing HEK-293 cells (iii). (D) Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in LPS-treated primary mouse peritoneal macrophages (i). A summary of the slope of ethidium dye uptake in primary mouse peritoneal macrophages (ii). Data show the mean±SD of at least three independent experiments. Fluorescence traces are representative of at least three separate experiments. *** p

    Journal: European Journal of Immunology

    Article Title: Pannexin-1-dependent caspase-1 activation and secretion of IL-1? is regulated by zinc

    doi: 10.1002/eji.200838843

    Figure Lengend Snippet: Zinc-dependent mechanism. (A) Nigericin (20 μM, 10 min)-induced IL-1β release (i) and pro-IL-1β processing (ii) in LPS-treated (1 μg/mL, 2 h) peritoneal macrophages was inhibited by TPEN. (B) In vitro inflammasome assembly and caspase-1 activity, induced by hypotonic lysis of LPS-treated peritoneal macrophages was measured by Ac-YVAD-AMC cleavage, and was not inhibited by TPEN. RFU, relative fluorescence units. (C) The effects of a 20 min incubation of 50 μM TPEN on the Fura-2 (F340/F360), [Ca 2+ ] i response to 1 mM ATP in P2X7 expressing HEK-293 cells (i). Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in P2X7 expressing HEK-293 cells (ii). A summary of the slope of ethidium dye uptake in P2X7 expressing HEK-293 cells (iii). (D) Representative fluorescence traces showing the effects of vehicle (DMSO), TPEN (50 μM), and 10 panx1 (mimetic pannexin-1 peptide, 400 μM), on ATP (3 mM) induced ethidium dye uptake in LPS-treated primary mouse peritoneal macrophages (i). A summary of the slope of ethidium dye uptake in primary mouse peritoneal macrophages (ii). Data show the mean±SD of at least three independent experiments. Fluorescence traces are representative of at least three separate experiments. *** p

    Article Snippet: The supernatants were collected and incubated with 20 μM Ac-YVAD-AMC (Alexis Biochemicals) for 4 h at 4°C or at 37°C.

    Techniques: In Vitro, Activity Assay, Lysis, Fluorescence, Incubation, Expressing

    Caspase-1 is activated early in differentiated mouse neuroblastoma N2a cells. Immunoblots showing caspase-1 activation in differentiated G37R ( a ) or G85R ( b ) positive N2a exposed to X/XO for 0, 1, 3, or 4 h. ( c ) Immunoblot of lysates from wt hSOD1-expressing cells (left) or G85R-positive cells (right) 4 h after X/XO treatment. ( d ) YVAD-AMC cleavage was measured as described and is reported relative to the cleavage induced by lysates of untreated (time 0) wt hSOD1-positive cultures. Data are the mean ± SD of three independent experiments for the G85R-positive cells and of two independent experiments assayed in duplicate for the G37R and wt hSOD1 expressing cells. Asterisks (*, P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Caspase-1 and -3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis

    doi:

    Figure Lengend Snippet: Caspase-1 is activated early in differentiated mouse neuroblastoma N2a cells. Immunoblots showing caspase-1 activation in differentiated G37R ( a ) or G85R ( b ) positive N2a exposed to X/XO for 0, 1, 3, or 4 h. ( c ) Immunoblot of lysates from wt hSOD1-expressing cells (left) or G85R-positive cells (right) 4 h after X/XO treatment. ( d ) YVAD-AMC cleavage was measured as described and is reported relative to the cleavage induced by lysates of untreated (time 0) wt hSOD1-positive cultures. Data are the mean ± SD of three independent experiments for the G85R-positive cells and of two independent experiments assayed in duplicate for the G37R and wt hSOD1 expressing cells. Asterisks (*, P

    Article Snippet: Equal amounts of lysates were incubated for 1 h at 37°C with 200 μl of Hepes buffer with either Ac-YVAD-AMC or Ac-DEVD-AMC (PharMingen; AMC = 7-amino-4-methylcoumarin) to measure caspase-1 and -3, respectively.

    Techniques: Western Blot, Activation Assay, Expressing

    Caspase inhibition assay, group I and III caspases. A , Inhibition of caspase-1, a representative member of the group I caspases. The tetrapeptide Ac-YVAD-AMC (10 μ m ) served as the substrate. Enzyme concentration was held constant at 1 n m . The

    Journal: The Journal of Neuroscience

    Article Title: The Neuronal Apoptosis Inhibitory Protein Is a Direct Inhibitor of Caspases 3 and 7

    doi: 10.1523/JNEUROSCI.22-06-02035.2002

    Figure Lengend Snippet: Caspase inhibition assay, group I and III caspases. A , Inhibition of caspase-1, a representative member of the group I caspases. The tetrapeptide Ac-YVAD-AMC (10 μ m ) served as the substrate. Enzyme concentration was held constant at 1 n m . The

    Article Snippet: Ac-YVAD-AMC (Biomol, Plymouth Meeting, PA) was used as the substrate for caspase-1 and Ac-DEVD-AMC for caspase-3, caspase-7, and caspase-8.

    Techniques: Inhibition, Concentration Assay

    CRCP activity of cytosolic protein extracts from CGCs after 1, 4, or 12 hr of treatment with K25+S, K25−S, K5+S, or K5−S media. A, Cleavage of Ac-DEVD-AMC or Ac-YVAD-AMC, substrates for CPP32- or ICE-like proteases, respectively, were assayed fluorometrically by measuring the accumulation of free aminomethylcoumarin ( AMC ). Activities are represented as the rate of AMC accumulation in pmol/min. Closed symbols represent CPP32-like activity; open symbols represent ICE-like activity (at 0 pmol/min for all time points and conditions assayed). The dashed line indicates the level of CPP32-like protease activity in K25+S treated cultures after 12 hr (control). B, CPP32-like activity was confirmed by incubating protein extracts with 35 S-labeled recombinant PARP and analyzing the reaction products by SDS-PAGE and phosphorimagery. Bands running at 113 kDa represent uncleaved PARP; 89 and 24 kDa bands represent PARP cleavage products generated by CPP32-like protease activity. Ctrl = K25+S treated cultures after 12 hr.

    Journal: The Journal of Neuroscience

    Article Title: The Role of CED-3-Related Cysteine Proteases in Apoptosis of Cerebellar Granule Cells

    doi: 10.1523/JNEUROSCI.17-16-06105.1997

    Figure Lengend Snippet: CRCP activity of cytosolic protein extracts from CGCs after 1, 4, or 12 hr of treatment with K25+S, K25−S, K5+S, or K5−S media. A, Cleavage of Ac-DEVD-AMC or Ac-YVAD-AMC, substrates for CPP32- or ICE-like proteases, respectively, were assayed fluorometrically by measuring the accumulation of free aminomethylcoumarin ( AMC ). Activities are represented as the rate of AMC accumulation in pmol/min. Closed symbols represent CPP32-like activity; open symbols represent ICE-like activity (at 0 pmol/min for all time points and conditions assayed). The dashed line indicates the level of CPP32-like protease activity in K25+S treated cultures after 12 hr (control). B, CPP32-like activity was confirmed by incubating protein extracts with 35 S-labeled recombinant PARP and analyzing the reaction products by SDS-PAGE and phosphorimagery. Bands running at 113 kDa represent uncleaved PARP; 89 and 24 kDa bands represent PARP cleavage products generated by CPP32-like protease activity. Ctrl = K25+S treated cultures after 12 hr.

    Article Snippet: To assay for CPP32- or ICE-like activity, 20 μg of cytosolic protein was incubated in a microtiter plate with the fluorescent tetrapeptide substrate Ac-DEVD-AMC or Ac-YVAD-AMC (20 μ m ) (Bachem, Torrance, CA), respectively.

    Techniques: Activity Assay, Labeling, Recombinant, SDS Page, Generated

    Analysis of IL-1β release, caspase-1 activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor AC-YVAD-CHO (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Activation of the NLRP3 Inflammasome Pathway by Uropathogenic Escherichia coli Is Virulence Factor-Dependent and Influences Colonization of Bladder Epithelial Cells

    doi: 10.3389/fcimb.2018.00081

    Figure Lengend Snippet: Analysis of IL-1β release, caspase-1 activity and LDH release in caspase-1 or NLRP3 deficient 5637 cells. Caspase-1 (A) and NLRP3 (B) knockdowns were created by CRISPR/Cas9 and evaluated by Western blot. GAPDH was used as a loading control. Cas9 (control cells), -caspase-1, or NLRP3-deficient bladder epithelial 5637 cells were infected with CFT073 for 6 h at MOI 10. IL-1β (C) and LDH release (D) were measured. 5637 cells were pre-incubated with DMSO, the caspase 1/4 inhibitor AC-YVAD-CHO (10 μM) or the caspase 3 inhibitor AC-DEVD-CHO (10 μM) for 1 h prior to infection with CFT073 at MOI 1 and 10 for 6 h followed by analysis of IL-1β release (E) and caspase-1 activity (F) . Caspase-1 results are presented as fold increase of mean fluorescence units (MFU) compared to unstimulated control cells. LDH release is presented as % of total LDH. IL-1β release is presented as % of unstimulated control and the dotted line represents the unstimulated control (E) . Data are presented as mean ± SEM ( n = 3 independent experiments). Asterisks denote statistical significance compared to respective unstimulated control (* p

    Article Snippet: Caspase-1 activity assay Bladder epithelial cells were grown to confluence in a 96-well plate and pre-incubated with the caspase-1 substrate Ac-YVAD-AMC (Enzo Life Sciences, New York, NY, USA) for 1 h at 37°C 5% CO2 .

    Techniques: Activity Assay, CRISPR, Western Blot, Infection, Incubation, Fluorescence