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  • 86
    Peptides International ac lehd amc
    Ac Lehd Amc, supplied by Peptides International, used in various techniques. Bioz Stars score: 86/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    AnaSpec ac lehd amc
    Ac Lehd Amc, supplied by AnaSpec, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Biomol GmbH ac lehd amc
    In vitro inhibition of caspase-9 activity by AMVIAP. Human caspase-9 activity was assayed in vitro with <t>Ac-LEHD-AMC</t> as a substrate. Caspase-9 was mixed with either GST at 2 μM (○), XIAP at 500 nM (+), and AMVIAP at 500 nM (•) or 5,000 nM (5 μM) (▴). Activity was estimated by LEHD-AMC cleavage. Each data series represents fluorescence emission (490 nm) at 1-min intervals for 120 min.
    Ac Lehd Amc, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 88/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cayman Chemical ac lehd amc
    In vitro inhibition of caspase-9 activity by AMVIAP. Human caspase-9 activity was assayed in vitro with <t>Ac-LEHD-AMC</t> as a substrate. Caspase-9 was mixed with either GST at 2 μM (○), XIAP at 500 nM (+), and AMVIAP at 500 nM (•) or 5,000 nM (5 μM) (▴). Activity was estimated by LEHD-AMC cleavage. Each data series represents fluorescence emission (490 nm) at 1-min intervals for 120 min.
    Ac Lehd Amc, supplied by Cayman Chemical, 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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    Enzo Biochem ac lehd amc
    Overexpression of GCL inhibits As3+-induced cytochrome c release and caspase-9 activation ) and cytochrome c expression in the fractions was assessed by immunoblotting. (B) Caspase-9-like activity was measured utilizing the fluorogenic substrate <t>Ac-LEHD-AMC.</t> The data presented in B are averages +/− SEM of at least three experiments. # p
    Ac Lehd Amc, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 92/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson ac lehd amc
    SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways. Notes: ( A – F ): SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways, inhibited caspase-8, and prevented DcR3-TRAIL-induced cascade activation. HepG2 cells were pretreated with 50 μM Ac-IETD-CHO or 50 μM <t>Ac-LEHD-CMK</t> 20 min before treatment with TRAIL (100 ng/mL, for 24 h). Caspase-3, caspase-8, and caspase-9 activity was determined fluorometrically in cell extracts using <t>Ac-DEVD-AMC,</t> Ac-IETD-AFC, and Ac-LEHD-AMC as flurogenic substrate, respectively. Abbreviations: DcR, decoy receptor; h, hours; TRAIL, tumor necrosis factor-related apoptosis-inducing ligand.
    Ac Lehd Amc, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore ac lehd amc
    Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: <t>Ac-YVAD-AMC</t> (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), <t>Ac-LEHD-AMC</t> (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).
    Ac Lehd Amc, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    AG Scientific ac lehd amc substrate
    Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: <t>Ac-YVAD-AMC</t> (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), <t>Ac-LEHD-AMC</t> (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).
    Ac Lehd Amc Substrate, supplied by AG Scientific, 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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    Thermo Fisher ac lehd amc substrate
    Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: <t>Ac-YVAD-AMC</t> (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), <t>Ac-LEHD-AMC</t> (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).
    Ac Lehd Amc Substrate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Pharmingen ac lehd amc
    Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: <t>Ac-YVAD-AMC</t> (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), <t>Ac-LEHD-AMC</t> (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).
    Ac Lehd Amc, supplied by Pharmingen, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bachem ac lehd amc
    FIGURE 1: T. gondii inhibits cytochrome c -induced activation of the caspase 9-caspase3/7 cascade in cell-free cytosolic extracts. (A, B) Cell-free cytosolic extracts of Jurkat cells were incubated with increasing amounts of parasites as indicated (cross-hatched bars; no. of parasites per 0.1 ml) or were left untreated (black bars). After 1 hour, caspase activation was triggered or not by cytochrome c and dATP. Cleavage of the caspase 3/7 substrate <t>DEVD-AMC</t> (A) or of the caspase 9 substrate <t>LEHD-AMC</t> (B) was measured fluorimetrically. Data represent the increase in substrate cleavage over time; they represent means ± S.E.M. from at least 3 independent experiments. Significant differences were identified by Student’s t -test (** P
    Ac Lehd Amc, supplied by Bachem, used in various techniques. Bioz Stars score: 87/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Alexis Inc ac lehd amc
    FIGURE 1: T. gondii inhibits cytochrome c -induced activation of the caspase 9-caspase3/7 cascade in cell-free cytosolic extracts. (A, B) Cell-free cytosolic extracts of Jurkat cells were incubated with increasing amounts of parasites as indicated (cross-hatched bars; no. of parasites per 0.1 ml) or were left untreated (black bars). After 1 hour, caspase activation was triggered or not by cytochrome c and dATP. Cleavage of the caspase 3/7 substrate <t>DEVD-AMC</t> (A) or of the caspase 9 substrate <t>LEHD-AMC</t> (B) was measured fluorimetrically. Data represent the increase in substrate cleavage over time; they represent means ± S.E.M. from at least 3 independent experiments. Significant differences were identified by Student’s t -test (** P
    Ac Lehd Amc, supplied by Alexis Inc, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    In vitro inhibition of caspase-9 activity by AMVIAP. Human caspase-9 activity was assayed in vitro with Ac-LEHD-AMC as a substrate. Caspase-9 was mixed with either GST at 2 μM (○), XIAP at 500 nM (+), and AMVIAP at 500 nM (•) or 5,000 nM (5 μM) (▴). Activity was estimated by LEHD-AMC cleavage. Each data series represents fluorescence emission (490 nm) at 1-min intervals for 120 min.

    Journal: Journal of Virology

    Article Title: Functional Analysis of the Inhibitor of Apoptosis (iap) Gene Carried by the Entomopoxvirus of Amsacta moorei

    doi: 10.1128/JVI.79.4.2335-2345.2005

    Figure Lengend Snippet: In vitro inhibition of caspase-9 activity by AMVIAP. Human caspase-9 activity was assayed in vitro with Ac-LEHD-AMC as a substrate. Caspase-9 was mixed with either GST at 2 μM (○), XIAP at 500 nM (+), and AMVIAP at 500 nM (•) or 5,000 nM (5 μM) (▴). Activity was estimated by LEHD-AMC cleavage. Each data series represents fluorescence emission (490 nm) at 1-min intervals for 120 min.

    Article Snippet: Caspase-9 reactions were performed in 96-well plates containing caspase reaction buffer supplemented with 0.4 mM Ac-LEHD-AMC (Biomol) and 200 U of recombinant active caspase-9 (100 U/μl; Biomol) in a total volume of 100 μl.

    Techniques: In Vitro, Inhibition, Activity Assay, Fluorescence

    Overexpression of GCL inhibits As3+-induced cytochrome c release and caspase-9 activation ) and cytochrome c expression in the fractions was assessed by immunoblotting. (B) Caspase-9-like activity was measured utilizing the fluorogenic substrate Ac-LEHD-AMC. The data presented in B are averages +/− SEM of at least three experiments. # p

    Journal: Toxicology letters

    Article Title: Enhanced glutathione biosynthetic capacity promotes resistance to As3+-induced apoptosis

    doi: 10.1016/j.toxlet.2009.12.004

    Figure Lengend Snippet: Overexpression of GCL inhibits As3+-induced cytochrome c release and caspase-9 activation ) and cytochrome c expression in the fractions was assessed by immunoblotting. (B) Caspase-9-like activity was measured utilizing the fluorogenic substrate Ac-LEHD-AMC. The data presented in B are averages +/− SEM of at least three experiments. # p

    Article Snippet: All reagents were prepared in either H2 O, sterile phosphate-buffered saline (PBS) or DMSO. z-VAD-fmk was from Bachem Bioscience (Torrance, CA) and Ac-DEVDAMC, Ac-IETD-AMC, and Ac-LEHD-AMC were from Alexis Biochemicals (San Diego, CA).

    Techniques: Over Expression, Activation Assay, Expressing, Activity Assay

    Time- and dose-dependent As3+-induced apoptosis in Hepa-1c1c7 cells ). (B) Caspase activities were determined as described in the Methods section utilizing the fluorogenic substrates Ac-DEVD-AMC (caspase-3), AcIETD-AMC (caspase-8), and Ac-LEHD-AMC (caspase-9). (C) Cells were pretreated with z-VAD-fmk (50 uM) for 1 h prior to treatment with As3+ (20 uM) for 16 h and apoptosis quantified as described above. Data presented are averages +/- SEM of at least three experiments. + p

    Journal: Toxicology letters

    Article Title: Enhanced glutathione biosynthetic capacity promotes resistance to As3+-induced apoptosis

    doi: 10.1016/j.toxlet.2009.12.004

    Figure Lengend Snippet: Time- and dose-dependent As3+-induced apoptosis in Hepa-1c1c7 cells ). (B) Caspase activities were determined as described in the Methods section utilizing the fluorogenic substrates Ac-DEVD-AMC (caspase-3), AcIETD-AMC (caspase-8), and Ac-LEHD-AMC (caspase-9). (C) Cells were pretreated with z-VAD-fmk (50 uM) for 1 h prior to treatment with As3+ (20 uM) for 16 h and apoptosis quantified as described above. Data presented are averages +/- SEM of at least three experiments. + p

    Article Snippet: All reagents were prepared in either H2 O, sterile phosphate-buffered saline (PBS) or DMSO. z-VAD-fmk was from Bachem Bioscience (Torrance, CA) and Ac-DEVDAMC, Ac-IETD-AMC, and Ac-LEHD-AMC were from Alexis Biochemicals (San Diego, CA).

    Techniques:

    SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways. Notes: ( A – F ): SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways, inhibited caspase-8, and prevented DcR3-TRAIL-induced cascade activation. HepG2 cells were pretreated with 50 μM Ac-IETD-CHO or 50 μM Ac-LEHD-CMK 20 min before treatment with TRAIL (100 ng/mL, for 24 h). Caspase-3, caspase-8, and caspase-9 activity was determined fluorometrically in cell extracts using Ac-DEVD-AMC, Ac-IETD-AFC, and Ac-LEHD-AMC as flurogenic substrate, respectively. Abbreviations: DcR, decoy receptor; h, hours; TRAIL, tumor necrosis factor-related apoptosis-inducing ligand.

    Journal: OncoTargets and therapy

    Article Title: Downregulation of DcR3 sensitizes hepatocellular carcinoma cells to TRAIL-induced apoptosis

    doi: 10.2147/OTT.S127202

    Figure Lengend Snippet: SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways. Notes: ( A – F ): SiDcR3-combined TRAIL activated extrinsic and intrinsic apoptotic signaling pathways, inhibited caspase-8, and prevented DcR3-TRAIL-induced cascade activation. HepG2 cells were pretreated with 50 μM Ac-IETD-CHO or 50 μM Ac-LEHD-CMK 20 min before treatment with TRAIL (100 ng/mL, for 24 h). Caspase-3, caspase-8, and caspase-9 activity was determined fluorometrically in cell extracts using Ac-DEVD-AMC, Ac-IETD-AFC, and Ac-LEHD-AMC as flurogenic substrate, respectively. Abbreviations: DcR, decoy receptor; h, hours; TRAIL, tumor necrosis factor-related apoptosis-inducing ligand.

    Article Snippet: Caspase assays Substrates Ac-DEVD-AMC, Ac-IETD-AFC, and Ac-LEHD-AMC were used to assess the activities of caspase-3, caspase-8, and caspase-9 in protein extractions using a fluorimeter according to the manufacturer’s instructions (BD Biosciences).

    Techniques: Activation Assay, Activity Assay

    Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: Ac-YVAD-AMC (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), Ac-LEHD-AMC (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).

    Journal: Scientific Reports

    Article Title: Transcriptomic and proteomic analysis reveals mechanisms of embryo abortion during chrysanthemum cross breeding

    doi: 10.1038/srep06536

    Figure Lengend Snippet: Caspase-like activities in normal and abortive chrysanthemum embryos. Embryo extracts were measured for substrate specificity using different caspase substrates: Ac-YVAD-AMC (YVADase), Ac-DEVD-AMC (DEVDase), Ac-LEVD-AMC (LEVDase), Ac-VEID-AMC (VEIDase), Ac-LEHD-AMC (LEHDase). Relative fluorescence units were calculated and expressed as a percentage of the LEHDase activity. AE 18 (abortive embryos) has the highest cleavage activities for Ac-LEVD-AMC, Ac-VEID-AMC and Ac-LEHD-AMC compared with NE12 and NE 18, indicating that chrysanthemum embryo abortion is a result of programmed cell death. Different letters indicate significant differences at alpha = 0.05 by the Bonferroni t-test (the bar is standard error).

    Article Snippet: Caspase-like activities were measured by using AMC substrates: Ac-YVAD-AMC, Ac-DEVD-AMC, Ac-LEVD-AMC, Ac-VEID-AMC, Ac-LEHD-AMC (sigma, USA), which are selective fluorogenic substrate for caspase 1, caspase 3, caspase 4, caspase 6, caspase 9, respectively.

    Techniques: Fluorescence, Activity Assay

    FIGURE 1: T. gondii inhibits cytochrome c -induced activation of the caspase 9-caspase3/7 cascade in cell-free cytosolic extracts. (A, B) Cell-free cytosolic extracts of Jurkat cells were incubated with increasing amounts of parasites as indicated (cross-hatched bars; no. of parasites per 0.1 ml) or were left untreated (black bars). After 1 hour, caspase activation was triggered or not by cytochrome c and dATP. Cleavage of the caspase 3/7 substrate DEVD-AMC (A) or of the caspase 9 substrate LEHD-AMC (B) was measured fluorimetrically. Data represent the increase in substrate cleavage over time; they represent means ± S.E.M. from at least 3 independent experiments. Significant differences were identified by Student’s t -test (** P

    Journal: Microbial Cell

    Article Title: Toxoplasma gondii inhibits cytochrome c-induced caspase activation in its host cell by interference with holo-apoptosome assembly

    doi: 10.15698/mic2015.05.201

    Figure Lengend Snippet: FIGURE 1: T. gondii inhibits cytochrome c -induced activation of the caspase 9-caspase3/7 cascade in cell-free cytosolic extracts. (A, B) Cell-free cytosolic extracts of Jurkat cells were incubated with increasing amounts of parasites as indicated (cross-hatched bars; no. of parasites per 0.1 ml) or were left untreated (black bars). After 1 hour, caspase activation was triggered or not by cytochrome c and dATP. Cleavage of the caspase 3/7 substrate DEVD-AMC (A) or of the caspase 9 substrate LEHD-AMC (B) was measured fluorimetrically. Data represent the increase in substrate cleavage over time; they represent means ± S.E.M. from at least 3 independent experiments. Significant differences were identified by Student’s t -test (** P

    Article Snippet: Briefly, 10 µl cell extract was mixed in triplicate with 90 µl of 50 mM NaCl, 10 mM HEPES, pH 7.0, 40 mM β-glycerophosphate, 2 mM MgCl2 , 5 mM EGTA, 0.1 mg/ml BSA, 0.1% CHAPS and 10 µM Ac-DEVD-AMC (caspase 3/7 substrate) or 50 µM Ac-LEHD-AMC (caspase 9 substrate; both from Bachem, Weil am Rhein, Germany).

    Techniques: Activation Assay, Incubation