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Roche roche halt protease inhibitor cocktails
Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 <t>inhibitor.</t> H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% <t>Roche/Halt</t> <t>protease</t> inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
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Article Title: Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates

Journal: Journal of Cancer

doi: 10.7150/jca.20779

Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 inhibitor. H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% Roche/Halt protease inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
Figure Legend Snippet: Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 inhibitor. H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% Roche/Halt protease inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.

Techniques Used: Modification, Incubation, Fluorescence

Related Articles

Modification:

Article Title: Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates
Article Snippet: These data show that Tris-based assay buffer supplemented with 0.5% combined Roche/Halt protease-inhibitor cocktails strongly suppress non-MP proteases without affecting recombinant or natural ADAM10sa and ADAM17sa. .. Validation of the modified PrAMA for examination of natural ADAM10sa and ADAM17sa in cell and tissue lysates was further performed as described below.

Protease Inhibitor:

Article Title: Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates
Article Snippet: .. These data show that Tris-based assay buffer supplemented with 0.5% combined Roche/Halt protease-inhibitor cocktails strongly suppress non-MP proteases without affecting recombinant or natural ADAM10sa and ADAM17sa. .. They also show that the high specificity PrAMA Syntherror/Sigmathreshold 0.5/≥1.0 scripts measure only the true-positive and distinguish accurately recombinant ADAM10sa and ADAM17sa, indicating that these PrAMA scripts might be optimal for the examination of the natural ADAM10sa and ADAM17sa in cell and tissue lysates.

Recombinant:

Article Title: Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates
Article Snippet: .. These data show that Tris-based assay buffer supplemented with 0.5% combined Roche/Halt protease-inhibitor cocktails strongly suppress non-MP proteases without affecting recombinant or natural ADAM10sa and ADAM17sa. .. They also show that the high specificity PrAMA Syntherror/Sigmathreshold 0.5/≥1.0 scripts measure only the true-positive and distinguish accurately recombinant ADAM10sa and ADAM17sa, indicating that these PrAMA scripts might be optimal for the examination of the natural ADAM10sa and ADAM17sa in cell and tissue lysates.

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    Roche roche halt protease inhibitor cocktails
    Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 <t>inhibitor.</t> H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% <t>Roche/Halt</t> <t>protease</t> inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
    Roche Halt Protease Inhibitor Cocktails, supplied by Roche, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/roche halt protease inhibitor cocktails/product/Roche
    Average 80 stars, based on 1 article reviews
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    Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 <t>inhibitor.</t> H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% <t>Roche/Halt</t> <t>protease</t> inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
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    Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 <t>inhibitor.</t> H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% <t>Roche/Halt</t> <t>protease</t> inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
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    Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 <t>inhibitor.</t> H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% <t>Roche/Halt</t> <t>protease</t> inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.
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    Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 inhibitor. H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% Roche/Halt protease inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.

    Journal: Journal of Cancer

    Article Title: Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates

    doi: 10.7150/jca.20779

    Figure Lengend Snippet: Modified PrAMA detects decreases of ADAM10sa in human-cell and -tissue lysates exposed to ADAM10 inhibitor. H441-cell ( A ) and T2495-tissue ( B ) lysates (2 μg) were supplemented with 0.5% Roche/Halt protease inhibitors, vehicle (Control) or GI254023X (1 μM), and PEPDAB substrates (10 μM), and incubated for 4 h. The developing fluorescence was measured hourly. The presented data are pM means of duplicate measurements ± SD of processed substrates, and are representative of ten experiments performed. The GI254023X-mediated inhibitions of PEPDAB005, 010 and/or 022 processing with the lysates are significant (H441: p=0.017, 0.0041 and 0.0058; T2495: p=0.05, 0.04 and 0.08, respectively). The substrate processing data were analyzed using the systematically increased Syntherror/Sigmathreshold parameters from 0.5/0.0 to 0.5/2.0. The obtained data at 4 h incubation are presented as PrAMA ADAM10sa AU of H441-cell ( C ) and T2495-tissue ( D ) lysates. PrAMA standard errors were 1.2% to 9%. Decreases of ADAM10sa in H441-cell ( E ) and T2495-tissue ( F ) lysates are presented as % of the specific enzyme activities in the control lysates relative to the GI254023X treated lysates.

    Article Snippet: These data show that Tris-based assay buffer supplemented with 0.5% combined Roche/Halt protease-inhibitor cocktails strongly suppress non-MP proteases without affecting recombinant or natural ADAM10sa and ADAM17sa.

    Techniques: Modification, Incubation, Fluorescence