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recombinant human asc protein(abnova)  (Abnova)

 
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    Abnova recombinant human asc protein(abnova)
    ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + <t>ASC</t> + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with <t>recombinant</t> human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).
    Recombinant Human Asc Protein(Abnova), supplied by Abnova, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human asc protein(abnova)/product/Abnova
    Average 90 stars, based on 1 article reviews
    recombinant human asc protein(abnova) - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Targeting ASC in NLRP3 inflammasome by caffeic acid phenethyl ester: a novel strategy to treat acute gout"

    Article Title: Targeting ASC in NLRP3 inflammasome by caffeic acid phenethyl ester: a novel strategy to treat acute gout

    Journal: Scientific Reports

    doi: 10.1038/srep38622

    ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + ASC + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with recombinant human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).
    Figure Legend Snippet: ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + ASC + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with recombinant human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).

    Techniques Used: Transfection, Luciferase, Plasmid Preparation, Expressing, Derivative Assay, Activation Assay, Activity Assay, Control, In Vitro, Recombinant, Fluorescence

    ( A ) The structure of biotin-tagged CA (BT-CA), biotin-tagged DMC (BT-DMC), and biotin-tagged DHC (BT-DHC). ( B ) LPS-primed BMDMs were treated with CAPE, BT-CA, BT-DMC, and BT-DHC (10 μM) for 1 hr and then stimulated with monosodium uric acid (MSU) crystals (500 μg/ml) for 6 hr. The cell culture supernatants were analyzed for secreted IL-1β using ELISA. The values represent the means ± SEM (n = 3). # Significantly different from vehicle alone, p < 0.0001. *Significantly different from MSU alone, p < 0.0001. ( C ) After BMDM cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr, cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. The amount of ASC expression in cell lysates were determined as “input”. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( D ) After 293T cells were transfected with ASC-expression plasmids, the cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr. The cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( E ) Sensograms of CAPE binding to recombinant ASC protein in the presence of detergent (0.005% Tween-20) were obtained from surface plasmon resonance (SPR) analysis. Different concentrations of CAPE are presented as an overlay plot aligned at the start of injection. ( F ) The line graph of dose-binding response unit curve and the table showing kinetic parameters of the binding between CAPE and ASC calculated using a simple 1:1 interaction model were from SPR analysis in ( E ). The maximal expected binding level (Rmax c ) was calculated by Biocore T200 evaluation software and Rmax e value was obtained from experimental maximum response unit. Veh, vehicle. P, precipitation. IB, immunoblotting. WB, western blotting.
    Figure Legend Snippet: ( A ) The structure of biotin-tagged CA (BT-CA), biotin-tagged DMC (BT-DMC), and biotin-tagged DHC (BT-DHC). ( B ) LPS-primed BMDMs were treated with CAPE, BT-CA, BT-DMC, and BT-DHC (10 μM) for 1 hr and then stimulated with monosodium uric acid (MSU) crystals (500 μg/ml) for 6 hr. The cell culture supernatants were analyzed for secreted IL-1β using ELISA. The values represent the means ± SEM (n = 3). # Significantly different from vehicle alone, p < 0.0001. *Significantly different from MSU alone, p < 0.0001. ( C ) After BMDM cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr, cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. The amount of ASC expression in cell lysates were determined as “input”. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( D ) After 293T cells were transfected with ASC-expression plasmids, the cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr. The cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( E ) Sensograms of CAPE binding to recombinant ASC protein in the presence of detergent (0.005% Tween-20) were obtained from surface plasmon resonance (SPR) analysis. Different concentrations of CAPE are presented as an overlay plot aligned at the start of injection. ( F ) The line graph of dose-binding response unit curve and the table showing kinetic parameters of the binding between CAPE and ASC calculated using a simple 1:1 interaction model were from SPR analysis in ( E ). The maximal expected binding level (Rmax c ) was calculated by Biocore T200 evaluation software and Rmax e value was obtained from experimental maximum response unit. Veh, vehicle. P, precipitation. IB, immunoblotting. WB, western blotting.

    Techniques Used: Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot, Expressing, Transfection, Binding Assay, Recombinant, SPR Assay, Injection, Software



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    recombinant human asc protein(abnova)  (Abnova)
    90
    Abnova recombinant human asc protein(abnova)
    ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + <t>ASC</t> + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with <t>recombinant</t> human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).
    Recombinant Human Asc Protein(Abnova), supplied by Abnova, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human asc protein(abnova)/product/Abnova
    Average 90 stars, based on 1 article reviews
    recombinant human asc protein(abnova) - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

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    ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + ASC + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with recombinant human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).

    Journal: Scientific Reports

    Article Title: Targeting ASC in NLRP3 inflammasome by caffeic acid phenethyl ester: a novel strategy to treat acute gout

    doi: 10.1038/srep38622

    Figure Lengend Snippet: ( A–C ) 293T cells were transiently transfected with the iGLuc luciferase reporter plasmid (100 ng) and expression plasmids. Luminescence derived from iGLuc activation in each sample was normalized by β-galactosidase activity transfected as an internal control in each sample. ( A ) *Significantly different from NLRP3 + ASC + caspase-1, 0.5: p = 0.0064, 1–10: p =< 0.0001. ( B ) *Significantly different from ASC + caspase-1, 0.5: p = 0.0036, 1: p = 0.0001, 5–10: p =< 0.0001. ( D ) In vitro assay for caspase-1 enzyme activity was performed using a fluorometric caspase-1 assay kit with recombinant human caspase-1 (rCaspase-1; Bio-vision) in the presence or absence of CAPE or Z-VAD-FMK according to the manufacture’s instruction. The fluorescence was recorded at 400 nm after excitation at 505 nm with SpectraMaxM5 (Molecular Devices, Sunnyvale, CA). *Significantly different from rCaspase-1 alone, p = 0.0007. The values represent the means ± SEM (n = 3).

    Article Snippet: Recombinant human ASC protein(Abnova) was captured with anti-ASC antibodies via antibody-antigen binding.

    Techniques: Transfection, Luciferase, Plasmid Preparation, Expressing, Derivative Assay, Activation Assay, Activity Assay, Control, In Vitro, Recombinant, Fluorescence

    ( A ) The structure of biotin-tagged CA (BT-CA), biotin-tagged DMC (BT-DMC), and biotin-tagged DHC (BT-DHC). ( B ) LPS-primed BMDMs were treated with CAPE, BT-CA, BT-DMC, and BT-DHC (10 μM) for 1 hr and then stimulated with monosodium uric acid (MSU) crystals (500 μg/ml) for 6 hr. The cell culture supernatants were analyzed for secreted IL-1β using ELISA. The values represent the means ± SEM (n = 3). # Significantly different from vehicle alone, p < 0.0001. *Significantly different from MSU alone, p < 0.0001. ( C ) After BMDM cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr, cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. The amount of ASC expression in cell lysates were determined as “input”. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( D ) After 293T cells were transfected with ASC-expression plasmids, the cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr. The cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( E ) Sensograms of CAPE binding to recombinant ASC protein in the presence of detergent (0.005% Tween-20) were obtained from surface plasmon resonance (SPR) analysis. Different concentrations of CAPE are presented as an overlay plot aligned at the start of injection. ( F ) The line graph of dose-binding response unit curve and the table showing kinetic parameters of the binding between CAPE and ASC calculated using a simple 1:1 interaction model were from SPR analysis in ( E ). The maximal expected binding level (Rmax c ) was calculated by Biocore T200 evaluation software and Rmax e value was obtained from experimental maximum response unit. Veh, vehicle. P, precipitation. IB, immunoblotting. WB, western blotting.

    Journal: Scientific Reports

    Article Title: Targeting ASC in NLRP3 inflammasome by caffeic acid phenethyl ester: a novel strategy to treat acute gout

    doi: 10.1038/srep38622

    Figure Lengend Snippet: ( A ) The structure of biotin-tagged CA (BT-CA), biotin-tagged DMC (BT-DMC), and biotin-tagged DHC (BT-DHC). ( B ) LPS-primed BMDMs were treated with CAPE, BT-CA, BT-DMC, and BT-DHC (10 μM) for 1 hr and then stimulated with monosodium uric acid (MSU) crystals (500 μg/ml) for 6 hr. The cell culture supernatants were analyzed for secreted IL-1β using ELISA. The values represent the means ± SEM (n = 3). # Significantly different from vehicle alone, p < 0.0001. *Significantly different from MSU alone, p < 0.0001. ( C ) After BMDM cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr, cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. The amount of ASC expression in cell lysates were determined as “input”. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( D ) After 293T cells were transfected with ASC-expression plasmids, the cell lysates were treated with BT-CA, BT-DMC, and BT-DHC (1 μM) at room temperature for 4 hr. The cell lysates were precipitated with NeutrAvidin beads and subjected to immunoblotting analysis. CAPE (1 μM) was added to cell lysates treated with BT-CA. ( E ) Sensograms of CAPE binding to recombinant ASC protein in the presence of detergent (0.005% Tween-20) were obtained from surface plasmon resonance (SPR) analysis. Different concentrations of CAPE are presented as an overlay plot aligned at the start of injection. ( F ) The line graph of dose-binding response unit curve and the table showing kinetic parameters of the binding between CAPE and ASC calculated using a simple 1:1 interaction model were from SPR analysis in ( E ). The maximal expected binding level (Rmax c ) was calculated by Biocore T200 evaluation software and Rmax e value was obtained from experimental maximum response unit. Veh, vehicle. P, precipitation. IB, immunoblotting. WB, western blotting.

    Article Snippet: Recombinant human ASC protein(Abnova) was captured with anti-ASC antibodies via antibody-antigen binding.

    Techniques: Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot, Expressing, Transfection, Binding Assay, Recombinant, SPR Assay, Injection, Software