lysc  (New England Biolabs)


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    Structured Review

    New England Biolabs lysc
    Lysc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lysc/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lysc - by Bioz Stars, 2022-09
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    New England Biolabs endoproteinase lysc
    Degradation of σ3 by exogenous and intracellular proteases. (A) Exogenous protease. T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions were incubated in virus storage buffer supplemented with <t>endoproteinase</t> <t>LysC</t> for the indicated amounts of time at 37°C. Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown). (B) Intracellular proteases. L cell monolayers were infected with T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions. At the indicated times post infection, the growth medium was supplemented with ammonium chloride. At 24 h post infection, the cells were lysed and viral yield was quantified by plaque assay. The data are presented as means ± SDs (n = 3 independent replicates). AC, ammonium chloride; Unt, untreated.
    Endoproteinase Lysc, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endoproteinase lysc/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    endoproteinase lysc - by Bioz Stars, 2022-09
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    Degradation of σ3 by exogenous and intracellular proteases. (A) Exogenous protease. T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown). (B) Intracellular proteases. L cell monolayers were infected with T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions. At the indicated times post infection, the growth medium was supplemented with ammonium chloride. At 24 h post infection, the cells were lysed and viral yield was quantified by plaque assay. The data are presented as means ± SDs (n = 3 independent replicates). AC, ammonium chloride; Unt, untreated.

    Journal: bioRxiv

    Article Title: Selection and characterization of a reovirus mutant with improved thermostability

    doi: 10.1101/511352

    Figure Lengend Snippet: Degradation of σ3 by exogenous and intracellular proteases. (A) Exogenous protease. T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown). (B) Intracellular proteases. L cell monolayers were infected with T1L, T1L μ1 M258I, T1L σ3 S344P, or T1L μ1 M258I σ3 S344P virions. At the indicated times post infection, the growth medium was supplemented with ammonium chloride. At 24 h post infection, the cells were lysed and viral yield was quantified by plaque assay. The data are presented as means ± SDs (n = 3 independent replicates). AC, ammonium chloride; Unt, untreated.

    Article Snippet: To determine if HR mutations alter disassembly kinetics, virions were digested in vitro with endoproteinase LysC (EKC).

    Techniques: Incubation, SDS Page, Staining, Infection, Plaque Assay

    Thermostability of a T1L/T3D M2 variant. (A) Protein compositions. T1L/T3D M2 and T1L/T3D M2 μ1 M258I σ3 S344P virions and ISVPs were analyzed by SDS-PAGE. The gel was Coomassie brilliant blue stained. The migration of capsid proteins is indicated on the left. μ1 resolves as μ1C, and μ1δ resolves as δ ( 33 ). μ1N and Φ are too small to resolve on the gel (n = 3 independent replicates; results from 1 representative experiment are shown). (B) Size distribution profiles. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions or ISVPs were analyzed by dynamic light scattering. For each variant, the virion (black) and ISVP (gray) size distribution profiles are overlaid (n = 3 independent replicates; results from 1 representative experiment are shown). (C) Thermal inactivation. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions or ISVPs were incubated in virus storage for 5 min at the indicated temperatures. The change in infectivity relative to samples incubated at 4°C was determined by plaque assay. The data are presented as means ± SDs. *, P ≤ 0.05 and difference in change in infectivity ≥ 2 log 10 units (n = 3 independent replicates). (D) Degradation of σ3 by exogenous protease. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown).

    Journal: bioRxiv

    Article Title: Selection and characterization of a reovirus mutant with improved thermostability

    doi: 10.1101/511352

    Figure Lengend Snippet: Thermostability of a T1L/T3D M2 variant. (A) Protein compositions. T1L/T3D M2 and T1L/T3D M2 μ1 M258I σ3 S344P virions and ISVPs were analyzed by SDS-PAGE. The gel was Coomassie brilliant blue stained. The migration of capsid proteins is indicated on the left. μ1 resolves as μ1C, and μ1δ resolves as δ ( 33 ). μ1N and Φ are too small to resolve on the gel (n = 3 independent replicates; results from 1 representative experiment are shown). (B) Size distribution profiles. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions or ISVPs were analyzed by dynamic light scattering. For each variant, the virion (black) and ISVP (gray) size distribution profiles are overlaid (n = 3 independent replicates; results from 1 representative experiment are shown). (C) Thermal inactivation. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions or ISVPs were incubated in virus storage for 5 min at the indicated temperatures. The change in infectivity relative to samples incubated at 4°C was determined by plaque assay. The data are presented as means ± SDs. *, P ≤ 0.05 and difference in change in infectivity ≥ 2 log 10 units (n = 3 independent replicates). (D) Degradation of σ3 by exogenous protease. T1L/T3D M2 or T1L/T3D M2 μ1 M258I σ3 S344P virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown).

    Article Snippet: To determine if HR mutations alter disassembly kinetics, virions were digested in vitro with endoproteinase LysC (EKC).

    Techniques: Variant Assay, SDS Page, Staining, Migration, Incubation, Infection, Plaque Assay

    Degradation of reovirus σ3 by exogenous and intracellular proteases. (A and B) Exogenous proteases. T1L, T1L/T3D M2, or T3D/T1L S4 virions were incubated in virus storage buffer supplemented with trypsin (A) or endoproteinase LysC (EKC) (B) for the indicated amounts of time at 8°C (trypsin incubation) or 37°C (EKC incubation). After digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = three independent replicates; results from one representative experiment are shown). (C) Intracellular proteases. L cell monolayers were infected with T1L, T1L/T3D M2, or T3D/T1L S4 virions. At the indicated times postinfection, the growth medium was supplemented with ammonium chloride. At 24 h postinfection, the cells were lysed, and viral yield was quantified by plaque assay. The data are presented as means ± the SD ( n = three independent replicates). AC, ammonium chloride; Unt, untreated.

    Journal: Journal of Virology

    Article Title: Components of the Reovirus Capsid Differentially Contribute to Stability

    doi: 10.1128/JVI.01894-18

    Figure Lengend Snippet: Degradation of reovirus σ3 by exogenous and intracellular proteases. (A and B) Exogenous proteases. T1L, T1L/T3D M2, or T3D/T1L S4 virions were incubated in virus storage buffer supplemented with trypsin (A) or endoproteinase LysC (EKC) (B) for the indicated amounts of time at 8°C (trypsin incubation) or 37°C (EKC incubation). After digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = three independent replicates; results from one representative experiment are shown). (C) Intracellular proteases. L cell monolayers were infected with T1L, T1L/T3D M2, or T3D/T1L S4 virions. At the indicated times postinfection, the growth medium was supplemented with ammonium chloride. At 24 h postinfection, the cells were lysed, and viral yield was quantified by plaque assay. The data are presented as means ± the SD ( n = three independent replicates). AC, ammonium chloride; Unt, untreated.

    Article Snippet: T1L, T1L/T3D M2, or T3D/T1L S4 virions (2 × 1012 particles/ml) were incubated in the presence of 5 μg/ml trypsin (Sigma-Aldrich) or 10 μg/ml endoproteinase LysC (EKC; New England Biolabs) at 8°C (trypsin digestion) or 37°C (EKC digestion) in an S1000 thermal cycler (Bio-Rad).

    Techniques: Incubation, SDS Page, Staining, Infection, Plaque Assay

    Degradation of σ3 by exogenous or intracellular protease. (A) Exogenous protease. T1L, T1L (μ1 M258I), T1L (σ3 S344P), or T1L (μ1 M258I, σ3 S344P) virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. 0+ time points were quenched immediately after mixing. Following digestion, equal particle numbers were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = 3 independent replicates; results from 1 representative experiment are shown). (B) Intracellular proteases. L cell monolayers were infected with T1L, T1L (μ1 M258I), T1L (σ3 S344P), or T1L (μ1 M258I, σ3 S344P) virions. At the indicated times postinfection, the growth medium was supplemented with ammonium chloride. At 24 h postinfection, the cells were lysed and viral yield was quantified by plaque assay. The data are presented as means ± SD ( n = 3 independent replicates). Unt, untreated.

    Journal: Journal of Virology

    Article Title: Selection and Characterization of a Reovirus Mutant with Increased Thermostability

    doi: 10.1128/JVI.00247-19

    Figure Lengend Snippet: Degradation of σ3 by exogenous or intracellular protease. (A) Exogenous protease. T1L, T1L (μ1 M258I), T1L (σ3 S344P), or T1L (μ1 M258I, σ3 S344P) virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. 0+ time points were quenched immediately after mixing. Following digestion, equal particle numbers were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = 3 independent replicates; results from 1 representative experiment are shown). (B) Intracellular proteases. L cell monolayers were infected with T1L, T1L (μ1 M258I), T1L (σ3 S344P), or T1L (μ1 M258I, σ3 S344P) virions. At the indicated times postinfection, the growth medium was supplemented with ammonium chloride. At 24 h postinfection, the cells were lysed and viral yield was quantified by plaque assay. The data are presented as means ± SD ( n = 3 independent replicates). Unt, untreated.

    Article Snippet: T1L, T1L/T3D M2, T1L (μ1 M258I), T1L (σ3 S344P), T1L (μ1 M258I, σ3 S344P), or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions (2 × 1012 particles/ml) were incubated in the presence of 10 μg/ml endoproteinase LysC (New England Biolabs) at 37°C in an S1000 thermal cycler (Bio-Rad).

    Techniques: Incubation, SDS Page, Staining, Infection, Plaque Assay

    ). μ1N and Φ are too small to resolve on the gel ( n = 3 independent replicates; results from 1 representative experiment are shown). (B) Size distribution profiles. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions or ISVPs were analyzed by dynamic light scattering. For each variant, the virion (black) and ISVP (gray) size distribution profiles are overlaid ( n = 3 independent replicates; results from 1 representative experiment are shown). (C) Thermal inactivation. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions or ISVPs were incubated in virus storage buffer for 5 min at the indicated temperatures. The change in infectivity relative to that of samples incubated at 4°C was determined by plaque assay. The data are presented as means ± SD. *, P ≤ 0.05 and difference in change in infectivity of ≥2 log 10 units ( n = 3 independent replicates). (D) Degradation of σ3 by exogenous protease. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. 0+ time points were quenched immediately after mixing. Following digestion, equal particle numbers were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = 3 independent replicates; results from 1 representative experiment are shown).

    Journal: Journal of Virology

    Article Title: Selection and Characterization of a Reovirus Mutant with Increased Thermostability

    doi: 10.1128/JVI.00247-19

    Figure Lengend Snippet: ). μ1N and Φ are too small to resolve on the gel ( n = 3 independent replicates; results from 1 representative experiment are shown). (B) Size distribution profiles. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions or ISVPs were analyzed by dynamic light scattering. For each variant, the virion (black) and ISVP (gray) size distribution profiles are overlaid ( n = 3 independent replicates; results from 1 representative experiment are shown). (C) Thermal inactivation. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions or ISVPs were incubated in virus storage buffer for 5 min at the indicated temperatures. The change in infectivity relative to that of samples incubated at 4°C was determined by plaque assay. The data are presented as means ± SD. *, P ≤ 0.05 and difference in change in infectivity of ≥2 log 10 units ( n = 3 independent replicates). (D) Degradation of σ3 by exogenous protease. T1L/T3D M2 or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions were incubated in virus storage buffer supplemented with endoproteinase LysC for the indicated amounts of time at 37°C. 0+ time points were quenched immediately after mixing. Following digestion, equal particle numbers were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained ( n = 3 independent replicates; results from 1 representative experiment are shown).

    Article Snippet: T1L, T1L/T3D M2, T1L (μ1 M258I), T1L (σ3 S344P), T1L (μ1 M258I, σ3 S344P), or T1L (σ3 S344P)/T3D M2 (μ1 M258I) virions (2 × 1012 particles/ml) were incubated in the presence of 10 μg/ml endoproteinase LysC (New England Biolabs) at 37°C in an S1000 thermal cycler (Bio-Rad).

    Techniques: Variant Assay, Incubation, Infection, Plaque Assay, SDS Page, Staining

    Degradation of the σ3 outer capsid protein by exogenous and intracellular proteases. (A and B) Exogenous proteases. T1L or T1L/T3D M2 virions were incubated in virus storage buffer supplemented with trypsin (A) or endoproteinase LysC (B) for the indicated amounts of time at 8°C (trypsin incubation) or 37°C (endoproteinase LysC incubation). Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown). (C) Intracellular proteases. L cell monolayers were infected with T1L or T1L/T3D M2 virions. At the indicated times post infection, the growth medium was supplemented with ammonium chloride. At 24 h post infection, the cells were lysed and viral yield was quantified by plaque assay. Data are presented as means ± SDs (n = 3 independent replicates). AC, ammonium chloride; Unt, untreated.

    Journal: bioRxiv

    Article Title: The reovirus μ1 protein contributes to the environmental stability of virions

    doi: 10.1101/357343

    Figure Lengend Snippet: Degradation of the σ3 outer capsid protein by exogenous and intracellular proteases. (A and B) Exogenous proteases. T1L or T1L/T3D M2 virions were incubated in virus storage buffer supplemented with trypsin (A) or endoproteinase LysC (B) for the indicated amounts of time at 8°C (trypsin incubation) or 37°C (endoproteinase LysC incubation). Following digestion, equal particle numbers from each time point were analyzed by SDS-PAGE. The gels were Coomassie brilliant blue stained (n = 3 independent replicates; results from 1 representative experiment are shown). (C) Intracellular proteases. L cell monolayers were infected with T1L or T1L/T3D M2 virions. At the indicated times post infection, the growth medium was supplemented with ammonium chloride. At 24 h post infection, the cells were lysed and viral yield was quantified by plaque assay. Data are presented as means ± SDs (n = 3 independent replicates). AC, ammonium chloride; Unt, untreated.

    Article Snippet: Degradation of σ3 by exogenous proteases T1L or T1L/T3D M2 virions (2×1012 particles/ml) were incubated in the presence of 5 μg/ml trypsin (Sigma-Aldrich) or 10 μg/ml endoproteinase LysC (EKC) (New England Biolabs) at 8°C (trypsin digestion) or 37°C (EKC digestion) in a S1000 thermal cycler (Bio-Rad).

    Techniques: Incubation, SDS Page, Staining, Infection, Plaque Assay