protease inhibitor cocktail  (Millipore)


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    Name:
    Protease Inhibitor Cocktail
    Description:

    Catalog Number:
    p8340
    Price:
    None
    Applications:
    Protease Inhibitor Cocktail has been used-. as a buffer component during sonication of GFP (green fluorescent protein)-huntingtin-transfected HEK 293 cells in GST (glutathione S-transferase) pull down assay. as a component of lysis buffer. as a component of radioimmunoprecipitation assay buffer (RIPA)
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    Structured Review

    Millipore protease inhibitor cocktail

    https://www.bioz.com/result/protease inhibitor cocktail/product/Millipore
    Average 99 stars, based on 2193 article reviews
    Price from $9.99 to $1999.99
    protease inhibitor cocktail - by Bioz Stars, 2021-01
    99/100 stars

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    Related Articles

    Sonication:

    Article Title: G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear RNA-binding protein regulated by protein kinase A
    Article Snippet: .. Two wells with 293T cells were washed in PBS and lysed by sonication in immunoprecipitation buffer (150 mM NaCl, 50 mM Tris pH 7.5, 0.5% Triton X-100, 1 × protease inhibitor cocktail (Sigma P8340), 1 mM PMSF (Sigma P7626) and 1 mM Na3 VO4 (Sigma S6508)). .. The lysates were cleared by centrifugation and adjusted to equal protein concentration (between 2.5 - 3.0 μg protein/μl) by the Bradford method (BioRad 500-0006).

    Article Title: Role of the carboxyl terminal di-leucine in phosphorylation and internalization of C5a receptor
    Article Snippet: .. After the experiment, cells were briefly washed with ice-cold PBS, collected in PBS with protease inhibitor cocktail III (Calbiochem) and sonicated briefly. .. Protein samples were lysed in Laemmli sample buffer, heated at 60°C for 15 min, separated on 8% or 10% SDS-polyacrylamide gel, and transferred to a 0.45 μm nitrocellulose membrane using a semi-wet unit (Bio-Rad).

    Protease Inhibitor:

    Article Title: G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear RNA-binding protein regulated by protein kinase A
    Article Snippet: .. Two wells with 293T cells were washed in PBS and lysed by sonication in immunoprecipitation buffer (150 mM NaCl, 50 mM Tris pH 7.5, 0.5% Triton X-100, 1 × protease inhibitor cocktail (Sigma P8340), 1 mM PMSF (Sigma P7626) and 1 mM Na3 VO4 (Sigma S6508)). .. The lysates were cleared by centrifugation and adjusted to equal protein concentration (between 2.5 - 3.0 μg protein/μl) by the Bradford method (BioRad 500-0006).

    Article Title: The serine protease hepsin mediates urinary secretion and polymerisation of Zona Pellucida domain protein uromodulin
    Article Snippet: .. After 24 h, the medium was replaced with Optimem supplemented with 0.1% protease inhibitor cocktail (PIC) (P8340, Sigma-Aldrich, Saint Louis, MO), 0.1% DMSO, 0.1 mM AEBSF, 0.08 μM aprotinin, 1.4 μM E64, 4 μM bestatin, 2 μM leupeptin and 1.5 μM pepstatin A (Sigma-Aldrich). .. Immunofluorescence analysis was performed after 24 hr of treatment.

    Article Title: Chemically monoubiquitinated PEX5 binds to the components of the peroxisomal docking and export machinery
    Article Snippet: .. For cytosol extraction four to seven 175 cm2 culture flasks of 90% confluent ΔPEX5 fibroblasts were harvested and resuspended in cytosol extraction buffer (20 mM HEPES, 150 mM NaCl, 5 mM imidazole, 20% glycerol, pH 7.4, protease inhibitor cocktail (PI) (Sigma; 1:200)). ..

    Article Title: Schistosoma mansoni Infection of Mice, Rats and Humans Elicits a Strong Antibody Response to a Limited Number of Reduction-Sensitive Epitopes on Five Major Tegumental Membrane Proteins
    Article Snippet: .. Recombinant insect cell pellets were either solubilized directly into non-reducing SDS Laemmli buffer (BioRad), or for use in western blot competition studies, we employed a non-reducing insect cell lysis buffer (1% Triton-X-100, 10mM Tris pH 8.0, 140 mM NaCl, 1x Sigma protease inhibitor cocktail). .. Production of recombinant schistosome membrane proteins in E . coli DNA encoding the predicted extracellular domains of SmLy6B, C, F, SmTsp-2, and Sm29 was amplified by PCR and ligated into a pET32 E. coli expression plasmid in frame with the E . coli thioredoxin (Trx) coding DNA and containing hexahistidine and epitope tags.

    Article Title: Amyloid-?1–42 Slows Clearance of Synaptically Released Glutamate by Mislocalizing Astrocytic GLT-1
    Article Snippet: .. Protein lysates from slices and cultured astrocytes were prepared using 1% Triton X-100 buffer [in m m : 20 Tris, 1 EDTA, 0.5 EGTA, 250 sucrose, Protease Inhibitor Cocktail (EMD Millipore)]. .. Lysate protein concentrations were determined by bicinchoninic acid assay (Thermo Scientific).

    Article Title: The C-Terminal Extension Unique to the Long Isoform of the Shelterin Component TIN2 Enhances Its Interaction with TRF2 in a Phosphorylation- and Dyskeratosis Congenita Cluster-Dependent Fashion
    Article Snippet: .. Cells were resuspended in ice-cold lysis buffer (50 mM Tris-HCl at pH 7.5, 1 mM EDTA, 400 mM NaCl, 1% Triton X-100, 0.1% SDS, 1 mM dithiothreitol [DTT], 1 mM phenylmethylsulfonyl fluoride [PMSF], and 1× protease inhibitor cocktail III [Calbiochem]) and incubated for 10 min on ice prior to addition of an equal amount of ice-cold water. .. Protein concentration was determined using the bicinchoninic acid (BCA) protein assay kit (Pierce).

    Article Title: Role of the carboxyl terminal di-leucine in phosphorylation and internalization of C5a receptor
    Article Snippet: .. After the experiment, cells were briefly washed with ice-cold PBS, collected in PBS with protease inhibitor cocktail III (Calbiochem) and sonicated briefly. .. Protein samples were lysed in Laemmli sample buffer, heated at 60°C for 15 min, separated on 8% or 10% SDS-polyacrylamide gel, and transferred to a 0.45 μm nitrocellulose membrane using a semi-wet unit (Bio-Rad).

    Cell Culture:

    Article Title: Amyloid-?1–42 Slows Clearance of Synaptically Released Glutamate by Mislocalizing Astrocytic GLT-1
    Article Snippet: .. Protein lysates from slices and cultured astrocytes were prepared using 1% Triton X-100 buffer [in m m : 20 Tris, 1 EDTA, 0.5 EGTA, 250 sucrose, Protease Inhibitor Cocktail (EMD Millipore)]. .. Lysate protein concentrations were determined by bicinchoninic acid assay (Thermo Scientific).

    Immunoprecipitation:

    Article Title: G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear RNA-binding protein regulated by protein kinase A
    Article Snippet: .. Two wells with 293T cells were washed in PBS and lysed by sonication in immunoprecipitation buffer (150 mM NaCl, 50 mM Tris pH 7.5, 0.5% Triton X-100, 1 × protease inhibitor cocktail (Sigma P8340), 1 mM PMSF (Sigma P7626) and 1 mM Na3 VO4 (Sigma S6508)). .. The lysates were cleared by centrifugation and adjusted to equal protein concentration (between 2.5 - 3.0 μg protein/μl) by the Bradford method (BioRad 500-0006).

    Incubation:

    Article Title: The C-Terminal Extension Unique to the Long Isoform of the Shelterin Component TIN2 Enhances Its Interaction with TRF2 in a Phosphorylation- and Dyskeratosis Congenita Cluster-Dependent Fashion
    Article Snippet: .. Cells were resuspended in ice-cold lysis buffer (50 mM Tris-HCl at pH 7.5, 1 mM EDTA, 400 mM NaCl, 1% Triton X-100, 0.1% SDS, 1 mM dithiothreitol [DTT], 1 mM phenylmethylsulfonyl fluoride [PMSF], and 1× protease inhibitor cocktail III [Calbiochem]) and incubated for 10 min on ice prior to addition of an equal amount of ice-cold water. .. Protein concentration was determined using the bicinchoninic acid (BCA) protein assay kit (Pierce).

    Western Blot:

    Article Title: Schistosoma mansoni Infection of Mice, Rats and Humans Elicits a Strong Antibody Response to a Limited Number of Reduction-Sensitive Epitopes on Five Major Tegumental Membrane Proteins
    Article Snippet: .. Recombinant insect cell pellets were either solubilized directly into non-reducing SDS Laemmli buffer (BioRad), or for use in western blot competition studies, we employed a non-reducing insect cell lysis buffer (1% Triton-X-100, 10mM Tris pH 8.0, 140 mM NaCl, 1x Sigma protease inhibitor cocktail). .. Production of recombinant schistosome membrane proteins in E . coli DNA encoding the predicted extracellular domains of SmLy6B, C, F, SmTsp-2, and Sm29 was amplified by PCR and ligated into a pET32 E. coli expression plasmid in frame with the E . coli thioredoxin (Trx) coding DNA and containing hexahistidine and epitope tags.

    Lysis:

    Article Title: Schistosoma mansoni Infection of Mice, Rats and Humans Elicits a Strong Antibody Response to a Limited Number of Reduction-Sensitive Epitopes on Five Major Tegumental Membrane Proteins
    Article Snippet: .. Recombinant insect cell pellets were either solubilized directly into non-reducing SDS Laemmli buffer (BioRad), or for use in western blot competition studies, we employed a non-reducing insect cell lysis buffer (1% Triton-X-100, 10mM Tris pH 8.0, 140 mM NaCl, 1x Sigma protease inhibitor cocktail). .. Production of recombinant schistosome membrane proteins in E . coli DNA encoding the predicted extracellular domains of SmLy6B, C, F, SmTsp-2, and Sm29 was amplified by PCR and ligated into a pET32 E. coli expression plasmid in frame with the E . coli thioredoxin (Trx) coding DNA and containing hexahistidine and epitope tags.

    Article Title: The C-Terminal Extension Unique to the Long Isoform of the Shelterin Component TIN2 Enhances Its Interaction with TRF2 in a Phosphorylation- and Dyskeratosis Congenita Cluster-Dependent Fashion
    Article Snippet: .. Cells were resuspended in ice-cold lysis buffer (50 mM Tris-HCl at pH 7.5, 1 mM EDTA, 400 mM NaCl, 1% Triton X-100, 0.1% SDS, 1 mM dithiothreitol [DTT], 1 mM phenylmethylsulfonyl fluoride [PMSF], and 1× protease inhibitor cocktail III [Calbiochem]) and incubated for 10 min on ice prior to addition of an equal amount of ice-cold water. .. Protein concentration was determined using the bicinchoninic acid (BCA) protein assay kit (Pierce).

    Recombinant:

    Article Title: Schistosoma mansoni Infection of Mice, Rats and Humans Elicits a Strong Antibody Response to a Limited Number of Reduction-Sensitive Epitopes on Five Major Tegumental Membrane Proteins
    Article Snippet: .. Recombinant insect cell pellets were either solubilized directly into non-reducing SDS Laemmli buffer (BioRad), or for use in western blot competition studies, we employed a non-reducing insect cell lysis buffer (1% Triton-X-100, 10mM Tris pH 8.0, 140 mM NaCl, 1x Sigma protease inhibitor cocktail). .. Production of recombinant schistosome membrane proteins in E . coli DNA encoding the predicted extracellular domains of SmLy6B, C, F, SmTsp-2, and Sm29 was amplified by PCR and ligated into a pET32 E. coli expression plasmid in frame with the E . coli thioredoxin (Trx) coding DNA and containing hexahistidine and epitope tags.

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  • 99
    Millipore complete protease
    PIP2 and PIP3 bind with and inhibit gelsolin. a Actin-depolymerization assay showing identical inhibition of gelsolin by equimolar PIP2 and PIP3 in an in vitro lysate-free assay. b <t>Complete</t> model of human gelsolin structure illustrating its 6 domains (G1-G6) and the C-terminal tail. c , d Molecular modeling illustrating potential sites of interaction of the N-terminus ( c ) and C-terminus ( d ) of gelsolin with PIP2. e , f Molecular modeling illustrating potential sites of interaction of the N-terminus ( e ) and C-terminus ( f ) of gelsolin with PIP3. Please also see Supplementary Movies 1 – 4 . Data represent means ± s.e.m. $ P
    Complete Protease, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/complete protease/product/Millipore
    Average 99 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    complete protease - by Bioz Stars, 2021-01
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    99
    Millipore protease inhibitor cocktail iii
    The protein complementation assay confirms the effects of the R282H mutation and a phosphorylation site mutation on TIN2L interaction with TRF2. (A) Quantification of fluorescence from coexpression of V1-TRF2 with TIN2L-V2, TIN2L-D391K+D395K-V2, or TIN2L-R282H-V2. Error bars represent the <t>SDs</t> from <t>three</t> separate transfections each measured in triplicate. *, P
    Protease Inhibitor Cocktail Iii, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 266 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protease inhibitor cocktail iii/product/Millipore
    Average 99 stars, based on 266 article reviews
    Price from $9.99 to $1999.99
    protease inhibitor cocktail iii - by Bioz Stars, 2021-01
    99/100 stars
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    99
    Millipore protease inhibitor cocktail set iii
    Coinfection with H. polygyrus increases neutrophil transepithelial migration into the P. aeruginosa infected airspace of the lung. FACS analysis using Ly6G and CD11b markers to isolate the neutrophil population in the ( a ) <t>BAL,</t> ( b ) lung tissue and ( c ) peripheral blood (PB), data are shown as mean ± SD, and are representative of <t>three</t> independent experiments. * P
    Protease Inhibitor Cocktail Set Iii, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 350 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protease inhibitor cocktail set iii/product/Millipore
    Average 99 stars, based on 350 article reviews
    Price from $9.99 to $1999.99
    protease inhibitor cocktail set iii - by Bioz Stars, 2021-01
    99/100 stars
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    PIP2 and PIP3 bind with and inhibit gelsolin. a Actin-depolymerization assay showing identical inhibition of gelsolin by equimolar PIP2 and PIP3 in an in vitro lysate-free assay. b Complete model of human gelsolin structure illustrating its 6 domains (G1-G6) and the C-terminal tail. c , d Molecular modeling illustrating potential sites of interaction of the N-terminus ( c ) and C-terminus ( d ) of gelsolin with PIP2. e , f Molecular modeling illustrating potential sites of interaction of the N-terminus ( e ) and C-terminus ( f ) of gelsolin with PIP3. Please also see Supplementary Movies 1 – 4 . Data represent means ± s.e.m. $ P

    Journal: Nature Communications

    Article Title: PI3Kα-regulated gelsolin activity is a critical determinant of cardiac cytoskeletal remodeling and heart disease

    doi: 10.1038/s41467-018-07812-8

    Figure Lengend Snippet: PIP2 and PIP3 bind with and inhibit gelsolin. a Actin-depolymerization assay showing identical inhibition of gelsolin by equimolar PIP2 and PIP3 in an in vitro lysate-free assay. b Complete model of human gelsolin structure illustrating its 6 domains (G1-G6) and the C-terminal tail. c , d Molecular modeling illustrating potential sites of interaction of the N-terminus ( c ) and C-terminus ( d ) of gelsolin with PIP2. e , f Molecular modeling illustrating potential sites of interaction of the N-terminus ( e ) and C-terminus ( f ) of gelsolin with PIP3. Please also see Supplementary Movies 1 – 4 . Data represent means ± s.e.m. $ P

    Article Snippet: Tissue and cellular proteins were prepared in phosphate buffered saline (137 mM NaCl, 2.7 mM KCl, 10 mM Na2 HPO4 and 1.8 mM KH2 PO4 ) pH 7.4 with 1× cOmplete Protease (#11697498001, Millipore Sigma) and PhosSTOP Phosphatase (#4906845001, Millipore Sigma) inhibitor cocktails.

    Techniques: Inhibition, In Vitro

    SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) Complete or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.

    Journal: bioRxiv

    Article Title: The specificity of SRC Homology 3 (SH3) domain interactions is modulated by their protein context in vivo

    doi: 10.1101/2020.05.18.103002

    Figure Lengend Snippet: SH3 domains shuffling impacts Sla1 PPIs, cells growth in different stress conditions and clathrin-mediated endocytosis. A) Sla1 SH3-deleted or -shuffled PPIs as detected by DHFR-PCA. The color code represents PPI strength as detected by DHFR-PCA (PCA score). All PPIs were measured in quadruplicate. A is for Abp1 SH3 and * is for the reinsertion of the WT domain as control strains. A scaled cartoon of Sla1 is also illustrated. B) Cophenetic correlation for the similarity of Sla1 SH3-shuffled PPI clusters with the growth phenotype clusters. Empirical p-value obtained from data permutation is p = 0.00002. C) Representative fluorescence microscopy timeframe analysis of a yeast cell expressing WT Sla1-GFP. The calculated trajectories for every Sla1-GFP foci detected are shown. Cell membrane is delimited with a dashed line and each Sla1-GFP particle colors represent its position in time. D) Sla1-GFP particles average effective distance travelled towards the cell center through time. Sla1 SH3-deleted strains are shown. The proportion of events that are not completed yet is represented by the color transparency of the curves (+ represent the time point when 95% of foci have disassembled). E) Complete or incomplete Sla1-GFP endocytosis events are shown (average per cell) for Sla1 SH3-deleted strains. F) Representation of the linearity of Sla1-GFP particle trajectories for each SH3 deletion or shuffling. G) Sla1-GFP particle lifetime (in seconds) are shown for the same strains as in F). See also Data S5.

    Article Snippet: Bacteria were thawed in GST buffer (20 mM Tris-HCl pH 7.5, 0.5 M NaCl, 1 mM EDTA and 1 mM DTT (Millipore Sigma)) with cOmplete protease inhibitors (Millipore Sigma) and disrupted with sonication.

    Techniques: Fluorescence, Microscopy, Expressing

    Sla1 SH3 domain shuffling greatly alters its interactome in vivo with strong impacts on endocytosis. A) PPIs detected by DHFR-PCA relative to Sla1 WT for SH3-shuffling or -deletion per SH3 position. PPIs were measured in quadruplicate. B) Scaled cartoon representation of Sla1 and illustration of Sla1 function as an adaptor linking early proteins with the actin machinery in yeast clathrin-mediated endocytosis. C) PPIs of Sla1 SH3-shuffled or -deleted with partners implicated in clathrin-mediated endocytosis. Each PPI was assessed in quadruplicate by DHFR-PCA. The color code represents the strength of the PPIs detected by DHFR-PCA (PCA score). Sla1 1|2|3 represents the WT protein. D) Schematic representation of Sla1 foci assembled at the cell membrane and their movement toward the center of the cell during internalization before disassembly, in time. E) Representative fluorescence microscopy images of cells expressing different Sla1-GFP proteins at multiple time points. Foci from WT Sla1-GFP, the negative control D|D|D and a Sla1-GFP shuffle (3|1|2) are shown, in time. The first time frame is green and the others are red. A merge with the starting point is shown for each time frame. F) Average effective distance travelled by Sla1-GFP particles towards the centroid of the cell through time for WT Sla1 (1|2|3), SH3-deleted control or shuffled strains. Color transparency represents the proportion of events that are not completed yet that are used to calculate the average distance at the different time points. Plus signs (+) represent the moment in time when 95% of the foci have disassembled. G) Average number of complete or incomplete Sla1-GFP endocytosis events per cell is shown. See also Figure S5 and Data S5.

    Journal: bioRxiv

    Article Title: The specificity of SRC Homology 3 (SH3) domain interactions is modulated by their protein context in vivo

    doi: 10.1101/2020.05.18.103002

    Figure Lengend Snippet: Sla1 SH3 domain shuffling greatly alters its interactome in vivo with strong impacts on endocytosis. A) PPIs detected by DHFR-PCA relative to Sla1 WT for SH3-shuffling or -deletion per SH3 position. PPIs were measured in quadruplicate. B) Scaled cartoon representation of Sla1 and illustration of Sla1 function as an adaptor linking early proteins with the actin machinery in yeast clathrin-mediated endocytosis. C) PPIs of Sla1 SH3-shuffled or -deleted with partners implicated in clathrin-mediated endocytosis. Each PPI was assessed in quadruplicate by DHFR-PCA. The color code represents the strength of the PPIs detected by DHFR-PCA (PCA score). Sla1 1|2|3 represents the WT protein. D) Schematic representation of Sla1 foci assembled at the cell membrane and their movement toward the center of the cell during internalization before disassembly, in time. E) Representative fluorescence microscopy images of cells expressing different Sla1-GFP proteins at multiple time points. Foci from WT Sla1-GFP, the negative control D|D|D and a Sla1-GFP shuffle (3|1|2) are shown, in time. The first time frame is green and the others are red. A merge with the starting point is shown for each time frame. F) Average effective distance travelled by Sla1-GFP particles towards the centroid of the cell through time for WT Sla1 (1|2|3), SH3-deleted control or shuffled strains. Color transparency represents the proportion of events that are not completed yet that are used to calculate the average distance at the different time points. Plus signs (+) represent the moment in time when 95% of the foci have disassembled. G) Average number of complete or incomplete Sla1-GFP endocytosis events per cell is shown. See also Figure S5 and Data S5.

    Article Snippet: Bacteria were thawed in GST buffer (20 mM Tris-HCl pH 7.5, 0.5 M NaCl, 1 mM EDTA and 1 mM DTT (Millipore Sigma)) with cOmplete protease inhibitors (Millipore Sigma) and disrupted with sonication.

    Techniques: In Vivo, Fluorescence, Microscopy, Expressing, Negative Control

    The protein complementation assay confirms the effects of the R282H mutation and a phosphorylation site mutation on TIN2L interaction with TRF2. (A) Quantification of fluorescence from coexpression of V1-TRF2 with TIN2L-V2, TIN2L-D391K+D395K-V2, or TIN2L-R282H-V2. Error bars represent the SDs from three separate transfections each measured in triplicate. *, P

    Journal: Molecular and Cellular Biology

    Article Title: The C-Terminal Extension Unique to the Long Isoform of the Shelterin Component TIN2 Enhances Its Interaction with TRF2 in a Phosphorylation- and Dyskeratosis Congenita Cluster-Dependent Fashion

    doi: 10.1128/MCB.00025-18

    Figure Lengend Snippet: The protein complementation assay confirms the effects of the R282H mutation and a phosphorylation site mutation on TIN2L interaction with TRF2. (A) Quantification of fluorescence from coexpression of V1-TRF2 with TIN2L-V2, TIN2L-D391K+D395K-V2, or TIN2L-R282H-V2. Error bars represent the SDs from three separate transfections each measured in triplicate. *, P

    Article Snippet: Cells were resuspended in ice-cold lysis buffer (50 mM Tris-HCl at pH 7.5, 1 mM EDTA, 400 mM NaCl, 1% Triton X-100, 0.1% SDS, 1 mM dithiothreitol [DTT], 1 mM phenylmethylsulfonyl fluoride [PMSF], and 1× protease inhibitor cocktail III [Calbiochem]) and incubated for 10 min on ice prior to addition of an equal amount of ice-cold water.

    Techniques: Mutagenesis, Fluorescence, Transfection

    Coinfection with H. polygyrus increases neutrophil transepithelial migration into the P. aeruginosa infected airspace of the lung. FACS analysis using Ly6G and CD11b markers to isolate the neutrophil population in the ( a ) BAL, ( b ) lung tissue and ( c ) peripheral blood (PB), data are shown as mean ± SD, and are representative of three independent experiments. * P

    Journal: Scientific Reports

    Article Title: Intestinal helminth infection enhances bacteria-induced recruitment of neutrophils to the airspace

    doi: 10.1038/s41598-019-51991-3

    Figure Lengend Snippet: Coinfection with H. polygyrus increases neutrophil transepithelial migration into the P. aeruginosa infected airspace of the lung. FACS analysis using Ly6G and CD11b markers to isolate the neutrophil population in the ( a ) BAL, ( b ) lung tissue and ( c ) peripheral blood (PB), data are shown as mean ± SD, and are representative of three independent experiments. * P

    Article Snippet: For protein lysate samples, one of the 0.5 mL BAL aliquots was treated with 10 μL protease inhibitor cocktail set III, EDTA-free (Calbiochem, MA) and 20 μl of 10% Triton X-100 (Sigma, MA) and mixed by inversion for 20 minutes at 4 °C.

    Techniques: Migration, Infection, FACS

    Helminth-induced increase in neutrophil migration during P. aeruginosa infection is correlated with increased MPO and ELA2 levels within the airspace. Protein extracts were prepared from BAL samples and analyzed for ( a ) neutrophil myeloperoxidase (MPO) and ( b ) elastase (ELA2). ( c ) LDH levels were assessed in the cell-free supernatant of the BAL to assess cytotoxicity. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Journal: Scientific Reports

    Article Title: Intestinal helminth infection enhances bacteria-induced recruitment of neutrophils to the airspace

    doi: 10.1038/s41598-019-51991-3

    Figure Lengend Snippet: Helminth-induced increase in neutrophil migration during P. aeruginosa infection is correlated with increased MPO and ELA2 levels within the airspace. Protein extracts were prepared from BAL samples and analyzed for ( a ) neutrophil myeloperoxidase (MPO) and ( b ) elastase (ELA2). ( c ) LDH levels were assessed in the cell-free supernatant of the BAL to assess cytotoxicity. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Article Snippet: For protein lysate samples, one of the 0.5 mL BAL aliquots was treated with 10 μL protease inhibitor cocktail set III, EDTA-free (Calbiochem, MA) and 20 μl of 10% Triton X-100 (Sigma, MA) and mixed by inversion for 20 minutes at 4 °C.

    Techniques: Migration, Infection

    Coinfection with H. polygyrus does not impact macrophage levels within the airspace, lung tissue or circulation during P. aeruginosa infection of the airspace. FACS analysis using F4/80 and CD11b markers to isolate the macrophage populations in the ( a ) BAL, ( b ) lung tissue and ( c ) monocytes in peripheral blood. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Journal: Scientific Reports

    Article Title: Intestinal helminth infection enhances bacteria-induced recruitment of neutrophils to the airspace

    doi: 10.1038/s41598-019-51991-3

    Figure Lengend Snippet: Coinfection with H. polygyrus does not impact macrophage levels within the airspace, lung tissue or circulation during P. aeruginosa infection of the airspace. FACS analysis using F4/80 and CD11b markers to isolate the macrophage populations in the ( a ) BAL, ( b ) lung tissue and ( c ) monocytes in peripheral blood. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Article Snippet: For protein lysate samples, one of the 0.5 mL BAL aliquots was treated with 10 μL protease inhibitor cocktail set III, EDTA-free (Calbiochem, MA) and 20 μl of 10% Triton X-100 (Sigma, MA) and mixed by inversion for 20 minutes at 4 °C.

    Techniques: Infection, FACS

    Coinfection with H. polygyrus increases cellular transepithelial migration into the lung airspace. After 2 weeks of helminth infection, the mice were infected with/without P. aeruginosa through intranasal inoculation. Mice were placed in the cage for 6 hours, and after incubation mice were sacrificed, BAL and lung tissue were obtained. ( a ) The result of BAL cell count. Data are shown as mean ± SD and are representative of three independent experiments. ** P

    Journal: Scientific Reports

    Article Title: Intestinal helminth infection enhances bacteria-induced recruitment of neutrophils to the airspace

    doi: 10.1038/s41598-019-51991-3

    Figure Lengend Snippet: Coinfection with H. polygyrus increases cellular transepithelial migration into the lung airspace. After 2 weeks of helminth infection, the mice were infected with/without P. aeruginosa through intranasal inoculation. Mice were placed in the cage for 6 hours, and after incubation mice were sacrificed, BAL and lung tissue were obtained. ( a ) The result of BAL cell count. Data are shown as mean ± SD and are representative of three independent experiments. ** P

    Article Snippet: For protein lysate samples, one of the 0.5 mL BAL aliquots was treated with 10 μL protease inhibitor cocktail set III, EDTA-free (Calbiochem, MA) and 20 μl of 10% Triton X-100 (Sigma, MA) and mixed by inversion for 20 minutes at 4 °C.

    Techniques: Migration, Infection, Mouse Assay, Incubation, Cell Counting

    Coinfection with H. polygyrus during P. aeruginosa acute pneumonia increases the CD4 + T-cells population in the airspace and lung tissues. FACS analysis using CD4 marker to isolate the CD4 + T-cell population in the ( a ) BAL, ( b ) lung tissue and ( c ) peripheral blood. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Journal: Scientific Reports

    Article Title: Intestinal helminth infection enhances bacteria-induced recruitment of neutrophils to the airspace

    doi: 10.1038/s41598-019-51991-3

    Figure Lengend Snippet: Coinfection with H. polygyrus during P. aeruginosa acute pneumonia increases the CD4 + T-cells population in the airspace and lung tissues. FACS analysis using CD4 marker to isolate the CD4 + T-cell population in the ( a ) BAL, ( b ) lung tissue and ( c ) peripheral blood. Data are shown as mean ± SD and are representative of three independent experiments. * P

    Article Snippet: For protein lysate samples, one of the 0.5 mL BAL aliquots was treated with 10 μL protease inhibitor cocktail set III, EDTA-free (Calbiochem, MA) and 20 μl of 10% Triton X-100 (Sigma, MA) and mixed by inversion for 20 minutes at 4 °C.

    Techniques: FACS, Marker