pcis filters  (Worthington Biochemical)


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  • 85
    Name:
    Deoxyribonuclease I
    Description:
    Chromatographically purified A lyophilized powder with glycine as a stabilizer
    Catalog Number:
    ls002004
    Price:
    33
    Size:
    5 mg
    Source:
    Bovine Pancreas
    Cas Number:
    9003.98.9
    Buy from Supplier


    Structured Review

    Worthington Biochemical pcis filters
    Early formation of influenza virus-specific CPE in cells inoculated with material collected by a <t>PCIS</t> at air sampling site 3. (a) Noninfected ATCC <t>MDCK</t> cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.
    Chromatographically purified A lyophilized powder with glycine as a stabilizer
    https://www.bioz.com/result/pcis filters/product/Worthington Biochemical
    Average 85 stars, based on 1188 article reviews
    Price from $9.99 to $1999.99
    pcis filters - by Bioz Stars, 2020-08
    85/100 stars

    Images

    1) Product Images from "Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler"

    Article Title: Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler

    Journal: Influenza Research and Treatment

    doi: 10.1155/2013/656825

    Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.
    Figure Legend Snippet: Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.

    Techniques Used: Sampling, Negative Control

    2) Product Images from "NFATc1 Regulates Programmed Death-1 Expression Upon T Cell Activation 1"

    Article Title: NFATc1 Regulates Programmed Death-1 Expression Upon T Cell Activation 1

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    doi:

    Two DNase I hypersensitive sites are located in 5′ conserved regions of the pdcd1 locus (A) The UCSC genome browser was used to identify regions of high DNA sequence conservation in the region 5′ of the PD-1 transcriptional start site (arrow). Two regions were identified and termed B and C (as seen labeled above with capital letters). (B) Nuclei from EL4 and A20 cells were isolated and treated with increasing concentrations of DNase I. Genomic DNA was obtained and digested with Hin dIII (H) to generate the full-length genomic DNA fragment (line below schematic). Digested DNA was then subjected to Southern blot analysis with a probe specific for the 3′ end of the Hin dIII fragment (box labeled in schematic). The resulting DNase I hypersensitive sites (DHS) map to conserved regions B and C located 5′ of the pdcd1 gene and are indicated by arrows.
    Figure Legend Snippet: Two DNase I hypersensitive sites are located in 5′ conserved regions of the pdcd1 locus (A) The UCSC genome browser was used to identify regions of high DNA sequence conservation in the region 5′ of the PD-1 transcriptional start site (arrow). Two regions were identified and termed B and C (as seen labeled above with capital letters). (B) Nuclei from EL4 and A20 cells were isolated and treated with increasing concentrations of DNase I. Genomic DNA was obtained and digested with Hin dIII (H) to generate the full-length genomic DNA fragment (line below schematic). Digested DNA was then subjected to Southern blot analysis with a probe specific for the 3′ end of the Hin dIII fragment (box labeled in schematic). The resulting DNase I hypersensitive sites (DHS) map to conserved regions B and C located 5′ of the pdcd1 gene and are indicated by arrows.

    Techniques Used: Sequencing, Labeling, Isolation, Southern Blot

    DNase I hypersensitive sites are located in the 5′ conserved region of the pdcd1 locus in primary CD8 T cells expressing PD-1 (A) A schematic of conserved regions of PD-1 and primer set amplicons are shown. (B) Nuclei from A20, EL4, and (C) primary CD8 T (+/- PMA/ionomycin) cells were isolated and treated with increasing concentrations of DNase I. Genomic DNA was isolated and subjected to real-time PCR analysis with primer sets (I, II, and III) spanning portions of the pdcd1 gene. Relative hypersensitivity was assayed by normalization of DNase I treated DNA to that of the genomic (untreated) DNA control and the data are plotted as fold sensitivity. Increasing DNase I concentration is indicated along the X-axis. The data shown are the average (-/+ standard error) of three independent experiments.
    Figure Legend Snippet: DNase I hypersensitive sites are located in the 5′ conserved region of the pdcd1 locus in primary CD8 T cells expressing PD-1 (A) A schematic of conserved regions of PD-1 and primer set amplicons are shown. (B) Nuclei from A20, EL4, and (C) primary CD8 T (+/- PMA/ionomycin) cells were isolated and treated with increasing concentrations of DNase I. Genomic DNA was isolated and subjected to real-time PCR analysis with primer sets (I, II, and III) spanning portions of the pdcd1 gene. Relative hypersensitivity was assayed by normalization of DNase I treated DNA to that of the genomic (untreated) DNA control and the data are plotted as fold sensitivity. Increasing DNase I concentration is indicated along the X-axis. The data shown are the average (-/+ standard error) of three independent experiments.

    Techniques Used: Expressing, Isolation, Real-time Polymerase Chain Reaction, Concentration Assay

    3) Product Images from "Increasing phosphoproteomic coverage through sequential digestion by complementary proteases"

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-011-5466-5

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation
    Figure Legend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Techniques Used:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion
    Figure Legend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Techniques Used:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong
    Figure Legend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Techniques Used:

    4) Product Images from "Increasing phosphoproteomic coverage through sequential digestion by complementary proteases"

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-011-5466-5

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation
    Figure Legend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Techniques Used:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion
    Figure Legend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Techniques Used:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong
    Figure Legend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Techniques Used:

    5) Product Images from "Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler"

    Article Title: Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler

    Journal: Influenza Research and Treatment

    doi: 10.1155/2013/656825

    Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.
    Figure Legend Snippet: Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.

    Techniques Used: Sampling, Negative Control

    6) Product Images from "Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler"

    Article Title: Detection and Isolation of Airborne Influenza A H3N2 Virus Using a Sioutas Personal Cascade Impactor Sampler

    Journal: Influenza Research and Treatment

    doi: 10.1155/2013/656825

    Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.
    Figure Legend Snippet: Early formation of influenza virus-specific CPE in cells inoculated with material collected by a PCIS at air sampling site 3. (a) Noninfected ATCC MDCK cells (negative control), 3 days postseed. (b) ATCC MDCK cells inoculated with material scraped off the PCIS after-filter. (c) Noninfected MDCK-SIAT2,6-UF cells, (negative control), 3 days postseed. (d) MDCK-SIAT2,6-UF cells inoculated with material scraped off the PCIS after-filter.

    Techniques Used: Sampling, Negative Control

    Related Articles

    Irradiation:

    Article Title: Characterization of the survival motor neuron (SMN) promoter provides evidence for complex combinatorial regulation in undifferentiated and differentiated P19 cells
    Article Snippet: .. Specifically, we used DMS, UVC irradiation and DNase I as DNA-modifying agents to map single-strand DNA breaks, comparing in vitro (naked DNA) and in vivo (living cells) footprints. .. In vivo footprints corresponding to nt −46 to +125 encompassing the minimal core promoter are presented in and summarized in .

    In Vivo:

    Article Title: Characterization of the survival motor neuron (SMN) promoter provides evidence for complex combinatorial regulation in undifferentiated and differentiated P19 cells
    Article Snippet: .. Specifically, we used DMS, UVC irradiation and DNase I as DNA-modifying agents to map single-strand DNA breaks, comparing in vitro (naked DNA) and in vivo (living cells) footprints. .. In vivo footprints corresponding to nt −46 to +125 encompassing the minimal core promoter are presented in and summarized in .

    In Vitro:

    Article Title: Characterization of the survival motor neuron (SMN) promoter provides evidence for complex combinatorial regulation in undifferentiated and differentiated P19 cells
    Article Snippet: .. Specifically, we used DMS, UVC irradiation and DNase I as DNA-modifying agents to map single-strand DNA breaks, comparing in vitro (naked DNA) and in vivo (living cells) footprints. .. In vivo footprints corresponding to nt −46 to +125 encompassing the minimal core promoter are presented in and summarized in .

    Produced:

    Article Title: Novel High-Throughput Deoxyribonuclease 1 Assay
    Article Snippet: .. The percentage of DNase I activity was calculated using Equation 1: DNase\u00a0I\u00a0activity (%) =\u00a0 (mean\u00a0velocity\u00a0of\u00a0a\u00a0compound/mean\u00a0velocity\u00a0of\u00a0DMSO)\u00a0\u00d7\u00a0100 (1) In similar assays, recombinant murine EndoG (produced in-house) was used at a concentration of 0.14 μM in 0.1 mM MgCl2 , 10 mM Tris-HCl, pH 7.4; and DNase II (Worthington, Lakewood, NJ) (3.32 nM) was tested in 100 mM sodium citrate buffer, pH 5.0. .. For evaluation of the quality of the assay, Z’ values were calculated using Equation 2: Z\u2019 =\u00a01\u00a0\u2212\u00a0(3SDC +\u00a03SDB )/(MC \u00a0\u2212\u00a0MB ) (2) where M = mean value; SD = standard deviation; C = control; and B = background.

    Concentration Assay:

    Article Title: Novel High-Throughput Deoxyribonuclease 1 Assay
    Article Snippet: .. The percentage of DNase I activity was calculated using Equation 1: DNase\u00a0I\u00a0activity (%) =\u00a0 (mean\u00a0velocity\u00a0of\u00a0a\u00a0compound/mean\u00a0velocity\u00a0of\u00a0DMSO)\u00a0\u00d7\u00a0100 (1) In similar assays, recombinant murine EndoG (produced in-house) was used at a concentration of 0.14 μM in 0.1 mM MgCl2 , 10 mM Tris-HCl, pH 7.4; and DNase II (Worthington, Lakewood, NJ) (3.32 nM) was tested in 100 mM sodium citrate buffer, pH 5.0. .. For evaluation of the quality of the assay, Z’ values were calculated using Equation 2: Z\u2019 =\u00a01\u00a0\u2212\u00a0(3SDC +\u00a03SDB )/(MC \u00a0\u2212\u00a0MB ) (2) where M = mean value; SD = standard deviation; C = control; and B = background.

    Incubation:

    Article Title: Identification of Viral Peptide Fragments for Vaccine Development
    Article Snippet: .. When the random digestion by DNase I is used for some genes, peculiarly a small amount of the full-length gene has been observed even after prolonged incubation. .. In this case, the digestion mixture should be passed through a column with an appropriate molecular weight cut-off to filter out the full-length gene, followed by a Microcon® YM-30 column to accomplish the buffer exchange.

    Article Title: Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans
    Article Snippet: .. As controls (i) NETs were mock-digested with nuclease-free RPMI and (ii) unstimulated neutrophils that did not release NETs were washed twice and incubated with RPMI containing 10 U/ml Dnase-1 for 20 min at 37°C. .. Four samples out of 4 wells were pooled, acetone precipitated, solubilized in 120 µl SDS loading buffer and boiled for 3 min. To account for potential protein loss due to proteolytic activity in the samples a complete purification procedure was performed in the presence of protease inhibitor cocktail (Sigma P1860; 1∶200) added to the wells 2 h after stimulation start as described above.

    other:

    Article Title: Transcriptional regulatory logic of the diurnal cycle in the mouse liver
    Article Snippet: Movie S2: Dynamics of DNase I, Pol II and H3K27ac at the Npas2 locus.

    Article Title: Identification of Viral Peptide Fragments for Vaccine Development
    Article Snippet: In the random digestion step, the use of DNase I in the presence of MnCl2 is critical as this protocol will generate DNA fragments of relatively uniform sizes, which facilitates the reassembly step ( 17 , also see Note ).

    Article Title: Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans
    Article Snippet: Supernatants were removed, NETs were washed twice with 1 ml RPMI and digested with 500 µl 10 U/ml DNase-1 each.

    Activity Assay:

    Article Title: Novel High-Throughput Deoxyribonuclease 1 Assay
    Article Snippet: .. The percentage of DNase I activity was calculated using Equation 1: DNase\u00a0I\u00a0activity (%) =\u00a0 (mean\u00a0velocity\u00a0of\u00a0a\u00a0compound/mean\u00a0velocity\u00a0of\u00a0DMSO)\u00a0\u00d7\u00a0100 (1) In similar assays, recombinant murine EndoG (produced in-house) was used at a concentration of 0.14 μM in 0.1 mM MgCl2 , 10 mM Tris-HCl, pH 7.4; and DNase II (Worthington, Lakewood, NJ) (3.32 nM) was tested in 100 mM sodium citrate buffer, pH 5.0. .. For evaluation of the quality of the assay, Z’ values were calculated using Equation 2: Z\u2019 =\u00a01\u00a0\u2212\u00a0(3SDC +\u00a03SDB )/(MC \u00a0\u2212\u00a0MB ) (2) where M = mean value; SD = standard deviation; C = control; and B = background.

    Staining:

    Article Title: Constitutive Nucleosome Depletion and Ordered Factor Assembly at the GRP78 Promoter Revealed by Single Molecule Footprinting
    Article Snippet: .. These were then digested at 37 °C for 15 min using various concentrations of DNase I (Worthington, San Francisco, California, United States) to obtain a suitable range of digestion of genomic DNA as revealed by EtBr staining. .. Digested genomic DNA was purified, redigested by RsaI, resolved on a 1.5% agarose gel, and Southern blotted.

    Recombinant:

    Article Title: Novel High-Throughput Deoxyribonuclease 1 Assay
    Article Snippet: .. The percentage of DNase I activity was calculated using Equation 1: DNase\u00a0I\u00a0activity (%) =\u00a0 (mean\u00a0velocity\u00a0of\u00a0a\u00a0compound/mean\u00a0velocity\u00a0of\u00a0DMSO)\u00a0\u00d7\u00a0100 (1) In similar assays, recombinant murine EndoG (produced in-house) was used at a concentration of 0.14 μM in 0.1 mM MgCl2 , 10 mM Tris-HCl, pH 7.4; and DNase II (Worthington, Lakewood, NJ) (3.32 nM) was tested in 100 mM sodium citrate buffer, pH 5.0. .. For evaluation of the quality of the assay, Z’ values were calculated using Equation 2: Z\u2019 =\u00a01\u00a0\u2212\u00a0(3SDC +\u00a03SDB )/(MC \u00a0\u2212\u00a0MB ) (2) where M = mean value; SD = standard deviation; C = control; and B = background.

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