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The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.
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The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.
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The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.
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The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.
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The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.

Journal: Mediators of Inflammation

Article Title: TLR Signalling Pathways Diverge in Their Ability to Induce PGE 2

doi: 10.1155/2016/5678046

Figure Lengend Snippet: The release of PGE 2 by DCs depends on the activation of the MAPK and NF- κ B pathways. (a) DCs were stimulated with increasing concentrations of LPS for 24 h and PGE 2 production was quantified by EIA. Data are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (b) DCs were pretreated for 1 h with the indicated doses of U0126, PD98059, SB203580, or BAY-11-7082 and then stimulated with LPS (100 ng/mL) for 24 h. The production of PGE 2 was evaluated in cell-free supernatants by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (c) DCs were treated as in (b), using 1 μ M of each inhibitor. The expression of COX2 and β -actin was determined by Western blot. One representative fluorogram out of three and its densitometric analysis are shown.

Article Snippet: Equal amounts of cytoplasmic, nuclear, or total extracts were analysed through 8–12% SDS-PAGE followed by Western blotting with antibodies against COX2 (mouse monoclonal, Cat. 160112, Cayman Chemical), phospho-ERK1/2 (rabbit polyclonal, Cat. 9101, Cell Signalling Technologies, Massachusetts, USA), phospho-p38 (rabbit polyclonal, Cat. 9211, Cell Signalling), phospho-cPLA 2 (rabbit polyclonal, Cat. 2831, Cell Signalling), phospho-MSK1 (rabbit polyclonal, Cat. 9595, Cell Signalling), NF- κ B p65 (rabbit polyclonal, C-20 Cat. sc-372, Santa Cruz Biotechnology), β -actin (mouse monoclonal, C-4 Cat. sc-44478, Santa Cruz Biotechnology), and Lamin B (goat polyclonal, C-20 Cat. sc-6216, Santa Cruz Biotechnology).

Techniques: Activation Assay, Expressing, Western Blot

TLRs differentially activate the MAPK and NF- κ B pathways. DCs were stimulated with TLR agonists as indicated in for 30 min. After cell lysis, extracts were blotted against phospho-p38, phospho-ERK1/2, and phospho-MSK1. Nuclear extracts were blotted against NF- κ B p65. β -actin and Lamin B represent loading controls for total and nuclear proteins, respectively. The image depicts results obtained in one representative donor out of three.

Journal: Mediators of Inflammation

Article Title: TLR Signalling Pathways Diverge in Their Ability to Induce PGE 2

doi: 10.1155/2016/5678046

Figure Lengend Snippet: TLRs differentially activate the MAPK and NF- κ B pathways. DCs were stimulated with TLR agonists as indicated in for 30 min. After cell lysis, extracts were blotted against phospho-p38, phospho-ERK1/2, and phospho-MSK1. Nuclear extracts were blotted against NF- κ B p65. β -actin and Lamin B represent loading controls for total and nuclear proteins, respectively. The image depicts results obtained in one representative donor out of three.

Article Snippet: Equal amounts of cytoplasmic, nuclear, or total extracts were analysed through 8–12% SDS-PAGE followed by Western blotting with antibodies against COX2 (mouse monoclonal, Cat. 160112, Cayman Chemical), phospho-ERK1/2 (rabbit polyclonal, Cat. 9101, Cell Signalling Technologies, Massachusetts, USA), phospho-p38 (rabbit polyclonal, Cat. 9211, Cell Signalling), phospho-cPLA 2 (rabbit polyclonal, Cat. 2831, Cell Signalling), phospho-MSK1 (rabbit polyclonal, Cat. 9595, Cell Signalling), NF- κ B p65 (rabbit polyclonal, C-20 Cat. sc-372, Santa Cruz Biotechnology), β -actin (mouse monoclonal, C-4 Cat. sc-44478, Santa Cruz Biotechnology), and Lamin B (goat polyclonal, C-20 Cat. sc-6216, Santa Cruz Biotechnology).

Techniques: Lysis

Lack of AA mobilization blocks the release of PGE 2 upon TLR1/2 and TLR2/6 stimulation. (a) DCs were stimulated with TLR agonists for 24 h. The expression of COX2 and β -actin was determined by Western blot. Fluorogram from one out of 3 representative donors and its densitometric analysis are shown. (b) DCs were stimulated with TLR agonists for 30 min and the phosphorylation of cPLA 2 was determined by immunoblot. One out of 3 representative donors and its densitometric analysis are shown. (c) DCs were labelled with 0.125 μ Ci/mL [ 14 C] AA overnight and then stimulated with the indicated TLR ligands for 3 h. The results are expressed as the means ± SEM ( n = 3) of the percentage of [ 14 C] AA release on the total radioactivity recovered from each stimulation; ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (d) DCs were incubated with TLR ligands in the presence (black bars) or absence (white bars) of 10 μ M AA. After 24 h, supernatants were collected and the production of PGE 2 was evaluated by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test.

Journal: Mediators of Inflammation

Article Title: TLR Signalling Pathways Diverge in Their Ability to Induce PGE 2

doi: 10.1155/2016/5678046

Figure Lengend Snippet: Lack of AA mobilization blocks the release of PGE 2 upon TLR1/2 and TLR2/6 stimulation. (a) DCs were stimulated with TLR agonists for 24 h. The expression of COX2 and β -actin was determined by Western blot. Fluorogram from one out of 3 representative donors and its densitometric analysis are shown. (b) DCs were stimulated with TLR agonists for 30 min and the phosphorylation of cPLA 2 was determined by immunoblot. One out of 3 representative donors and its densitometric analysis are shown. (c) DCs were labelled with 0.125 μ Ci/mL [ 14 C] AA overnight and then stimulated with the indicated TLR ligands for 3 h. The results are expressed as the means ± SEM ( n = 3) of the percentage of [ 14 C] AA release on the total radioactivity recovered from each stimulation; ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test. (d) DCs were incubated with TLR ligands in the presence (black bars) or absence (white bars) of 10 μ M AA. After 24 h, supernatants were collected and the production of PGE 2 was evaluated by EIA. Results are expressed as mean ± SEM ( n = 3); ∗ P < 0.05 by one-way ANOVA with Dunnett's post hoc test.

Article Snippet: Equal amounts of cytoplasmic, nuclear, or total extracts were analysed through 8–12% SDS-PAGE followed by Western blotting with antibodies against COX2 (mouse monoclonal, Cat. 160112, Cayman Chemical), phospho-ERK1/2 (rabbit polyclonal, Cat. 9101, Cell Signalling Technologies, Massachusetts, USA), phospho-p38 (rabbit polyclonal, Cat. 9211, Cell Signalling), phospho-cPLA 2 (rabbit polyclonal, Cat. 2831, Cell Signalling), phospho-MSK1 (rabbit polyclonal, Cat. 9595, Cell Signalling), NF- κ B p65 (rabbit polyclonal, C-20 Cat. sc-372, Santa Cruz Biotechnology), β -actin (mouse monoclonal, C-4 Cat. sc-44478, Santa Cruz Biotechnology), and Lamin B (goat polyclonal, C-20 Cat. sc-6216, Santa Cruz Biotechnology).

Techniques: Expressing, Western Blot, Phospho-proteomics, Radioactivity, Incubation

List of valid and putative type strains of Mycobacterium species sequences

Journal:

Article Title: Assessment of Partial Sequencing of the 65-Kilodalton Heat Shock Protein Gene ( hsp65 ) for Routine Identification of Mycobacterium Species Isolated from Clinical Sources

doi: 10.1128/JCM.42.7.3000-3011.2004

Figure Lengend Snippet: List of valid and putative type strains of Mycobacterium species sequences

Article Snippet: M. holsaticum , DSM 44478 , M. tuberculosis , ATCC 27294.

Techniques: Variant Assay

Percentage sequence match for putative and valid Mycobacterium spp.

Journal:

Article Title: Assessment of Partial Sequencing of the 65-Kilodalton Heat Shock Protein Gene ( hsp65 ) for Routine Identification of Mycobacterium Species Isolated from Clinical Sources

doi: 10.1128/JCM.42.7.3000-3011.2004

Figure Lengend Snippet: Percentage sequence match for putative and valid Mycobacterium spp.

Article Snippet: M. holsaticum , DSM 44478 , M. tuberculosis , ATCC 27294.

Techniques: Sequencing

Comparison of mycobacteria identified by biochemical test panels, AccuProbe tests, and 16S rRNA gene sequencing a

Journal:

Article Title: Assessment of Partial Sequencing of the 65-Kilodalton Heat Shock Protein Gene ( hsp65 ) for Routine Identification of Mycobacterium Species Isolated from Clinical Sources

doi: 10.1128/JCM.42.7.3000-3011.2004

Figure Lengend Snippet: Comparison of mycobacteria identified by biochemical test panels, AccuProbe tests, and 16S rRNA gene sequencing a

Article Snippet: M. holsaticum , DSM 44478 , M. tuberculosis , ATCC 27294.

Techniques: Comparison, Sequencing, Variant Assay