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antibodies against serpinb9  (Novus Biologicals)
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Novus Biologicals antibodies against serpinb9
Fig. 1. TLR3 triggering induces <t>serpinB9</t> expression in human TECs. Primary TECs were stimulated for 16 h (light gray bars) or 40 h (dark gray bars) with 100 ng/mL TNF-α, 100 ng/mL IFNγ, 100 ng/mL IL-1β, 1000 pg/mL IL-6, 100 μg/mL LTA (TLR2 ligand), 100 μg/mL poly(I:C) (pIC, TLR3 ligand), 10 μg/mL LPS (TLR4 ligand), 100 μg/mL imiquimod (ImiQ, TLR7 ligand) or 10 μg/mL CpG oligonucleotides (CpG, TLR9 ligand). For each stimulus, three concentrations with a one-log difference were tested, and the highest concentration is depicted in the figure. (A) SerpinB9 expression was analysed, by quantitative PCR. An increase of mRNA above 2-fold (dotted line) was considered significant. (B and C) Protein levels of serpinB9 were determined by western blot analysis. Representative blots of serpinB9 expression in TECs stimulated for 16 h are depicted below the graph. The bars represent the fold change in serpinB9 expression compared to unstimulated TECs (mean ± SEM, n ≥3). **P < 0.01. (C) The TLR3 inhibitor chloroquine (HCQ, 10–100 μM) was administered 30 min prior to stimulation with poly(I:C) (pIC, 0.1–500 μg/mL, 16 h).
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Fig. 1. TLR3 triggering induces serpinB9 expression in human TECs. Primary TECs were stimulated for 16 h (light gray bars) or 40 h (dark gray bars) with 100 ng/mL TNF-α, 100 ng/mL IFNγ, 100 ng/mL IL-1β, 1000 pg/mL IL-6, 100 μg/mL LTA (TLR2 ligand), 100 μg/mL poly(I:C) (pIC, TLR3 ligand), 10 μg/mL LPS (TLR4 ligand), 100 μg/mL imiquimod (ImiQ, TLR7 ligand) or 10 μg/mL CpG oligonucleotides (CpG, TLR9 ligand). For each stimulus, three concentrations with a one-log difference were tested, and the highest concentration is depicted in the figure. (A) SerpinB9 expression was analysed, by quantitative PCR. An increase of mRNA above 2-fold (dotted line) was considered significant. (B and C) Protein levels of serpinB9 were determined by western blot analysis. Representative blots of serpinB9 expression in TECs stimulated for 16 h are depicted below the graph. The bars represent the fold change in serpinB9 expression compared to unstimulated TECs (mean ± SEM, n ≥3). **P < 0.01. (C) The TLR3 inhibitor chloroquine (HCQ, 10–100 μM) was administered 30 min prior to stimulation with poly(I:C) (pIC, 0.1–500 μg/mL, 16 h).

Journal: Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

Article Title: SerpinB9 expression in human renal tubular epithelial cells is induced by triggering of the viral dsRNA sensors TLR3, MDA5 and RIG-I.

doi: 10.1093/ndt/gfr690

Figure Lengend Snippet: Fig. 1. TLR3 triggering induces serpinB9 expression in human TECs. Primary TECs were stimulated for 16 h (light gray bars) or 40 h (dark gray bars) with 100 ng/mL TNF-α, 100 ng/mL IFNγ, 100 ng/mL IL-1β, 1000 pg/mL IL-6, 100 μg/mL LTA (TLR2 ligand), 100 μg/mL poly(I:C) (pIC, TLR3 ligand), 10 μg/mL LPS (TLR4 ligand), 100 μg/mL imiquimod (ImiQ, TLR7 ligand) or 10 μg/mL CpG oligonucleotides (CpG, TLR9 ligand). For each stimulus, three concentrations with a one-log difference were tested, and the highest concentration is depicted in the figure. (A) SerpinB9 expression was analysed, by quantitative PCR. An increase of mRNA above 2-fold (dotted line) was considered significant. (B and C) Protein levels of serpinB9 were determined by western blot analysis. Representative blots of serpinB9 expression in TECs stimulated for 16 h are depicted below the graph. The bars represent the fold change in serpinB9 expression compared to unstimulated TECs (mean ± SEM, n ≥3). **P < 0.01. (C) The TLR3 inhibitor chloroquine (HCQ, 10–100 μM) was administered 30 min prior to stimulation with poly(I:C) (pIC, 0.1–500 μg/mL, 16 h).

Article Snippet: Proteins (50 μg per lane) were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane and probed with primary antibodies against serpinB9 (mouse IgG1, clone PI9-17; kindly provided by Prof. S.M. van Ham, Sanquin, Amsterdam, The Netherlands [11], or mouse IgG1, clone 7D8; AbD Serotec, Dusseldorf, Germany), serpinB8 (mouse IgG; Abcam, Cambridge, UK), TLR3 (mouse IgG1, clone 40C1285.6; Abnova GmbH, Heidelberg, Germany), MDA5 (goat Ig; Imgenex, San Diego, CA), RIG-I (mouse IgG1, clone Alme-1; Enzo Life Sciences, Zandhoven, Belgium) and actin (goat Ig, I19; Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Expressing, Concentration Assay, Real-time Polymerase Chain Reaction, Western Blot

Fig. 3. The dsRNA receptors TLR3, MDA5 and RIG-I upregulate serpinB9 expression in TECs independent of new protein synthesis. Primary TECs were stimulated for 16 h with 0.01–10 μg/mL poly(I:C) (pIC) or 0.1 μg/mL 3pRNA. The transfection reagent Fugene HD (FG) was used to accomplish cytoplasmic delivery. SerpinB9 expression was determined by western blot analysis (A) or quantitative PCR (B). The bars represent the fold change in serpinB9 expression compared to unstimulated cells (mean ± SEM, n = 3). (B) The inhibitors Bay 11-7082 (Bay, 5 μM) or cycloheximide (CHX, 5 μg/mL) were administered 30 min prior to dsRNA receptor activation; *P < 0.05.

Journal: Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

Article Title: SerpinB9 expression in human renal tubular epithelial cells is induced by triggering of the viral dsRNA sensors TLR3, MDA5 and RIG-I.

doi: 10.1093/ndt/gfr690

Figure Lengend Snippet: Fig. 3. The dsRNA receptors TLR3, MDA5 and RIG-I upregulate serpinB9 expression in TECs independent of new protein synthesis. Primary TECs were stimulated for 16 h with 0.01–10 μg/mL poly(I:C) (pIC) or 0.1 μg/mL 3pRNA. The transfection reagent Fugene HD (FG) was used to accomplish cytoplasmic delivery. SerpinB9 expression was determined by western blot analysis (A) or quantitative PCR (B). The bars represent the fold change in serpinB9 expression compared to unstimulated cells (mean ± SEM, n = 3). (B) The inhibitors Bay 11-7082 (Bay, 5 μM) or cycloheximide (CHX, 5 μg/mL) were administered 30 min prior to dsRNA receptor activation; *P < 0.05.

Article Snippet: Proteins (50 μg per lane) were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane and probed with primary antibodies against serpinB9 (mouse IgG1, clone PI9-17; kindly provided by Prof. S.M. van Ham, Sanquin, Amsterdam, The Netherlands [11], or mouse IgG1, clone 7D8; AbD Serotec, Dusseldorf, Germany), serpinB8 (mouse IgG; Abcam, Cambridge, UK), TLR3 (mouse IgG1, clone 40C1285.6; Abnova GmbH, Heidelberg, Germany), MDA5 (goat Ig; Imgenex, San Diego, CA), RIG-I (mouse IgG1, clone Alme-1; Enzo Life Sciences, Zandhoven, Belgium) and actin (goat Ig, I19; Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Expressing, Transfection, Western Blot, Real-time Polymerase Chain Reaction, Activation Assay

Fig. 4. SerpinB9 expression in the kidney is enhanced during viral infection. (A) SerpinB9 transcription in frozen biopsy specimens obtained from stable patients (n = 5) and patients infected with CMV (n = 6), EBV (n = 4) or BKV (n = 7) depicted as relative expression (median). *P < 0.05, **P < 0.01. (B and C) Immunohostochemical stainings for serpinB9 on formalin-fixed paraffin-embedded tissue slides. (B) Semi-quantitative scoring of the tubular SerpinB9 expression, scored as described in the Materials and Methods (median). (C) Representative pictures of the serpinB9 staining pattern observed in stable, CMV, EBV and BKV biopsies, with serpinB9 expression found in the tubuli (black arrows) and infiltrating lymphocytes (red arrow) (magnification 200 × ).

Journal: Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

Article Title: SerpinB9 expression in human renal tubular epithelial cells is induced by triggering of the viral dsRNA sensors TLR3, MDA5 and RIG-I.

doi: 10.1093/ndt/gfr690

Figure Lengend Snippet: Fig. 4. SerpinB9 expression in the kidney is enhanced during viral infection. (A) SerpinB9 transcription in frozen biopsy specimens obtained from stable patients (n = 5) and patients infected with CMV (n = 6), EBV (n = 4) or BKV (n = 7) depicted as relative expression (median). *P < 0.05, **P < 0.01. (B and C) Immunohostochemical stainings for serpinB9 on formalin-fixed paraffin-embedded tissue slides. (B) Semi-quantitative scoring of the tubular SerpinB9 expression, scored as described in the Materials and Methods (median). (C) Representative pictures of the serpinB9 staining pattern observed in stable, CMV, EBV and BKV biopsies, with serpinB9 expression found in the tubuli (black arrows) and infiltrating lymphocytes (red arrow) (magnification 200 × ).

Article Snippet: Proteins (50 μg per lane) were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane and probed with primary antibodies against serpinB9 (mouse IgG1, clone PI9-17; kindly provided by Prof. S.M. van Ham, Sanquin, Amsterdam, The Netherlands [11], or mouse IgG1, clone 7D8; AbD Serotec, Dusseldorf, Germany), serpinB8 (mouse IgG; Abcam, Cambridge, UK), TLR3 (mouse IgG1, clone 40C1285.6; Abnova GmbH, Heidelberg, Germany), MDA5 (goat Ig; Imgenex, San Diego, CA), RIG-I (mouse IgG1, clone Alme-1; Enzo Life Sciences, Zandhoven, Belgium) and actin (goat Ig, I19; Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Expressing, Infection, Staining

Fig. 5. Schematic overview of dsRNA receptor signalling in TECs. Human TECs express the dsRNA sensors TLR3, MDA5 and RIG-I. TLR3 is located in the membrane of endolysosomes and becomes activated after endocytosis of viral particles or dsRNA. The cytoplasmic receptors MDA5 and RIG-I recognize dsRNA generated during viral replication in infected cells. The three dsRNA receptors activate the same transcription factors; namely NF-κB and IRF-3/7. Triggering of NF-κB induces transcription of proinflammatory cytokines like TNF-α, while IRF-3/7 initiate gene expression of Type I IFNs. Transcription of serpinB9 and the dsRNA receptors themselves is regulated by both NF- κB and IRFs. In addition, Type I IFNs trigger the IFN receptor leading to IRF-9-mediated transcription of the dsRNA receptor genes. This feed forward loop renders TECs more sensitive to dsRNA.

Journal: Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

Article Title: SerpinB9 expression in human renal tubular epithelial cells is induced by triggering of the viral dsRNA sensors TLR3, MDA5 and RIG-I.

doi: 10.1093/ndt/gfr690

Figure Lengend Snippet: Fig. 5. Schematic overview of dsRNA receptor signalling in TECs. Human TECs express the dsRNA sensors TLR3, MDA5 and RIG-I. TLR3 is located in the membrane of endolysosomes and becomes activated after endocytosis of viral particles or dsRNA. The cytoplasmic receptors MDA5 and RIG-I recognize dsRNA generated during viral replication in infected cells. The three dsRNA receptors activate the same transcription factors; namely NF-κB and IRF-3/7. Triggering of NF-κB induces transcription of proinflammatory cytokines like TNF-α, while IRF-3/7 initiate gene expression of Type I IFNs. Transcription of serpinB9 and the dsRNA receptors themselves is regulated by both NF- κB and IRFs. In addition, Type I IFNs trigger the IFN receptor leading to IRF-9-mediated transcription of the dsRNA receptor genes. This feed forward loop renders TECs more sensitive to dsRNA.

Article Snippet: Proteins (50 μg per lane) were separated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis and transferred to a nitrocellulose membrane and probed with primary antibodies against serpinB9 (mouse IgG1, clone PI9-17; kindly provided by Prof. S.M. van Ham, Sanquin, Amsterdam, The Netherlands [11], or mouse IgG1, clone 7D8; AbD Serotec, Dusseldorf, Germany), serpinB8 (mouse IgG; Abcam, Cambridge, UK), TLR3 (mouse IgG1, clone 40C1285.6; Abnova GmbH, Heidelberg, Germany), MDA5 (goat Ig; Imgenex, San Diego, CA), RIG-I (mouse IgG1, clone Alme-1; Enzo Life Sciences, Zandhoven, Belgium) and actin (goat Ig, I19; Santa Cruz Biotechnology, Santa Cruz, CA).

Techniques: Membrane, Generated, Infection, Gene Expression