ng g recombinant human  (R&D Systems)

 
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  • 90
    Name:
    Recombinant Human Noggin Protein CF
    Description:
    The Recombinant Human Noggin Protein from R D Systems is derived from NS0 The Recombinant Human Noggin Protein has been validated for the following applications Bioactivity
    Catalog Number:
    6057-NG-025/CF
    Price:
    329
    Category:
    Proteins and Enzymes
    Source:
    NS0-derived Recombinant Human Noggin Protein
    Applications:
    Bioactivity
    Purity:
    >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie« Blue Staining.
    Conjugate:
    Unconjugated
    Size:
    25 ug
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    Structured Review

    R&D Systems ng g recombinant human
    Recombinant Human Noggin Protein CF
    The Recombinant Human Noggin Protein from R D Systems is derived from NS0 The Recombinant Human Noggin Protein has been validated for the following applications Bioactivity
    https://www.bioz.com/result/ng g recombinant human/product/R&D Systems
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ng g recombinant human - by Bioz Stars, 2021-09
    90/100 stars

    Images

    1) Product Images from "Vascular endothelial growth factor-A165b ameliorates outer-retinal barrier and vascular dysfunction in the diabetic retina"

    Article Title: Vascular endothelial growth factor-A165b ameliorates outer-retinal barrier and vascular dysfunction in the diabetic retina

    Journal: Clinical Science (London, England : 1979)

    doi: 10.1042/CS20170102

    Systemic VEGF-A 165 b prevents diabetes-induced increase in solute flux ( A ) Sprague–Dawley female rats were induced with diabetes using STZ (50 mg/kg i.p., n =10) and control rats ( n =5) were injected with saline (i.p.) on day 0. After 4 days, blood glucose was tested and blood glucose ≥ 15mmol/l were deemed diabetic. ( B ) Diabetic rats were treated with either vehicle (saline, biweekly i.p., n =5) or VEGF-A 165 b (20 ng/g, biweekly i.p., n =5). At 8 weeks post-STZ induction, Evans Blue (EB, 45 mg/kg) was injected i.v. into terminally anaesthetized rats. Plasma was collected every 15 minutes for 2 h, after which, animals were killed and retinae were excised. ( C ) Retinae were weighed and EB was extracted using formamide, allowing EB solute flux (C) and permeability surface area product ( D ) to be calculated; Kruskal–Wallis test with Dunn's post-hoc test, ** p
    Figure Legend Snippet: Systemic VEGF-A 165 b prevents diabetes-induced increase in solute flux ( A ) Sprague–Dawley female rats were induced with diabetes using STZ (50 mg/kg i.p., n =10) and control rats ( n =5) were injected with saline (i.p.) on day 0. After 4 days, blood glucose was tested and blood glucose ≥ 15mmol/l were deemed diabetic. ( B ) Diabetic rats were treated with either vehicle (saline, biweekly i.p., n =5) or VEGF-A 165 b (20 ng/g, biweekly i.p., n =5). At 8 weeks post-STZ induction, Evans Blue (EB, 45 mg/kg) was injected i.v. into terminally anaesthetized rats. Plasma was collected every 15 minutes for 2 h, after which, animals were killed and retinae were excised. ( C ) Retinae were weighed and EB was extracted using formamide, allowing EB solute flux (C) and permeability surface area product ( D ) to be calculated; Kruskal–Wallis test with Dunn's post-hoc test, ** p

    Techniques Used: Injection, Permeability

    VEGF-A 165 b prevents retinal ganglion cell shrinkage ( A ) Sprague–Dawley rats induced with diabetes were treated with vehicle (saline i.p., n =4) or VEGF-A 165 b (20 ng/g i.p., n =4) biweekly for 8 weeks. Animals were then killed and retinae excised and ( A ) stained for RGC marker NeuN. RGC NeuN+ staining was counted ( B ) and areas measured ( C ). ( D ) The frequency of NeuN+ areas (50 μm bins) was plotted against area, and Lorentzian curve fitted, and curve fit compared with an F -test; P
    Figure Legend Snippet: VEGF-A 165 b prevents retinal ganglion cell shrinkage ( A ) Sprague–Dawley rats induced with diabetes were treated with vehicle (saline i.p., n =4) or VEGF-A 165 b (20 ng/g i.p., n =4) biweekly for 8 weeks. Animals were then killed and retinae excised and ( A ) stained for RGC marker NeuN. RGC NeuN+ staining was counted ( B ) and areas measured ( C ). ( D ) The frequency of NeuN+ areas (50 μm bins) was plotted against area, and Lorentzian curve fitted, and curve fit compared with an F -test; P

    Techniques Used: Staining, Marker

    VEGF-A 165 b prevents diabetes-induced increase in retinal vascular density ( A ) STZ (50 mg/kg, i.p.) was used to induce diabetes in Sprague–Dawley rats ( n =10). Saline was injected in vehicle controls (i.p., n =4). Diabetic rats were either treated with VEGF-A 165 b (20 ng/g, biweekly i.p., n =5) or saline (biweekly i.p., n =5). All groups were weighed weekly and rats with a blood glucose ≥15 mmol/l were deemed diabetic. ( B ) Rats were killed at 8 weeks and retinae were stained for blood vessels using IB4 and DAPI. Vascular density was calculated from three parts of the retina in each animal (denoted by shading) using Imaris software, measured as both area ( C ) and volume ( D ) occupied by vasculature in a 2D and 3D plane respectively. This was corroborated by measuring integrated density on Fiji software ( E ). Retinae were also assessed for vessel straightness using Imaris software as a marker for vessel tortuosity ( F ); one-way ANOVA, Tukey's post-hoc test, * p
    Figure Legend Snippet: VEGF-A 165 b prevents diabetes-induced increase in retinal vascular density ( A ) STZ (50 mg/kg, i.p.) was used to induce diabetes in Sprague–Dawley rats ( n =10). Saline was injected in vehicle controls (i.p., n =4). Diabetic rats were either treated with VEGF-A 165 b (20 ng/g, biweekly i.p., n =5) or saline (biweekly i.p., n =5). All groups were weighed weekly and rats with a blood glucose ≥15 mmol/l were deemed diabetic. ( B ) Rats were killed at 8 weeks and retinae were stained for blood vessels using IB4 and DAPI. Vascular density was calculated from three parts of the retina in each animal (denoted by shading) using Imaris software, measured as both area ( C ) and volume ( D ) occupied by vasculature in a 2D and 3D plane respectively. This was corroborated by measuring integrated density on Fiji software ( E ). Retinae were also assessed for vessel straightness using Imaris software as a marker for vessel tortuosity ( F ); one-way ANOVA, Tukey's post-hoc test, * p

    Techniques Used: Injection, Staining, Software, Marker

    Related Articles

    Recombinant:

    Article Title: Vascular endothelial growth factor-A165b ameliorates outer-retinal barrier and vascular dysfunction in the diabetic retina
    Article Snippet: .. For the chronic experiment, diabetic rats were treated with 20 ng/g recombinant human (rh)VEGF-A165 b (i.p., R & D Systems, MN, U.S.A.) or saline biweekly for the experimental period. ..

    Invasion Assay:

    Article Title: Soluble factors from the notochordal-rich intervertebral disc inhibit endothelial cell invasion and vessel formation in the presence and absence of pro-inflammatory cytokines
    Article Snippet: .. Additive studies examined the following treatment conditions: (1) Basal medium, (2) CS (Sigma, #C9819) at 10 and 100 μg/ml , and (3) Noggin (R & D Systems #6057-NG-025/CF) at 10 and 100 ng/ml , for both the cell invasion assay and tubular formation assays. ..

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  • 93
    R&D Systems affinity purified normal goat igg
    <t>CCL21</t> neutralization abrogates microglial activation, neuronal hyperexcitability, and pain-related behaviors. a–c , Microglial activation in the VPL 4 weeks after SCI was unaffected by <t>IgG</t> injection ( a ), whereas neutralizing antibodies directed against CCL21 (αCCL21; b ) robustly deactivated microglia at 8 h ( b ) and 24 h ( c ). d , Quantification of Cd11b/c field area revealed significant decreases in microglial activation in animals receiving minocycline ( + p
    Affinity Purified Normal Goat Igg, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/affinity purified normal goat igg/product/R&D Systems
    Average 93 stars, based on 1 article reviews
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    93
    R&D Systems anti mmp 3 antibody
    The Agrocybe cylindracea galectin (ACG)/Jacalin index reflects rheumatoid arthritis (RA) activity. a Correlation of matrix metalloproteinase-3 <t>(MMP-3)</t> quantities before and after immunoprecipitation (IP). Serum MMP-3 measured by turbidimetric immunoassay and MMP-3 in IP samples measured by Western blot (WB) analysis ( n = 24). b Representative data derived from antibody-overlay lectin microarray. Data are from a patient with RA who had high disease activity and a patient with RA who was in remission. Net intensity from triplicate experiments is presented as the mean ± SD. c Correlation between immunoprecipitated MMP-3 quantity and lectin signal. Patients with more than moderate disease activity are represented by open symbols ; otherwise, data are shown as filled symbols . d Correlation between the ACG/Jacalin index and Disease Activity Score in 28 joints with erythrocyte sedimentation rate (DAS28-ESR). MAL_I Maackia amurensis leukoagglutinin I, SNA Sambucus nigra agglutinin, PHA(E) Phaseolus vulgaris erythroagglutinin, NPA Narcissus pseudonarcissus agglutinin, BPL Bauhinia purpurea lectin, ABA Agaricus bisporus agglutinin, LEL Lycopersicon esculentum lectin, STL Solanum tuberosum lectin, PNA peanut agglutinin, ACA Amaranthus caudatus agglutinin, MPA Maclura pomifera agglutinin, MAH Maackia amurensis hemagglutinin, WGA wheat germ agglutinin
    Anti Mmp 3 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti mmp 3 antibody/product/R&D Systems
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    95
    R&D Systems il 32 g
    Roles of STAT1 and STAT3 in cytokine-induced PD-L1 protein expression on monocytes.  a  and  b.  Cytokine-induced PD-L1 protein expression on Monos was associated with new  PDL1  mRNA transcription. Monos were treated with IL-1a, IL-10, IL-27, IL-32 g or IFN-g. PD-L1 mRNA and surface protein were measured by q-RT-PCR and flow cytometry after 16 h or 48 h, respectively. Fold changes in PD-L1 protein and mRNA were calculated. Representative data from Monos derived from one of two normal donors are shown.  a.  Fold changes in PD-L1 protein and mRNA levels in normal donor Monos after IL-10 (100 ng/ml), IL-32 g (100 ng/ml) or IFN-g (100 IU/ml) exposure.  b.  Fold changes of PD-L1 protein and mRNA levels in normal donor Monos after IL-1a (10 ng/ml), IL-27 (50 ng/ml) or IFN-g (100 IU/ml) treatment.  c and d.  Fresh isolated Monos were transfected with 300 pmol STAT1 or STAT3 siRNA and treated with the indicated cytokines 2 days later. Total or phosphorylated STATs and cell surface PD-L1 expression were assessed with Western blotting and flow cytometry after 15 min or 1 day, respectively.  c.  siRNA knockdown significantly reduced total and phosphorylated STAT1 and STAT3.  d . STAT1 knockdown reduced IFN-g- and IL27-induced PD-L1 protein expression, while STAT3 knockdown reduced IL10-induced PD-L1 expression. Numbers in parentheses indicate number of normal donors having Monos with these findings
    Il 32 G, supplied by R&D Systems, 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/il 32 g/product/R&D Systems
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    93
    R&D Systems anti human gm csf monoclonal antibody
    Alterations in mRNA and protein expression of key mediators and receptors of neuroinflammation under treatment with P2X7R antagonists in U251. ( A ) <t>GM-CSF</t> mRNA expression was significantly decreased after treatment of <t>AZ10606120</t> compared to untreated control. ( B ) GM-CSF protein levels were also significantly decreased in samples treated with AZ10606120. There was no significant difference in GM-CSFRα ( C ) P2X7R ( D ), NFκB1 ( E ), and NFκB2 ( F ) mRNA expression across all treatments. Data is represented as mean ± SEM, n = 10–12 ( A , B , D ) Unpaired t-test, ( C , E , F ) 1-way ANOVA, ****P
    Anti Human Gm Csf Monoclonal Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    CCL21 neutralization abrogates microglial activation, neuronal hyperexcitability, and pain-related behaviors. a–c , Microglial activation in the VPL 4 weeks after SCI was unaffected by IgG injection ( a ), whereas neutralizing antibodies directed against CCL21 (αCCL21; b ) robustly deactivated microglia at 8 h ( b ) and 24 h ( c ). d , Quantification of Cd11b/c field area revealed significant decreases in microglial activation in animals receiving minocycline ( + p

    Journal: The Journal of Neuroscience

    Article Title: Modulation of Thalamic Nociceptive Processing after Spinal Cord Injury through Remote Activation of Thalamic Microglia by Cysteine–Cysteine Chemokine Ligand 21

    doi: 10.1523/JNEUROSCI.2209-07.2007

    Figure Lengend Snippet: CCL21 neutralization abrogates microglial activation, neuronal hyperexcitability, and pain-related behaviors. a–c , Microglial activation in the VPL 4 weeks after SCI was unaffected by IgG injection ( a ), whereas neutralizing antibodies directed against CCL21 (αCCL21; b ) robustly deactivated microglia at 8 h ( b ) and 24 h ( c ). d , Quantification of Cd11b/c field area revealed significant decreases in microglial activation in animals receiving minocycline ( + p

    Article Snippet: In a 1.0 μl total volume slowly over a period of 6 min, animals received artificial CSF (aCSF) (1.3 m m CaCl2 ·2H2 O, 2.6 m m KCl, 0.9 m m MgCl, 21.0 m m NaHCO3 , 2.5 m m Na2 HPO4 ·7H2 O, 125.0 m m NaCl, prepared in sterile H2 O) , recombinant mouse CCL21 (rmCCL21) (1.2 ng; R & D Systems, Minneapolis, MN) , goat anti-mouse CCL21 neutralizing antibody (αCCL21) (5 ng; R & D Systems) , affinity-purified normal goat IgG (13 ng; R & D Systems) , and/or minocycline (10 μg; Sigma, St. Louis, MO) ( ; ), which potently downregulates the activity of microglia in vivo ( ; ; ).

    Techniques: Neutralization, Activation Assay, Injection

    The Agrocybe cylindracea galectin (ACG)/Jacalin index reflects rheumatoid arthritis (RA) activity. a Correlation of matrix metalloproteinase-3 (MMP-3) quantities before and after immunoprecipitation (IP). Serum MMP-3 measured by turbidimetric immunoassay and MMP-3 in IP samples measured by Western blot (WB) analysis ( n = 24). b Representative data derived from antibody-overlay lectin microarray. Data are from a patient with RA who had high disease activity and a patient with RA who was in remission. Net intensity from triplicate experiments is presented as the mean ± SD. c Correlation between immunoprecipitated MMP-3 quantity and lectin signal. Patients with more than moderate disease activity are represented by open symbols ; otherwise, data are shown as filled symbols . d Correlation between the ACG/Jacalin index and Disease Activity Score in 28 joints with erythrocyte sedimentation rate (DAS28-ESR). MAL_I Maackia amurensis leukoagglutinin I, SNA Sambucus nigra agglutinin, PHA(E) Phaseolus vulgaris erythroagglutinin, NPA Narcissus pseudonarcissus agglutinin, BPL Bauhinia purpurea lectin, ABA Agaricus bisporus agglutinin, LEL Lycopersicon esculentum lectin, STL Solanum tuberosum lectin, PNA peanut agglutinin, ACA Amaranthus caudatus agglutinin, MPA Maclura pomifera agglutinin, MAH Maackia amurensis hemagglutinin, WGA wheat germ agglutinin

    Journal: Arthritis Research & Therapy

    Article Title: Alteration of matrix metalloproteinase-3 O-glycan structure as a biomarker for disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-016-1013-2

    Figure Lengend Snippet: The Agrocybe cylindracea galectin (ACG)/Jacalin index reflects rheumatoid arthritis (RA) activity. a Correlation of matrix metalloproteinase-3 (MMP-3) quantities before and after immunoprecipitation (IP). Serum MMP-3 measured by turbidimetric immunoassay and MMP-3 in IP samples measured by Western blot (WB) analysis ( n = 24). b Representative data derived from antibody-overlay lectin microarray. Data are from a patient with RA who had high disease activity and a patient with RA who was in remission. Net intensity from triplicate experiments is presented as the mean ± SD. c Correlation between immunoprecipitated MMP-3 quantity and lectin signal. Patients with more than moderate disease activity are represented by open symbols ; otherwise, data are shown as filled symbols . d Correlation between the ACG/Jacalin index and Disease Activity Score in 28 joints with erythrocyte sedimentation rate (DAS28-ESR). MAL_I Maackia amurensis leukoagglutinin I, SNA Sambucus nigra agglutinin, PHA(E) Phaseolus vulgaris erythroagglutinin, NPA Narcissus pseudonarcissus agglutinin, BPL Bauhinia purpurea lectin, ABA Agaricus bisporus agglutinin, LEL Lycopersicon esculentum lectin, STL Solanum tuberosum lectin, PNA peanut agglutinin, ACA Amaranthus caudatus agglutinin, MPA Maclura pomifera agglutinin, MAH Maackia amurensis hemagglutinin, WGA wheat germ agglutinin

    Article Snippet: Protein G-purified biotinylated anti-MMP-3 antibody (200 ng; R & D Systems, Minneapolis, MN, USA) was added to precleared samples and incubated overnight at 4 °C.

    Techniques: Activity Assay, Immunoprecipitation, Western Blot, Derivative Assay, Microarray, Sedimentation, Electron Paramagnetic Resonance, Whole Genome Amplification

    Matrix metalloproteinase-3 (MMP-3) with elevated Agrocybe cylindracea galectin (ACG)/Jacalin signals produced in local lesions reflects the degree of sialylation. a Synovial fluid MMP-3 was measured by Western blot analysis after immunoprecipitation. Patients with RA ( lanes 1–3 ) and patients with OA ( lanes 4–6 ). b Representative lectin signals derived from synovial MMP-3 (mean ± SD). c The structure of T and sialyl-T antigen. Jacalin recognizes the former. d Jacalin and ACG signals compared before and after sialic acid digestion (mean ± SD). e The estimated basic structure of MMP-3 O -glycan. ABA Agaricus bisporus agglutinin, UDA Urtica dioica agglutinin , ACA Amaranthus caudatus agglutinin, WGA wheat germ agglutinin

    Journal: Arthritis Research & Therapy

    Article Title: Alteration of matrix metalloproteinase-3 O-glycan structure as a biomarker for disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-016-1013-2

    Figure Lengend Snippet: Matrix metalloproteinase-3 (MMP-3) with elevated Agrocybe cylindracea galectin (ACG)/Jacalin signals produced in local lesions reflects the degree of sialylation. a Synovial fluid MMP-3 was measured by Western blot analysis after immunoprecipitation. Patients with RA ( lanes 1–3 ) and patients with OA ( lanes 4–6 ). b Representative lectin signals derived from synovial MMP-3 (mean ± SD). c The structure of T and sialyl-T antigen. Jacalin recognizes the former. d Jacalin and ACG signals compared before and after sialic acid digestion (mean ± SD). e The estimated basic structure of MMP-3 O -glycan. ABA Agaricus bisporus agglutinin, UDA Urtica dioica agglutinin , ACA Amaranthus caudatus agglutinin, WGA wheat germ agglutinin

    Article Snippet: Protein G-purified biotinylated anti-MMP-3 antibody (200 ng; R & D Systems, Minneapolis, MN, USA) was added to precleared samples and incubated overnight at 4 °C.

    Techniques: Produced, Western Blot, Immunoprecipitation, Derivative Assay, Whole Genome Amplification

    Schematic overview of the antibody-overlay lectin microarray. A total of 45 kinds of lectins are spotted in triplicate on the array slide. Immunoprecipitation samples were applied to them, and glycoproteins bound to the lectins through their glycans. After washing, the lectins that bound to matrix metalloproteinase (MMP)-3 glycans were detected using anti-MMP-3-specific antibody

    Journal: Arthritis Research & Therapy

    Article Title: Alteration of matrix metalloproteinase-3 O-glycan structure as a biomarker for disease activity of rheumatoid arthritis

    doi: 10.1186/s13075-016-1013-2

    Figure Lengend Snippet: Schematic overview of the antibody-overlay lectin microarray. A total of 45 kinds of lectins are spotted in triplicate on the array slide. Immunoprecipitation samples were applied to them, and glycoproteins bound to the lectins through their glycans. After washing, the lectins that bound to matrix metalloproteinase (MMP)-3 glycans were detected using anti-MMP-3-specific antibody

    Article Snippet: Protein G-purified biotinylated anti-MMP-3 antibody (200 ng; R & D Systems, Minneapolis, MN, USA) was added to precleared samples and incubated overnight at 4 °C.

    Techniques: Microarray, Immunoprecipitation

    Roles of STAT1 and STAT3 in cytokine-induced PD-L1 protein expression on monocytes.  a  and  b.  Cytokine-induced PD-L1 protein expression on Monos was associated with new  PDL1  mRNA transcription. Monos were treated with IL-1a, IL-10, IL-27, IL-32 g or IFN-g. PD-L1 mRNA and surface protein were measured by q-RT-PCR and flow cytometry after 16 h or 48 h, respectively. Fold changes in PD-L1 protein and mRNA were calculated. Representative data from Monos derived from one of two normal donors are shown.  a.  Fold changes in PD-L1 protein and mRNA levels in normal donor Monos after IL-10 (100 ng/ml), IL-32 g (100 ng/ml) or IFN-g (100 IU/ml) exposure.  b.  Fold changes of PD-L1 protein and mRNA levels in normal donor Monos after IL-1a (10 ng/ml), IL-27 (50 ng/ml) or IFN-g (100 IU/ml) treatment.  c and d.  Fresh isolated Monos were transfected with 300 pmol STAT1 or STAT3 siRNA and treated with the indicated cytokines 2 days later. Total or phosphorylated STATs and cell surface PD-L1 expression were assessed with Western blotting and flow cytometry after 15 min or 1 day, respectively.  c.  siRNA knockdown significantly reduced total and phosphorylated STAT1 and STAT3.  d . STAT1 knockdown reduced IFN-g- and IL27-induced PD-L1 protein expression, while STAT3 knockdown reduced IL10-induced PD-L1 expression. Numbers in parentheses indicate number of normal donors having Monos with these findings

    Journal: Journal for Immunotherapy of Cancer

    Article Title: Mechanisms regulating PD-L1 expression on tumor and immune cells

    doi: 10.1186/s40425-019-0770-2

    Figure Lengend Snippet: Roles of STAT1 and STAT3 in cytokine-induced PD-L1 protein expression on monocytes. a and b. Cytokine-induced PD-L1 protein expression on Monos was associated with new PDL1 mRNA transcription. Monos were treated with IL-1a, IL-10, IL-27, IL-32 g or IFN-g. PD-L1 mRNA and surface protein were measured by q-RT-PCR and flow cytometry after 16 h or 48 h, respectively. Fold changes in PD-L1 protein and mRNA were calculated. Representative data from Monos derived from one of two normal donors are shown. a. Fold changes in PD-L1 protein and mRNA levels in normal donor Monos after IL-10 (100 ng/ml), IL-32 g (100 ng/ml) or IFN-g (100 IU/ml) exposure. b. Fold changes of PD-L1 protein and mRNA levels in normal donor Monos after IL-1a (10 ng/ml), IL-27 (50 ng/ml) or IFN-g (100 IU/ml) treatment. c and d. Fresh isolated Monos were transfected with 300 pmol STAT1 or STAT3 siRNA and treated with the indicated cytokines 2 days later. Total or phosphorylated STATs and cell surface PD-L1 expression were assessed with Western blotting and flow cytometry after 15 min or 1 day, respectively. c. siRNA knockdown significantly reduced total and phosphorylated STAT1 and STAT3. d . STAT1 knockdown reduced IFN-g- and IL27-induced PD-L1 protein expression, while STAT3 knockdown reduced IL10-induced PD-L1 expression. Numbers in parentheses indicate number of normal donors having Monos with these findings

    Article Snippet: Cells were cultured in the presence of recombinant IFN-g (100 or 250 IU/ml; Biogen, Cambridge, MA), IL-1a (10 ng/ml), IL-6 (20 ng/ml), IL-10 (100 ng/ml), IL-27 (50 ng/ml) or IL-32 g (100 ng/ml; all R & D Systems, Minneapolis, MN) for the indicated time periods (Additional file : Table S2).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Flow Cytometry, Cytometry, Derivative Assay, Isolation, Transfection, Western Blot

    Alterations in mRNA and protein expression of key mediators and receptors of neuroinflammation under treatment with P2X7R antagonists in U251. ( A ) GM-CSF mRNA expression was significantly decreased after treatment of AZ10606120 compared to untreated control. ( B ) GM-CSF protein levels were also significantly decreased in samples treated with AZ10606120. There was no significant difference in GM-CSFRα ( C ) P2X7R ( D ), NFκB1 ( E ), and NFκB2 ( F ) mRNA expression across all treatments. Data is represented as mean ± SEM, n = 10–12 ( A , B , D ) Unpaired t-test, ( C , E , F ) 1-way ANOVA, ****P

    Journal: Scientific Reports

    Article Title: Inhibition of purinergic P2X receptor 7 (P2X7R) decreases granulocyte-macrophage colony-stimulating factor (GM-CSF) expression in U251 glioblastoma cells

    doi: 10.1038/s41598-020-71887-x

    Figure Lengend Snippet: Alterations in mRNA and protein expression of key mediators and receptors of neuroinflammation under treatment with P2X7R antagonists in U251. ( A ) GM-CSF mRNA expression was significantly decreased after treatment of AZ10606120 compared to untreated control. ( B ) GM-CSF protein levels were also significantly decreased in samples treated with AZ10606120. There was no significant difference in GM-CSFRα ( C ) P2X7R ( D ), NFκB1 ( E ), and NFκB2 ( F ) mRNA expression across all treatments. Data is represented as mean ± SEM, n = 10–12 ( A , B , D ) Unpaired t-test, ( C , E , F ) 1-way ANOVA, ****P

    Article Snippet: ReagentsCells were grown to 70% confluency and then treated for 72 h unless specified otherwise with the following reagents: human GM-CSF (15 ng/mL; R & D Systems), AZ10606120 (15 μM; Sigma), anti-human GM-CSF monoclonal antibody (20 ng/mL; R & D Systems) and Temozolomide (TMZ; 50 μM; Sigma).

    Techniques: Expressing

    Diagrammatic representation of AZ10606120 interactions with P2X7R and GM-CSF and its effects on tumour growth. P2X7R acts through NFκB to release cytokines and growth factors that can increase tumour growth. AZ10606120 is an antagonist that inhibits P2X7R and leads to a reduction in GM-CSF production in the U251 cells as well as inhibiting tumour proliferation. GM-CSFRβ is not expressed in the U251 cell line, and a role of GM-CSFRα signalling has not yet been identified.

    Journal: Scientific Reports

    Article Title: Inhibition of purinergic P2X receptor 7 (P2X7R) decreases granulocyte-macrophage colony-stimulating factor (GM-CSF) expression in U251 glioblastoma cells

    doi: 10.1038/s41598-020-71887-x

    Figure Lengend Snippet: Diagrammatic representation of AZ10606120 interactions with P2X7R and GM-CSF and its effects on tumour growth. P2X7R acts through NFκB to release cytokines and growth factors that can increase tumour growth. AZ10606120 is an antagonist that inhibits P2X7R and leads to a reduction in GM-CSF production in the U251 cells as well as inhibiting tumour proliferation. GM-CSFRβ is not expressed in the U251 cell line, and a role of GM-CSFRα signalling has not yet been identified.

    Article Snippet: ReagentsCells were grown to 70% confluency and then treated for 72 h unless specified otherwise with the following reagents: human GM-CSF (15 ng/mL; R & D Systems), AZ10606120 (15 μM; Sigma), anti-human GM-CSF monoclonal antibody (20 ng/mL; R & D Systems) and Temozolomide (TMZ; 50 μM; Sigma).

    Techniques: