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  • 99
    Thermo Fisher g bmmc medium rpmi 1640 medium
    G Bmmc Medium Rpmi 1640 Medium, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore safranin o bmmcs
    Safranin O Bmmcs, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    AllCells LLC bmmcs
    Bmmcs, supplied by AllCells LLC, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Becton Dickinson bmmcs
    Representative FACS histograms of bone marrow mononuclear cells and CD11b + monocytes isolated by <t>immunomagnetic</t> separation. <t>BMMCs:</t> Bone marrow mononuclear cells.
    Bmmcs, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 99/100, based on 397 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher bmmcs
    Representative FACS histograms of bone marrow mononuclear cells and CD11b + monocytes isolated by <t>immunomagnetic</t> separation. <t>BMMCs:</t> Bone marrow mononuclear cells.
    Bmmcs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 835 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bmmcs  (GBF)
    85
    GBF bmmcs
    Generation of <t>BMMCs</t> expressing <t>GBF-DsRed2.</t> (A) Bone marrow was infected with an MSCV-based retroviral plasmid encoding DsRed2 vector alone or fused to the GBF, differentiated into bone marrow-derived mast cells, and then FACS sorted for expression of
    Bmmcs, supplied by GBF, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    PeproTech bmmc
    Type I IFN-induced Nos2 expression post- PD-1 blockade in the TME. a Microarray analysis and qRT-PCR analyses of TILs in MC38 during PD-1 blockade. CD45 + cells from MC38 tumors were cell-sorted 48 h post-1, 2 injections of anti-PD-1 or isotype control mAbs to perform trancriptomic analyses. Heat-map depicting the shared significant downregulated and upregulated genes in the anti-PD-1 treated groups compared with the isotype control treated groups across time points 1 and 2. b Relative expression of Nos2 in CD45 + cells from MC38 tumors 48 h after 1, 2, 3 and 4 injections of anti-PD-1 or Isotype mAbs using qRT-PCR analyses. c and g Same as b with MCA205WT tumor bearers after treatment with 1, 2, 3 and 4 injections of mAbs evaluated in both CD45 + c and CD45 − g fractions. d and h Representative gating strategy and flow cytometric analyses of NOS2 protein expression in CD45 + cells d and in the CD45 - fraction h , 48 h after the fourth injection of anti-PD-1 or its isotype control mAbs. e , f Relative expression of Nos2 quantified by qRT-PCR following stimulations of <t>BMDCs</t> and <t>BMMCs</t> e or various tumor cell lines f with either IFNα, IFNγ or LPS. Each dot corresponds to one stimulated sample or 1 mouse with 2 or more biological replicates per experiment and 5 mice per group per time point per experiment. Graphs depict 1 experiment ( b , time points 3 and 4, d and h ), are representative of 1 experiment out of 2–3 performed ( b , time points 1 and 2), or are the pool of 2–3 independent experiments c , e – g including biological replicates for each experiment. Unpaired t -tests were used to compare two groups ( b – d , f for AT3 tumor model and g , h ). ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups e , f . * p
    Bmmc, supplied by PeproTech, used in various techniques. Bioz Stars score: 94/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore bmmcs
    Type I IFN-induced Nos2 expression post- PD-1 blockade in the TME. a Microarray analysis and qRT-PCR analyses of TILs in MC38 during PD-1 blockade. CD45 + cells from MC38 tumors were cell-sorted 48 h post-1, 2 injections of anti-PD-1 or isotype control mAbs to perform trancriptomic analyses. Heat-map depicting the shared significant downregulated and upregulated genes in the anti-PD-1 treated groups compared with the isotype control treated groups across time points 1 and 2. b Relative expression of Nos2 in CD45 + cells from MC38 tumors 48 h after 1, 2, 3 and 4 injections of anti-PD-1 or Isotype mAbs using qRT-PCR analyses. c and g Same as b with MCA205WT tumor bearers after treatment with 1, 2, 3 and 4 injections of mAbs evaluated in both CD45 + c and CD45 − g fractions. d and h Representative gating strategy and flow cytometric analyses of NOS2 protein expression in CD45 + cells d and in the CD45 - fraction h , 48 h after the fourth injection of anti-PD-1 or its isotype control mAbs. e , f Relative expression of Nos2 quantified by qRT-PCR following stimulations of <t>BMDCs</t> and <t>BMMCs</t> e or various tumor cell lines f with either IFNα, IFNγ or LPS. Each dot corresponds to one stimulated sample or 1 mouse with 2 or more biological replicates per experiment and 5 mice per group per time point per experiment. Graphs depict 1 experiment ( b , time points 3 and 4, d and h ), are representative of 1 experiment out of 2–3 performed ( b , time points 1 and 2), or are the pool of 2–3 independent experiments c , e – g including biological replicates for each experiment. Unpaired t -tests were used to compare two groups ( b – d , f for AT3 tumor model and g , h ). ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups e , f . * p
    Bmmcs, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 584 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    BioVision bmmc
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Bmmc, supplied by BioVision, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cedarlane bmmc
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Bmmc, supplied by Cedarlane, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bmmc  (Sepax)
    85
    Sepax bmmc
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Bmmc, supplied by Sepax, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Cellgro bmmcs
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Bmmcs, supplied by Cellgro, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Atlanta Biologicals bmmc media
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Bmmc Media, supplied by Atlanta Biologicals, used in various techniques. Bioz Stars score: 95/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    STEMCELL Technologies Inc control bmmc
    Silica induces <t>LDH</t> release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in <t>BMMC.</t> ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC
    Control Bmmc, supplied by STEMCELL Technologies Inc, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Amaxa c57bl 6 bmmc
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    C57bl 6 Bmmc, supplied by Amaxa, used in various techniques. Bioz Stars score: 87/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Amaxa grk2 deleted bmmcs
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Grk2 Deleted Bmmcs, supplied by Amaxa, used in various techniques. Bioz Stars score: 87/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher bmmc derived scs
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Bmmc Derived Scs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Amaxa bmmc nucleofector ii
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Bmmc Nucleofector Ii, supplied by Amaxa, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Matsunami Glass confocal microscopy bmmcs
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Confocal Microscopy Bmmcs, supplied by Matsunami Glass, 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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    80
    10X Genomics frozen bmmcs healthy donors 1
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Frozen Bmmcs Healthy Donors 1, supplied by 10X Genomics, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Conversant Bio primary mm samples human bmmcs
    <t>C57BL/6</t> and 129/Sv <t>BMMC</t> show variation in TGFβ1 responsiveness
    Primary Mm Samples Human Bmmcs, supplied by Conversant Bio, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Millipore bmmc mouse anti dinitrophenol
    Treatment of mast cells with LatA results in altered F-actin localization, diminished membrane expression of rafts and F-actin, and impaired F-actin + cytoneme formation. (A) Effects of LatA treatment on F-actin, GM1 localization, and cell morphology, in <t>BMMC.</t> BMMC were treated with 250 ng/ml of Latrunculin A for 45 min, then left unstimulated (i), sensitized overnight (ii), sensitized and cross-linked with antigen for 5 min (iii) or sensitized and stimulated with antigen and MIP-1α for 5 min (iv). After permeabilization using 0.1% triton X100, cells were stained for F-actin using phalloidin-Alexa 488 and for GM1 + rafts using cholera toxin-Alexa 555. Differential-interference-contrast (DIC) images are also provided to show the nuclear structure. N, nucleus. (B) Sensitized <t>RBL-CCR1</t> cells, untreated and treated with LatA. The untreated cells (top left panel) display typical basophil morphology and lack cytonemes. Cells treated with LatA (top right panel) lack typical basophil cytoskeleton morphology, and instead display cell swelling and small radial elongations (not cytonemes). Cross-linked or costimulated BMMC treated with LatA (bottom panels) failed to produce directional cytoneme extensions ( > 50 μm) and instead formed short branched extensions. Cells were stained for F-actin (phalloidin) and GM1 as described above. The proportion of cells producing cytonemes, shown in the graph, was determined by manually examining 30 cells/condition in 3 separate experiments. ***, P
    Bmmc Mouse Anti Dinitrophenol, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher slp 76 deficient bmmc cultures
    Tyrosine phosphorylation of PLC-γ in response to FcɛRI ligation. (A) Tyrosine phosphorylation of <t>SLP-76</t> and coimmunoprecipitation with btk and Vav. <t>BMMC</t> were sensitized with rat IgE (2.5 μg of rat IgE per ml) followed by cross-linking with F(ab′) 2 anti-rat Ig (10 μg/ml) and incubated for 2 min at 37°C. Cell lysates were immunoprecipitated (IP) with rabbit anti-SLP-76 antiserum. Membrane was successively probed with anti-pTyr, anti-btk, anti-SLP-76, and anti-Vav antibodies. The degree of association of SLP-76 with btk and Vav after stimulation was normalized to the signal for SLP-76 as determined by densitometry. Similar results were obtained in two experiments. (B) Tyrosine phosphorylation of PLC-γ1 and PLC-γ2 in WT and SLP-76 −/− BMMC. BMMC were sensitized with IgE and stimulated for 7 min as described above. Cell lysates were immunoprecipitated with anti-PLC-γ1 and anti-PLC-γ2. PLC-γ1/2 tyrosine phosphorylation was analyzed by immunoblotting with antiphosphotyrosine antibody (4G10). The membranes were reprobed with anti-PLC-γ1 and anti-PLC-γ2 to control for loading. (C) Tyrosine phosphorylation of PLC-γ2 in SLP-76-reconstituted BMMC. The top two sets of lanes represent a single experiment with cells stimulated simultaneously and then processed in parallel. The bottom set of lanes represents a separate experiment for SLP-76 YYF. Membranes were reprobed with anti-PLC-γ2 to control for loading. Similar results were found in three different experiments. Fold induction normalized to signal for loading was determined by densitometry.
    Slp 76 Deficient Bmmc Cultures, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC bone marrow mononuclear cells
    MVNP regulation of SIRPβ1 signaling in preosteoclast <t>cells.</t> (A) MVNP enhances SIRPβ1 interaction with DAP12 in <t>normal</t> <t>human</t> <t>bone</t> <t>marrow</t> <t>mononuclear</t> cells. Cells were transduced with EV or MVNP and stimulated with and without M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total cell lysates obtained from these cells were subjected to immunoprecipitation using anti -DAP12 or control IgG antibodies. Immunoprecipitants were subjected to western blot analysis for SIRPβ1. Total DAP12 expressions in these cells were served for loading control. (B) shRNA suppression of SIRPβ1 inhibits MVNP increased p-syk expression. Normal human bone marrow derived mononuclear cells were transduced with EV or MVNP in the presence and absence of SIRPβ1 shRNA and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 24 h. Total cell lysates were subjected to western blot analysis for p-syk and syk expression.
    Bone Marrow Mononuclear Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher cd138 bmmcs
    HDAC3 expression is increased in MM-derived BMSC compared to healthy donor-derived BMSC but HDAC3 is not necessary for BMSC viability or proliferation. (a) Gene expression analysis from the IFM/DFCI 2009 dataset revealed that HDAC3 expression is higher in <t>CD138-</t> <t>BMMCs</t> when compared to CD138+ BMMCs derived from patients with MM. (b) Co-culture of HS-5 cells with MM1S.Luc triggers induction of HDAC3 expression in BMSC. GAPDH was used as loading control. Quantification was performed using ImageJ. (c) HDAC3 KO HS-5 cells have comparable viability to HDAC3 WT HS-5 cells as assessed by CCK-8 assay. (d) HDAC3 inhibition using BG45 is not cytotoxic towards HS-5 even at doses two-folds higher than the Ec50 of MM1S as measured by CCK-8 assay at 96 hours. (e) Endothelial tube formation assay shows compromised formation of endothelial tubes in BMEC60 cells transfected with HDAC3 siRNA compared to scrambled siRNA. Two representative, independent experiments shown.
    Cd138 Bmmcs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC bmmc growth medium
    HDAC3 expression is increased in MM-derived BMSC compared to healthy donor-derived BMSC but HDAC3 is not necessary for BMSC viability or proliferation. (a) Gene expression analysis from the IFM/DFCI 2009 dataset revealed that HDAC3 expression is higher in <t>CD138-</t> <t>BMMCs</t> when compared to CD138+ BMMCs derived from patients with MM. (b) Co-culture of HS-5 cells with MM1S.Luc triggers induction of HDAC3 expression in BMSC. GAPDH was used as loading control. Quantification was performed using ImageJ. (c) HDAC3 KO HS-5 cells have comparable viability to HDAC3 WT HS-5 cells as assessed by CCK-8 assay. (d) HDAC3 inhibition using BG45 is not cytotoxic towards HS-5 even at doses two-folds higher than the Ec50 of MM1S as measured by CCK-8 assay at 96 hours. (e) Endothelial tube formation assay shows compromised formation of endothelial tubes in BMEC60 cells transfected with HDAC3 siRNA compared to scrambled siRNA. Two representative, independent experiments shown.
    Bmmc Growth Medium, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Representative FACS histograms of bone marrow mononuclear cells and CD11b + monocytes isolated by immunomagnetic separation. BMMCs: Bone marrow mononuclear cells.

    Journal: World Journal of Gastroenterology

    Article Title: Bone marrow-derived monocyte infusion improves hepatic fibrosis by decreasing osteopontin, TGF-β1, IL-13 and oxidative stress

    doi: 10.3748/wjg.v23.i28.5146

    Figure Lengend Snippet: Representative FACS histograms of bone marrow mononuclear cells and CD11b + monocytes isolated by immunomagnetic separation. BMMCs: Bone marrow mononuclear cells.

    Article Snippet: Cell characterization The BMMCs and monocytes obtained by immunomagnetic separation were first incubated with Anti-CD11b (PE Rat Anti-Mouse CD11b, M1/70 clone, BD Pharmingen™, San Jose, CA, United States), Anti-CD14 (FITC Rat Anti-Mouse CD14, rmC5-3 clone; BD Pharmingen™), Anti-CD45 (APC Rat Anti-Mouse CD45, 30-F11 clone; BD Pharmingen™), Anti-CD34 (PE Rat Anti-Mouse CD34, RAM34 clone; BD Pharmingen™) and Anti-Ly6A (FITC Rat Anti-Mouse Ly-6A/E, D & clone; BD Pharmingen™).

    Techniques: FACS, Isolation, Immunomagnetic Separation

    Generation of BMMCs expressing GBF-DsRed2. (A) Bone marrow was infected with an MSCV-based retroviral plasmid encoding DsRed2 vector alone or fused to the GBF, differentiated into bone marrow-derived mast cells, and then FACS sorted for expression of

    Journal:

    Article Title: Disruption of SLP-76 Interaction with Gads Inhibits Dynamic Clustering of SLP-76 and Fc?RI Signaling in Mast Cells †

    doi: 10.1128/MCB.26.5.1826-1838.2006

    Figure Lengend Snippet: Generation of BMMCs expressing GBF-DsRed2. (A) Bone marrow was infected with an MSCV-based retroviral plasmid encoding DsRed2 vector alone or fused to the GBF, differentiated into bone marrow-derived mast cells, and then FACS sorted for expression of

    Article Snippet: BMMCs expressing either GBF or vector were stimulated for 24 h by cross-linking the FcɛRI receptor with antigen.

    Techniques: Expressing, Infection, Plasmid Preparation, Derivative Assay, FACS

    GBF expression blocks FcɛRI signaling in BMMCs. (A) Anti-DNP IgE-sensitized unsorted BMMCs expressing GBF-DsRed2 or DsRed2 vector alone were loaded with the calcium-sensitive dye Indo-1 and assayed for calcium flux by flow cytometry. Cells were

    Journal:

    Article Title: Disruption of SLP-76 Interaction with Gads Inhibits Dynamic Clustering of SLP-76 and Fc?RI Signaling in Mast Cells †

    doi: 10.1128/MCB.26.5.1826-1838.2006

    Figure Lengend Snippet: GBF expression blocks FcɛRI signaling in BMMCs. (A) Anti-DNP IgE-sensitized unsorted BMMCs expressing GBF-DsRed2 or DsRed2 vector alone were loaded with the calcium-sensitive dye Indo-1 and assayed for calcium flux by flow cytometry. Cells were

    Article Snippet: BMMCs expressing either GBF or vector were stimulated for 24 h by cross-linking the FcɛRI receptor with antigen.

    Techniques: Expressing, Plasmid Preparation, Flow Cytometry, Cytometry

    Type I IFN-induced Nos2 expression post- PD-1 blockade in the TME. a Microarray analysis and qRT-PCR analyses of TILs in MC38 during PD-1 blockade. CD45 + cells from MC38 tumors were cell-sorted 48 h post-1, 2 injections of anti-PD-1 or isotype control mAbs to perform trancriptomic analyses. Heat-map depicting the shared significant downregulated and upregulated genes in the anti-PD-1 treated groups compared with the isotype control treated groups across time points 1 and 2. b Relative expression of Nos2 in CD45 + cells from MC38 tumors 48 h after 1, 2, 3 and 4 injections of anti-PD-1 or Isotype mAbs using qRT-PCR analyses. c and g Same as b with MCA205WT tumor bearers after treatment with 1, 2, 3 and 4 injections of mAbs evaluated in both CD45 + c and CD45 − g fractions. d and h Representative gating strategy and flow cytometric analyses of NOS2 protein expression in CD45 + cells d and in the CD45 - fraction h , 48 h after the fourth injection of anti-PD-1 or its isotype control mAbs. e , f Relative expression of Nos2 quantified by qRT-PCR following stimulations of BMDCs and BMMCs e or various tumor cell lines f with either IFNα, IFNγ or LPS. Each dot corresponds to one stimulated sample or 1 mouse with 2 or more biological replicates per experiment and 5 mice per group per time point per experiment. Graphs depict 1 experiment ( b , time points 3 and 4, d and h ), are representative of 1 experiment out of 2–3 performed ( b , time points 1 and 2), or are the pool of 2–3 independent experiments c , e – g including biological replicates for each experiment. Unpaired t -tests were used to compare two groups ( b – d , f for AT3 tumor model and g , h ). ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups e , f . * p

    Journal: Cell Research

    Article Title: Sustained Type I interferon signaling as a mechanism of resistance to PD-1 blockade

    doi: 10.1038/s41422-019-0224-x

    Figure Lengend Snippet: Type I IFN-induced Nos2 expression post- PD-1 blockade in the TME. a Microarray analysis and qRT-PCR analyses of TILs in MC38 during PD-1 blockade. CD45 + cells from MC38 tumors were cell-sorted 48 h post-1, 2 injections of anti-PD-1 or isotype control mAbs to perform trancriptomic analyses. Heat-map depicting the shared significant downregulated and upregulated genes in the anti-PD-1 treated groups compared with the isotype control treated groups across time points 1 and 2. b Relative expression of Nos2 in CD45 + cells from MC38 tumors 48 h after 1, 2, 3 and 4 injections of anti-PD-1 or Isotype mAbs using qRT-PCR analyses. c and g Same as b with MCA205WT tumor bearers after treatment with 1, 2, 3 and 4 injections of mAbs evaluated in both CD45 + c and CD45 − g fractions. d and h Representative gating strategy and flow cytometric analyses of NOS2 protein expression in CD45 + cells d and in the CD45 - fraction h , 48 h after the fourth injection of anti-PD-1 or its isotype control mAbs. e , f Relative expression of Nos2 quantified by qRT-PCR following stimulations of BMDCs and BMMCs e or various tumor cell lines f with either IFNα, IFNγ or LPS. Each dot corresponds to one stimulated sample or 1 mouse with 2 or more biological replicates per experiment and 5 mice per group per time point per experiment. Graphs depict 1 experiment ( b , time points 3 and 4, d and h ), are representative of 1 experiment out of 2–3 performed ( b , time points 1 and 2), or are the pool of 2–3 independent experiments c , e – g including biological replicates for each experiment. Unpaired t -tests were used to compare two groups ( b – d , f for AT3 tumor model and g , h ). ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups e , f . * p

    Article Snippet: After red blood cell lysis with ACK buffer, cells were cultured in IMDM supplemented with 10% of FCS + 2 mM l -Glutamine + 100 UI/mL Penicillin/Streptomycin + 50 µM 2-mercaptoethanol (Sigma-Aldrich) (referred herein as complete IMDM medium) at 0.5 × 106 /mL and treated with 10 ng/mL of GM-CSF and IL-4 for BMDCs and 50 ng/mL of M-CSF for BMMCs (all from Peprotech).

    Techniques: Expressing, Microarray, Quantitative RT-PCR, Flow Cytometry, Injection, Mouse Assay

    Sources and kinetics of Type I IFN in the TME during PD-1 inhibition. a and b In vitro assays. Relative expression of Ifnβ1 quantified by qRT-PCR following stimulations of various tumor cell lines or BMDCs and BMMCs with IFNα, IFNγ or LPS. Each dot represents one sample and graphs represent 1 experiment or are the pool of 2 to 3 independent experiments including biological replicates for each experiment. Unpaired t-tests were used to compare 2 groups. ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups. c – h In vivo studies. Flow cytometry sorting of CD45 + live fractions from the TME of MCA205WT c – e or MC38 f – h tumors 48 h after 1, 2, 3 or 4 i.p. administrations of anti-PD-1 (or isotype control) mAb. Relative expression of Ifnβ1 c and f and IFN-sensitive gene products d , e , g , h quantified by qRT-PCR. Unpaired t-tests were used to compared transcription levels between the anti-PD-1 and isotype control treated groups for each time point. Each dot represents 1 mouse with 5 mice per time point per experiment. Graphs represent 1 representative experiment out of 2–3 independent experiments (MC38, time points 1 and 2, d , e ), 1 experiment (MC38, time points 3 and 4) or are the pool of 2–3 independent experiments c . * p

    Journal: Cell Research

    Article Title: Sustained Type I interferon signaling as a mechanism of resistance to PD-1 blockade

    doi: 10.1038/s41422-019-0224-x

    Figure Lengend Snippet: Sources and kinetics of Type I IFN in the TME during PD-1 inhibition. a and b In vitro assays. Relative expression of Ifnβ1 quantified by qRT-PCR following stimulations of various tumor cell lines or BMDCs and BMMCs with IFNα, IFNγ or LPS. Each dot represents one sample and graphs represent 1 experiment or are the pool of 2 to 3 independent experiments including biological replicates for each experiment. Unpaired t-tests were used to compare 2 groups. ANOVA statistical tests and pairwise comparisons with Bonferroni adjustment were adopted for more than 2 groups. c – h In vivo studies. Flow cytometry sorting of CD45 + live fractions from the TME of MCA205WT c – e or MC38 f – h tumors 48 h after 1, 2, 3 or 4 i.p. administrations of anti-PD-1 (or isotype control) mAb. Relative expression of Ifnβ1 c and f and IFN-sensitive gene products d , e , g , h quantified by qRT-PCR. Unpaired t-tests were used to compared transcription levels between the anti-PD-1 and isotype control treated groups for each time point. Each dot represents 1 mouse with 5 mice per time point per experiment. Graphs represent 1 representative experiment out of 2–3 independent experiments (MC38, time points 1 and 2, d , e ), 1 experiment (MC38, time points 3 and 4) or are the pool of 2–3 independent experiments c . * p

    Article Snippet: After red blood cell lysis with ACK buffer, cells were cultured in IMDM supplemented with 10% of FCS + 2 mM l -Glutamine + 100 UI/mL Penicillin/Streptomycin + 50 µM 2-mercaptoethanol (Sigma-Aldrich) (referred herein as complete IMDM medium) at 0.5 × 106 /mL and treated with 10 ng/mL of GM-CSF and IL-4 for BMDCs and 50 ng/mL of M-CSF for BMMCs (all from Peprotech).

    Techniques: Inhibition, In Vitro, Expressing, Quantitative RT-PCR, In Vivo, Flow Cytometry, Cytometry, Mouse Assay

    Silica induces LDH release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in BMMC. ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC

    Journal:

    Article Title: Silica-Directed Mast Cell Activation Is Enhanced by Scavenger Receptors

    doi: 10.1165/rcmb.2006-0197OC

    Figure Lengend Snippet: Silica induces LDH release, apoptosis, and ROS production, but has little effect on β-hexosaminidase release in BMMC. ( A ) LDH release was measured in supernatant of silica-exposed BMMC. ( B ) Apoptosis was determined by DNA fragmentation in BMMC

    Article Snippet: The percentage of LDH release was measured in supernatants of BMMC exposed to silica for 24 h (BioVision, Mountain View, CA).

    Techniques:

    C57BL/6 and 129/Sv BMMC show variation in TGFβ1 responsiveness

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

    Article Title: Genotype-dependent Effects of TGFβ1 on Mast Cell Function: Targeting the Stat5 Pathway

    doi: 10.4049/jimmunol.1202723

    Figure Lengend Snippet: C57BL/6 and 129/Sv BMMC show variation in TGFβ1 responsiveness

    Article Snippet: To determine if altered Stat5 regulation is functionally important, Stat5B was overexpressed (approximately 2-fold) in C57BL/6 BMMC by transfection ( ).

    Techniques:

    Treatment of mast cells with LatA results in altered F-actin localization, diminished membrane expression of rafts and F-actin, and impaired F-actin + cytoneme formation. (A) Effects of LatA treatment on F-actin, GM1 localization, and cell morphology, in BMMC. BMMC were treated with 250 ng/ml of Latrunculin A for 45 min, then left unstimulated (i), sensitized overnight (ii), sensitized and cross-linked with antigen for 5 min (iii) or sensitized and stimulated with antigen and MIP-1α for 5 min (iv). After permeabilization using 0.1% triton X100, cells were stained for F-actin using phalloidin-Alexa 488 and for GM1 + rafts using cholera toxin-Alexa 555. Differential-interference-contrast (DIC) images are also provided to show the nuclear structure. N, nucleus. (B) Sensitized RBL-CCR1 cells, untreated and treated with LatA. The untreated cells (top left panel) display typical basophil morphology and lack cytonemes. Cells treated with LatA (top right panel) lack typical basophil cytoskeleton morphology, and instead display cell swelling and small radial elongations (not cytonemes). Cross-linked or costimulated BMMC treated with LatA (bottom panels) failed to produce directional cytoneme extensions ( > 50 μm) and instead formed short branched extensions. Cells were stained for F-actin (phalloidin) and GM1 as described above. The proportion of cells producing cytonemes, shown in the graph, was determined by manually examining 30 cells/condition in 3 separate experiments. ***, P

    Journal: International Immunology

    Article Title: Interaction between activated chemokine receptor 1 and Fc?RI at membrane rafts promotes communication and F-actin-rich cytoneme extensions between mast cells

    doi: 10.1093/intimm/dxp118

    Figure Lengend Snippet: Treatment of mast cells with LatA results in altered F-actin localization, diminished membrane expression of rafts and F-actin, and impaired F-actin + cytoneme formation. (A) Effects of LatA treatment on F-actin, GM1 localization, and cell morphology, in BMMC. BMMC were treated with 250 ng/ml of Latrunculin A for 45 min, then left unstimulated (i), sensitized overnight (ii), sensitized and cross-linked with antigen for 5 min (iii) or sensitized and stimulated with antigen and MIP-1α for 5 min (iv). After permeabilization using 0.1% triton X100, cells were stained for F-actin using phalloidin-Alexa 488 and for GM1 + rafts using cholera toxin-Alexa 555. Differential-interference-contrast (DIC) images are also provided to show the nuclear structure. N, nucleus. (B) Sensitized RBL-CCR1 cells, untreated and treated with LatA. The untreated cells (top left panel) display typical basophil morphology and lack cytonemes. Cells treated with LatA (top right panel) lack typical basophil cytoskeleton morphology, and instead display cell swelling and small radial elongations (not cytonemes). Cross-linked or costimulated BMMC treated with LatA (bottom panels) failed to produce directional cytoneme extensions ( > 50 μm) and instead formed short branched extensions. Cells were stained for F-actin (phalloidin) and GM1 as described above. The proportion of cells producing cytonemes, shown in the graph, was determined by manually examining 30 cells/condition in 3 separate experiments. ***, P

    Article Snippet: Cells were kept unsensitized or were sensitized by treatment with 22 ng ml−1 (RBL cells) or 100 ng ml−1 (BMMC) mouse anti-dinitrophenol (DNP) IgE mAb (Sigma, St Louis, MO, USA) overnight at 37°C in 5% CO2 .

    Techniques: Expressing, Staining

    Tyrosine phosphorylation of PLC-γ in response to FcɛRI ligation. (A) Tyrosine phosphorylation of SLP-76 and coimmunoprecipitation with btk and Vav. BMMC were sensitized with rat IgE (2.5 μg of rat IgE per ml) followed by cross-linking with F(ab′) 2 anti-rat Ig (10 μg/ml) and incubated for 2 min at 37°C. Cell lysates were immunoprecipitated (IP) with rabbit anti-SLP-76 antiserum. Membrane was successively probed with anti-pTyr, anti-btk, anti-SLP-76, and anti-Vav antibodies. The degree of association of SLP-76 with btk and Vav after stimulation was normalized to the signal for SLP-76 as determined by densitometry. Similar results were obtained in two experiments. (B) Tyrosine phosphorylation of PLC-γ1 and PLC-γ2 in WT and SLP-76 −/− BMMC. BMMC were sensitized with IgE and stimulated for 7 min as described above. Cell lysates were immunoprecipitated with anti-PLC-γ1 and anti-PLC-γ2. PLC-γ1/2 tyrosine phosphorylation was analyzed by immunoblotting with antiphosphotyrosine antibody (4G10). The membranes were reprobed with anti-PLC-γ1 and anti-PLC-γ2 to control for loading. (C) Tyrosine phosphorylation of PLC-γ2 in SLP-76-reconstituted BMMC. The top two sets of lanes represent a single experiment with cells stimulated simultaneously and then processed in parallel. The bottom set of lanes represents a separate experiment for SLP-76 YYF. Membranes were reprobed with anti-PLC-γ2 to control for loading. Similar results were found in three different experiments. Fold induction normalized to signal for loading was determined by densitometry.

    Journal: Molecular and Cellular Biology

    Article Title: Structural Requirements of SLP-76 in Signaling via the High-Affinity Immunoglobulin E Receptor (Fc?RI) in Mast Cells

    doi: 10.1128/MCB.23.7.2395-2406.2003

    Figure Lengend Snippet: Tyrosine phosphorylation of PLC-γ in response to FcɛRI ligation. (A) Tyrosine phosphorylation of SLP-76 and coimmunoprecipitation with btk and Vav. BMMC were sensitized with rat IgE (2.5 μg of rat IgE per ml) followed by cross-linking with F(ab′) 2 anti-rat Ig (10 μg/ml) and incubated for 2 min at 37°C. Cell lysates were immunoprecipitated (IP) with rabbit anti-SLP-76 antiserum. Membrane was successively probed with anti-pTyr, anti-btk, anti-SLP-76, and anti-Vav antibodies. The degree of association of SLP-76 with btk and Vav after stimulation was normalized to the signal for SLP-76 as determined by densitometry. Similar results were obtained in two experiments. (B) Tyrosine phosphorylation of PLC-γ1 and PLC-γ2 in WT and SLP-76 −/− BMMC. BMMC were sensitized with IgE and stimulated for 7 min as described above. Cell lysates were immunoprecipitated with anti-PLC-γ1 and anti-PLC-γ2. PLC-γ1/2 tyrosine phosphorylation was analyzed by immunoblotting with antiphosphotyrosine antibody (4G10). The membranes were reprobed with anti-PLC-γ1 and anti-PLC-γ2 to control for loading. (C) Tyrosine phosphorylation of PLC-γ2 in SLP-76-reconstituted BMMC. The top two sets of lanes represent a single experiment with cells stimulated simultaneously and then processed in parallel. The bottom set of lanes represents a separate experiment for SLP-76 YYF. Membranes were reprobed with anti-PLC-γ2 to control for loading. Similar results were found in three different experiments. Fold induction normalized to signal for loading was determined by densitometry.

    Article Snippet: Viral particle-containing supernatant was added to SLP-76-deficient BMMC cultures prestimulated with stem cell factor (Biosource International) and 8 μg of Polybrene per ml (Sigma, St. Louis, Mo.) in fibronectin (Sigma)-coated plates.

    Techniques: Planar Chromatography, Ligation, Incubation, Immunoprecipitation

    Retroviral transduction with SLP-76 reconstitutes FcɛRI-mediated signaling in SLP-76 −/− mast cells. (A) IgE receptor expression on BMMC from WT, SLP-76 −/− (KO) mice, and SLP-76 −/− BMMC reconstituted (reconst.) with control vector or WT SLP-76. Cells were treated with mouse IgE and then incubated with biotinylated anti-IgE and streptavidin-CyChrome (solid line). Control staining was with biotinylated anti-IgE and streptavidin-CyChrome alone (dashed line). (B) SLP-76 protein expression was assessed by immunoblotting after separation of proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. (C) Calcium mobilization was detected in BMMC loaded with indo 1-AM. BMMC (10 × 10 6 /ml) were sensitized with IgE (5 μg/ml) for 1 h at room temperature and then stimulated with 25 μg of F(ab′) 2 anti-rat Ig per ml followed later by ionomycin (10 μM) at the indicated time points. Results are expressed as percentage of ionomycin-induced calcium mobilization. (D) Release of β-hexosaminidase. BMMC (10 6 ) were incubated with 2.5 μg of IgE per ml for 1 h on ice and then stimulated with F(ab′) 2 anti-rat Ig at the indicated concentrations. The results represent the mean ± standard deviation of three experiments, each performed in duplicate. **, P

    Journal: Molecular and Cellular Biology

    Article Title: Structural Requirements of SLP-76 in Signaling via the High-Affinity Immunoglobulin E Receptor (Fc?RI) in Mast Cells

    doi: 10.1128/MCB.23.7.2395-2406.2003

    Figure Lengend Snippet: Retroviral transduction with SLP-76 reconstitutes FcɛRI-mediated signaling in SLP-76 −/− mast cells. (A) IgE receptor expression on BMMC from WT, SLP-76 −/− (KO) mice, and SLP-76 −/− BMMC reconstituted (reconst.) with control vector or WT SLP-76. Cells were treated with mouse IgE and then incubated with biotinylated anti-IgE and streptavidin-CyChrome (solid line). Control staining was with biotinylated anti-IgE and streptavidin-CyChrome alone (dashed line). (B) SLP-76 protein expression was assessed by immunoblotting after separation of proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. (C) Calcium mobilization was detected in BMMC loaded with indo 1-AM. BMMC (10 × 10 6 /ml) were sensitized with IgE (5 μg/ml) for 1 h at room temperature and then stimulated with 25 μg of F(ab′) 2 anti-rat Ig per ml followed later by ionomycin (10 μM) at the indicated time points. Results are expressed as percentage of ionomycin-induced calcium mobilization. (D) Release of β-hexosaminidase. BMMC (10 6 ) were incubated with 2.5 μg of IgE per ml for 1 h on ice and then stimulated with F(ab′) 2 anti-rat Ig at the indicated concentrations. The results represent the mean ± standard deviation of three experiments, each performed in duplicate. **, P

    Article Snippet: Viral particle-containing supernatant was added to SLP-76-deficient BMMC cultures prestimulated with stem cell factor (Biosource International) and 8 μg of Polybrene per ml (Sigma, St. Louis, Mo.) in fibronectin (Sigma)-coated plates.

    Techniques: Transduction, Expressing, Mouse Assay, Plasmid Preparation, Incubation, Staining, Polyacrylamide Gel Electrophoresis, Standard Deviation

    Calcium mobilization in reconstituted BMMC in response to FcɛRI ligation. Change of fluorescence of the calcium-sensitive dye indo 1-AM was monitored for the indicated time. IgE-sensitized cells were stimulated with F(ab′) 2 anti-rat Ig and ionomycin at the indicated time points (▴). BMMC reconstituted (reconst.) with a mutant construct are shown in comparison with SLP-76 −/− (KO) or WT BMMC analyzed in parallel. Results are expressed as percentage of ionomycin-induced calcium mobilization. Similar results were obtained in at least five experiments for each of the mutants.

    Journal: Molecular and Cellular Biology

    Article Title: Structural Requirements of SLP-76 in Signaling via the High-Affinity Immunoglobulin E Receptor (Fc?RI) in Mast Cells

    doi: 10.1128/MCB.23.7.2395-2406.2003

    Figure Lengend Snippet: Calcium mobilization in reconstituted BMMC in response to FcɛRI ligation. Change of fluorescence of the calcium-sensitive dye indo 1-AM was monitored for the indicated time. IgE-sensitized cells were stimulated with F(ab′) 2 anti-rat Ig and ionomycin at the indicated time points (▴). BMMC reconstituted (reconst.) with a mutant construct are shown in comparison with SLP-76 −/− (KO) or WT BMMC analyzed in parallel. Results are expressed as percentage of ionomycin-induced calcium mobilization. Similar results were obtained in at least five experiments for each of the mutants.

    Article Snippet: Viral particle-containing supernatant was added to SLP-76-deficient BMMC cultures prestimulated with stem cell factor (Biosource International) and 8 μg of Polybrene per ml (Sigma, St. Louis, Mo.) in fibronectin (Sigma)-coated plates.

    Techniques: Ligation, Fluorescence, Mutagenesis, Construct

    MVNP regulation of SIRPβ1 signaling in preosteoclast cells. (A) MVNP enhances SIRPβ1 interaction with DAP12 in normal human bone marrow mononuclear cells. Cells were transduced with EV or MVNP and stimulated with and without M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total cell lysates obtained from these cells were subjected to immunoprecipitation using anti -DAP12 or control IgG antibodies. Immunoprecipitants were subjected to western blot analysis for SIRPβ1. Total DAP12 expressions in these cells were served for loading control. (B) shRNA suppression of SIRPβ1 inhibits MVNP increased p-syk expression. Normal human bone marrow derived mononuclear cells were transduced with EV or MVNP in the presence and absence of SIRPβ1 shRNA and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 24 h. Total cell lysates were subjected to western blot analysis for p-syk and syk expression.

    Journal: Bone Reports

    Article Title: Measles virus nucleocapsid protein modulates the Signal Regulatory Protein-β1 (SIRPβ1) to enhance osteoclast differentiation in Paget's disease of bone

    doi: 10.1016/j.bonr.2016.06.002

    Figure Lengend Snippet: MVNP regulation of SIRPβ1 signaling in preosteoclast cells. (A) MVNP enhances SIRPβ1 interaction with DAP12 in normal human bone marrow mononuclear cells. Cells were transduced with EV or MVNP and stimulated with and without M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total cell lysates obtained from these cells were subjected to immunoprecipitation using anti -DAP12 or control IgG antibodies. Immunoprecipitants were subjected to western blot analysis for SIRPβ1. Total DAP12 expressions in these cells were served for loading control. (B) shRNA suppression of SIRPβ1 inhibits MVNP increased p-syk expression. Normal human bone marrow derived mononuclear cells were transduced with EV or MVNP in the presence and absence of SIRPβ1 shRNA and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 24 h. Total cell lysates were subjected to western blot analysis for p-syk and syk expression.

    Article Snippet: Normal primary human bone marrow mononuclear cells were purchased from ATCC (Manassas, VA) and peripheral blood monocytes (PBMC) were obtained from Stem Cell Technologies Inc., (Vancouver, BC).

    Techniques: Transduction, Immunoprecipitation, Western Blot, shRNA, Expressing, Derivative Assay

    MVNP induces SIRPβ1 in normal human bone marrow derived mononuclear cells. (A) Cells were transduced with EV or MVNP retroviral expression plasmid and stimulated with and without M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total RNA isolated was subjected to real-time RT-PCR analysis for SIRPβ1 expression. (B) SIPRβ1 mRNA expression in patients with PDB. Total RNA isolated from normal (n = 5) and Paget's patients (n = 4) bone marrow cells were subjected to real-time RT-PCR analysis for SIRPβ1 mRNA expression. The relative level of mRNA expression was normalized by GAPDH amplification. The values are expressed as mean ± SD for three independent experiment (*p

    Journal: Bone Reports

    Article Title: Measles virus nucleocapsid protein modulates the Signal Regulatory Protein-β1 (SIRPβ1) to enhance osteoclast differentiation in Paget's disease of bone

    doi: 10.1016/j.bonr.2016.06.002

    Figure Lengend Snippet: MVNP induces SIRPβ1 in normal human bone marrow derived mononuclear cells. (A) Cells were transduced with EV or MVNP retroviral expression plasmid and stimulated with and without M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total RNA isolated was subjected to real-time RT-PCR analysis for SIRPβ1 expression. (B) SIPRβ1 mRNA expression in patients with PDB. Total RNA isolated from normal (n = 5) and Paget's patients (n = 4) bone marrow cells were subjected to real-time RT-PCR analysis for SIRPβ1 mRNA expression. The relative level of mRNA expression was normalized by GAPDH amplification. The values are expressed as mean ± SD for three independent experiment (*p

    Article Snippet: Normal primary human bone marrow mononuclear cells were purchased from ATCC (Manassas, VA) and peripheral blood monocytes (PBMC) were obtained from Stem Cell Technologies Inc., (Vancouver, BC).

    Techniques: Derivative Assay, Transduction, Expressing, Plasmid Preparation, Isolation, Quantitative RT-PCR, Amplification

    SIRPβ1 participation in MVNP regulated gene expression during OCL differentiation. (A) shRNA suppression of SIRPβ1 inhibits MVNP enhanced c-Fos expression. Normal human bone marrow derived mononuclear cells were transduced with MVNP in the presence and absence of SIRPβ1 shRNA or control shRNA and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total cell lysates were subjected to western blot analysis for c-Fos expression. (B) SIRPβ1 shRNA suppression decreases DC-STAMP and CTGF mRNA expression. Human bone marrow derived mononuclear cells were transduced with EV or MVNP in the presence of control or SIRPβ1 shRNA and cultured for 48 h with RANKL and M-CSF. Total RNA isolated from these cells was subjected to real-time RT-PCR analysis for DC-STAMP and CTGF mRNA expression. The level of mRNA expression was normalized with GAPDH amplification. The values are expressed as mean ± SD for three independent experiments (p

    Journal: Bone Reports

    Article Title: Measles virus nucleocapsid protein modulates the Signal Regulatory Protein-β1 (SIRPβ1) to enhance osteoclast differentiation in Paget's disease of bone

    doi: 10.1016/j.bonr.2016.06.002

    Figure Lengend Snippet: SIRPβ1 participation in MVNP regulated gene expression during OCL differentiation. (A) shRNA suppression of SIRPβ1 inhibits MVNP enhanced c-Fos expression. Normal human bone marrow derived mononuclear cells were transduced with MVNP in the presence and absence of SIRPβ1 shRNA or control shRNA and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total cell lysates were subjected to western blot analysis for c-Fos expression. (B) SIRPβ1 shRNA suppression decreases DC-STAMP and CTGF mRNA expression. Human bone marrow derived mononuclear cells were transduced with EV or MVNP in the presence of control or SIRPβ1 shRNA and cultured for 48 h with RANKL and M-CSF. Total RNA isolated from these cells was subjected to real-time RT-PCR analysis for DC-STAMP and CTGF mRNA expression. The level of mRNA expression was normalized with GAPDH amplification. The values are expressed as mean ± SD for three independent experiments (p

    Article Snippet: Normal primary human bone marrow mononuclear cells were purchased from ATCC (Manassas, VA) and peripheral blood monocytes (PBMC) were obtained from Stem Cell Technologies Inc., (Vancouver, BC).

    Techniques: Expressing, shRNA, Derivative Assay, Transduction, Western Blot, Cell Culture, Isolation, Quantitative RT-PCR, Amplification

    Microarray profiling of gene expression in control empty vector (EV) and MVNP transduced normal human bone marrow derived mononuclear cells. Cells transduced with EV and MVNP retroviral vectors and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total RNA isolated from these cells were subjected to Agilent whole genome 4K × 44K array system for microarray analysis for ~ 26,000 genes revealed differential gene expression in MVNP transduced cells by (A) cluster analysis and (B) scatter plot. Gene expression profile presented as: red — high expression; yellow — medium expression; blue — low expression. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Journal: Bone Reports

    Article Title: Measles virus nucleocapsid protein modulates the Signal Regulatory Protein-β1 (SIRPβ1) to enhance osteoclast differentiation in Paget's disease of bone

    doi: 10.1016/j.bonr.2016.06.002

    Figure Lengend Snippet: Microarray profiling of gene expression in control empty vector (EV) and MVNP transduced normal human bone marrow derived mononuclear cells. Cells transduced with EV and MVNP retroviral vectors and stimulated with M-CSF (10 ng/ml) and RANKL (100 ng/ml) for 48 h. Total RNA isolated from these cells were subjected to Agilent whole genome 4K × 44K array system for microarray analysis for ~ 26,000 genes revealed differential gene expression in MVNP transduced cells by (A) cluster analysis and (B) scatter plot. Gene expression profile presented as: red — high expression; yellow — medium expression; blue — low expression. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Normal primary human bone marrow mononuclear cells were purchased from ATCC (Manassas, VA) and peripheral blood monocytes (PBMC) were obtained from Stem Cell Technologies Inc., (Vancouver, BC).

    Techniques: Microarray, Expressing, Plasmid Preparation, Derivative Assay, Transduction, Isolation

    HDAC3 expression is increased in MM-derived BMSC compared to healthy donor-derived BMSC but HDAC3 is not necessary for BMSC viability or proliferation. (a) Gene expression analysis from the IFM/DFCI 2009 dataset revealed that HDAC3 expression is higher in CD138- BMMCs when compared to CD138+ BMMCs derived from patients with MM. (b) Co-culture of HS-5 cells with MM1S.Luc triggers induction of HDAC3 expression in BMSC. GAPDH was used as loading control. Quantification was performed using ImageJ. (c) HDAC3 KO HS-5 cells have comparable viability to HDAC3 WT HS-5 cells as assessed by CCK-8 assay. (d) HDAC3 inhibition using BG45 is not cytotoxic towards HS-5 even at doses two-folds higher than the Ec50 of MM1S as measured by CCK-8 assay at 96 hours. (e) Endothelial tube formation assay shows compromised formation of endothelial tubes in BMEC60 cells transfected with HDAC3 siRNA compared to scrambled siRNA. Two representative, independent experiments shown.

    Journal: Leukemia

    Article Title: Targeting Histone Deacetylase 3 (HDAC3) in the Bone Marrow Microenvironment Inhibits Multiple Myeloma Proliferation by Modulating Exosomes and IL-6 Trans-Signaling

    doi: 10.1038/s41375-019-0493-x

    Figure Lengend Snippet: HDAC3 expression is increased in MM-derived BMSC compared to healthy donor-derived BMSC but HDAC3 is not necessary for BMSC viability or proliferation. (a) Gene expression analysis from the IFM/DFCI 2009 dataset revealed that HDAC3 expression is higher in CD138- BMMCs when compared to CD138+ BMMCs derived from patients with MM. (b) Co-culture of HS-5 cells with MM1S.Luc triggers induction of HDAC3 expression in BMSC. GAPDH was used as loading control. Quantification was performed using ImageJ. (c) HDAC3 KO HS-5 cells have comparable viability to HDAC3 WT HS-5 cells as assessed by CCK-8 assay. (d) HDAC3 inhibition using BG45 is not cytotoxic towards HS-5 even at doses two-folds higher than the Ec50 of MM1S as measured by CCK-8 assay at 96 hours. (e) Endothelial tube formation assay shows compromised formation of endothelial tubes in BMEC60 cells transfected with HDAC3 siRNA compared to scrambled siRNA. Two representative, independent experiments shown.

    Article Snippet: For siRNA transfection of CD138− BMMCs, the NEON® transfection system (Thermo Fisher Scientific) was used.

    Techniques: Expressing, Derivative Assay, Co-Culture Assay, CCK-8 Assay, Inhibition, Endothelial Tube Formation Assay, Transfection