mouse igg2b Search Results


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  • 95
    Thermo Fisher mouse igg1 apc
    FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16) are all involved in ADE of ZIKV infection by DENV immune sera. PBMCs from healthy donors (n = 3) were treated with monoclonal antibodies (1 μg/ml, 3 μg/ml or 10 μg/ml) against each FcγR types or combined (1 μg/ml, 3 μg/ml or 10 μg/ml in total), or with <t>IgG</t> control antibody prior to performing the boosted ZIKV ADE assay with DENV-1 immune serum (D1-E01, 1/2,500 dilution). The percentage of anti-E positive Vero cells in the control group, where no anti-FcγR antibodies were applied at the ADE condition was defined as 100%. The mean and standard deviation of results from three independent experiments without blocking antibody treatment (A) or with blocking antibody treatment (B) were presented. Statistical significances were determined by comparison of the relative proportion of infected cells with blocking antibody treatment to that of the control IgG antibody treatment under the same antibody concentration using unpaired two-tailed Student’s t test and designated as “*”for p
    Mouse Igg1 Apc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 165 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore igg
    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific <t>IgG</t> in the serum (1:1,000 dilution) and <t>IgA</t> in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p
    Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam mouse igg 2b
    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific <t>IgG</t> in the serum (1:1,000 dilution) and <t>IgA</t> in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p
    Mouse Igg 2b, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Miltenyi Biotec isotype control mouse igg 2b pe
    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific <t>IgG</t> in the serum (1:1,000 dilution) and <t>IgA</t> in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p
    Isotype Control Mouse Igg 2b Pe, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Abcam control mouse igg 2b
    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific <t>IgG</t> in the serum (1:1,000 dilution) and <t>IgA</t> in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p
    Control Mouse Igg 2b, supplied by Abcam, used in various techniques. Bioz Stars score: 89/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher mouse antihuman igg4
    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific <t>IgG</t> in the serum (1:1,000 dilution) and <t>IgA</t> in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p
    Mouse Antihuman Igg4, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher mouse igg
    Aurora B associates with <t>p53</t> at various phases of the cell cycle. ( A ) Lysates of U2OS cells were IP with either anti-Aurora B (AB2254; Abcam) or anti-p53 antibodies (AB-2) or preimmune <t>IgG</t> (negative control) followed by immunoblotting (IB) with antibodies as labeled to show co-IP of Aurora B and p53. ( B ) GST pull-down assay was performed with combinations of in vitro translated Aurora B, GST, and GST-tagged p53 as labeled. Aurora B that was bound to GST-p53 was detected by IB. Coomassie staining of GST and GST-p53 inputs are in C . In vitro translated Aurora B was detected by immunoblot ( Lower ). ( C ) As presented in B , results of in vitro GST pull-down assay of immunopurified Flag-Aurora B with GST or GST-tagged p53 deletion constructs are shown. The asterisks indicate the stained bands of GST, GST-p53, and GST-p53 deletion mutants. ( D ) Hct116 cells were synchronized to S phase by double thymidine block. Cell samples at labeled time points after release of thymidine block were stained with PI and analyzed by FACS for DNA content. DNA content histograms are shown for the time points as labeled. ( E ) Lysates of synchronized Hct116 cells from D were analyzed by immunoblot with indicated antibodies. Aurora B–p53 interaction at various phases of the cell cycle (as labeled above) was detected by IP with anti-Aurora B antibody followed by IB for p53 and Aurora B (IP:AurB and IB:AurB).
    Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 5070 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Pharmingen isotype control antibodies pe mouse igg 2b
    Aurora B associates with <t>p53</t> at various phases of the cell cycle. ( A ) Lysates of U2OS cells were IP with either anti-Aurora B (AB2254; Abcam) or anti-p53 antibodies (AB-2) or preimmune <t>IgG</t> (negative control) followed by immunoblotting (IB) with antibodies as labeled to show co-IP of Aurora B and p53. ( B ) GST pull-down assay was performed with combinations of in vitro translated Aurora B, GST, and GST-tagged p53 as labeled. Aurora B that was bound to GST-p53 was detected by IB. Coomassie staining of GST and GST-p53 inputs are in C . In vitro translated Aurora B was detected by immunoblot ( Lower ). ( C ) As presented in B , results of in vitro GST pull-down assay of immunopurified Flag-Aurora B with GST or GST-tagged p53 deletion constructs are shown. The asterisks indicate the stained bands of GST, GST-p53, and GST-p53 deletion mutants. ( D ) Hct116 cells were synchronized to S phase by double thymidine block. Cell samples at labeled time points after release of thymidine block were stained with PI and analyzed by FACS for DNA content. DNA content histograms are shown for the time points as labeled. ( E ) Lysates of synchronized Hct116 cells from D were analyzed by immunoblot with indicated antibodies. Aurora B–p53 interaction at various phases of the cell cycle (as labeled above) was detected by IP with anti-Aurora B antibody followed by IB for p53 and Aurora B (IP:AurB and IB:AurB).
    Isotype Control Antibodies Pe Mouse Igg 2b, supplied by Pharmingen, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad igg2b
    Endogenous anti-FrCas E immunoglobulin response in infected/treated mice. Experiments were performed using litters of 9 to 10 animals. (A) Total anti-FrCas E <t>IgG.</t> Blood samples were collected from the infected/treated and noninfected/treated mice presented
    Igg2b, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 245 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher igg2a pe
    Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) <t>rabbit-IgG</t> and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.
    Igg2a Pe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    R&D Systems mouse igg2 b
    Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) <t>rabbit-IgG</t> and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.
    Mouse Igg2 B, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    BioLegend anti mouse igg2b
    Enhanced immunoglobulin generation in CGD mice: IgG subtype and adjuvant dependence. Mice were immunized by subcutaneous injection into the outer ear of ovalbumin with either alum (A–C) or curdlan (D–F) as adjuvant. Levels of Anti-ovalbumin IgG1 (A,D) , <t>IgG2b</t> (B,E) and IgG2c (C,F) were measured 10 and 14 days following immunization ( n = 12). * p
    Anti Mouse Igg2b, supplied by BioLegend, used in various techniques. Bioz Stars score: 95/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher apc mouse igg1
    Enhanced immunoglobulin generation in CGD mice: IgG subtype and adjuvant dependence. Mice were immunized by subcutaneous injection into the outer ear of ovalbumin with either alum (A–C) or curdlan (D–F) as adjuvant. Levels of Anti-ovalbumin IgG1 (A,D) , <t>IgG2b</t> (B,E) and IgG2c (C,F) were measured 10 and 14 days following immunization ( n = 12). * p
    Apc Mouse Igg1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher control mouse igg
    Betacelluin, EGF, and HRGβ induce <t>β1-integrin-dependent</t> MDA-MB-435 cell migration on LAM. (A) Cells were grown to ∼75% confluency and placed in serum-free media for 16 h before harvesting as for adhesion assays. Polycarbonate filters (8 μm) were coated overnight at 4°C in PBS containing mouse EHS-LAM or EHS-COLL (our unpublished data) at 20 μg/ml. Forty-eight-well chemotaxis chambers were assembled with assay media alone or containing increasing amounts of growth factors in the lower chambers, as indicated. LAM-coated filters were placed over the lower wells and, ∼23,000 MDA-MB-435 cells were placed in the upper wells and allowed to migrate at 37°C for 4–6 h. Migrated cells in each well were quantitated on fixed and stained filters. The sum of four microscopic fields was taken for each well, and three wells were averaged for each stimulation condition. (B) Antibody blocking studies were carried out by preincubating cells with control <t>IgG</t> (open bars) or the inhibitory β1-integrin-specific mAb P5D2 (solid bars) at 1 μg/1 × 10 6 cells on ice for 10 min before adding the cells to the upper wells of chambers containing EGF or HRGβ and containing filters coated with LAM or COLL. Some variability was observed with the levels of basal migration in the data shown in A, because each growth factor titration was carried out in a separate chemotaxis chamber. However, the level of stimulation over that of basal migration for each growth factor was reproducible over at least three separate assays.
    Control Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 231 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher mouse igg1 antibody
    mRNP assay of Ras12V cell lysate to measure endogenous RBP binding to ODC RNA To determine endogenous binding of HuR to the ODC transcript, HuR was immunoprecipitated from Ras12V cells as described in the Methods. Cell lysates isolated in RLB were incubated with a 50% (v/v) suspension of Protein A-sepharose beads precoated with either <t>IgG1</t> or anti-HuR (Santa Cruz Biotech). After washing in NP40-based buffer, beads were treated with RNase-free DNase I and proteinase K, then RNA was extracted and reverse transcribed to obtain cDNA. The presence of ODC was analyzed by conventional PCR using primer pairs corresponding to a 635 bp region within the ODC transcript (see Note 8 ). Lanes labeled “Input RNA” represent duplicate PCR reactions performed with the same ODC primers on cDNA prepared from cell lysate without immunoprecipitation, indicating the presence of ODC RNA in the lysate.
    Mouse Igg1 Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher igg3
    (A) C. albicans -specific IgM, IgG, and IgA titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled sera of at least four mice/group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate. (B) C. albicans -specific IgG1, <t>IgG3,</t> IgG2a, and IgG2b titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled serum samples of at least four mice per group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate.
    Igg3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1171 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Agilent technologies mn normal mouse igg2 b
    (A) C. albicans -specific IgM, IgG, and IgA titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled sera of at least four mice/group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate. (B) C. albicans -specific IgG1, <t>IgG3,</t> IgG2a, and IgG2b titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled serum samples of at least four mice per group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate.
    Mn Normal Mouse Igg2 B, supplied by Agilent technologies, 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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    94
    Thermo Fisher mouse igg1 mab
    Generation of an antibody specific for CD300A or CD300C. A–C , relative expression levels of CD300C among human tissues ( A ), among human hematopoietic cell lines ( B ), or among human PB-derived B cells, T cells, monocytes, and granulocytes ( C ) were estimated by real time PCR. The amount of expression was indicated relative to that in PB ( A ), MOLM13 cell lines ( B ), or monocytes ( C ). The data are representative of three independent experiments. D , the sensitivity and specificity of anti-CD300A mAb or anti-CD300C mAb were examined by flow cytometry. Ba/F3 cells were transduced with FLAG-tagged CD300A, CD300B, CD300C, CD300D, CD300E, CD300F, or mock. The cells were stained with biotin-conjugated anti-CD300A mAb or rat IgG2a mAb ( first row ) or biotin-conjugated anti-CD300C mAb or mouse <t>IgG1</t> mAb ( second row ), followed by R-PE-conjugated streptavidin. Alternatively, the cells were stained with FITC-conjugated anti-FLAG mAb or mouse IgG1 mAb ( third row ). The results of control staining are shown as filled histograms .
    Mouse Igg1 Mab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher mouse monoclonal igg1
    ICP0 interacts with p65 and p50. The HEK 293T cells were cotransfected with ICP0-Myc and Flag-p65 expression plasmids (A) and ICP0-Myc and Flag-p50 expression plasmids (D). At 36 h after transfection, cells were harvested and lysed; the samples were then subjected to IP assays using anti-Myc MAb (IP:Myc) or nonspecific mouse monoclonal antibody <t>(IgG).</t> IP samples were separated by 10% SDS-PAGE, and proteins were transferred onto a PVDF membrane. WB were probed with the indicated Ab. (B, C, E, F) HEK 293T cells were transfected with Flag-ICP0 expression plasmid. At 24 h posttransfection, cells were mock treated (B and E) or treated (C and F) with TNF-α (10 ng/ml) and incubated for an additional 8 h, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody <t>(IgG2b).</t> HEK 293T cells were infected with WT HSV-1 at an MOI of 10 for 16 h. The cells were then lysed, and the extracts were subjected to IP using anti-ICP0 pAb (IP:ICP0) or control IgG. Precipitates were analyzed by Western blotting (G and H).
    Mouse Monoclonal Igg1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16) are all involved in ADE of ZIKV infection by DENV immune sera. PBMCs from healthy donors (n = 3) were treated with monoclonal antibodies (1 μg/ml, 3 μg/ml or 10 μg/ml) against each FcγR types or combined (1 μg/ml, 3 μg/ml or 10 μg/ml in total), or with IgG control antibody prior to performing the boosted ZIKV ADE assay with DENV-1 immune serum (D1-E01, 1/2,500 dilution). The percentage of anti-E positive Vero cells in the control group, where no anti-FcγR antibodies were applied at the ADE condition was defined as 100%. The mean and standard deviation of results from three independent experiments without blocking antibody treatment (A) or with blocking antibody treatment (B) were presented. Statistical significances were determined by comparison of the relative proportion of infected cells with blocking antibody treatment to that of the control IgG antibody treatment under the same antibody concentration using unpaired two-tailed Student’s t test and designated as “*”for p

    Journal: PLoS ONE

    Article Title: Dengue immune sera enhance Zika virus infection in human peripheral blood monocytes through Fc gamma receptors

    doi: 10.1371/journal.pone.0200478

    Figure Lengend Snippet: FcγRI (CD64), FcγRII (CD32) and FcγRIII (CD16) are all involved in ADE of ZIKV infection by DENV immune sera. PBMCs from healthy donors (n = 3) were treated with monoclonal antibodies (1 μg/ml, 3 μg/ml or 10 μg/ml) against each FcγR types or combined (1 μg/ml, 3 μg/ml or 10 μg/ml in total), or with IgG control antibody prior to performing the boosted ZIKV ADE assay with DENV-1 immune serum (D1-E01, 1/2,500 dilution). The percentage of anti-E positive Vero cells in the control group, where no anti-FcγR antibodies were applied at the ADE condition was defined as 100%. The mean and standard deviation of results from three independent experiments without blocking antibody treatment (A) or with blocking antibody treatment (B) were presented. Statistical significances were determined by comparison of the relative proportion of infected cells with blocking antibody treatment to that of the control IgG antibody treatment under the same antibody concentration using unpaired two-tailed Student’s t test and designated as “*”for p

    Article Snippet: Isotype control murine immunoglobulin IgG1 κ (FITC; APC; clone P3.6.2.8.1), mouse IgG2a κ (PE; PE-Cy7; Alexa Fluor 488; clone eBM2a), mouse IgG2b κ (PE; clone eBMG2b) were purchased from eBioscience.

    Techniques: Infection, Standard Deviation, Blocking Assay, Concentration Assay, Two Tailed Test

    Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific IgG in the serum (1:1,000 dilution) and IgA in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p

    Journal: Frontiers in Immunology

    Article Title: Mucosal Delivery of Fusion Proteins with Bacillus subtilis Spores Enhances Protection against Tuberculosis by Bacillus Calmette-Guérin

    doi: 10.3389/fimmu.2018.00346

    Figure Lengend Snippet: Enhanced humoral immunity caused by Spore-FP1. Immunized mice were tested for the presence of antigen-specific IgG in the serum (1:1,000 dilution) and IgA in the BAL (1 mL PBS flush; 1:10 dilution) by ELISA, with optical density read at 450 nm in duplicate. (A) Levels of IgG and IgA specific to Ag85B. (B) Levels of IgG and IgA specific to ACR. Results are expressed as mean ± SEM. Data shown are derived from n = 3 individual mice and are representative of two independent experiments. Significance was tested against the unstimulated control by one-way ANOVA with Tukey’s posttest, * p

    Article Snippet: Levels of IgA or IgG were detected using peroxidase-conjugated anti-mouse IgA or anti-mouse IgG (Sigma) and OPD substrate (Sigma).

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay

    Aurora B associates with p53 at various phases of the cell cycle. ( A ) Lysates of U2OS cells were IP with either anti-Aurora B (AB2254; Abcam) or anti-p53 antibodies (AB-2) or preimmune IgG (negative control) followed by immunoblotting (IB) with antibodies as labeled to show co-IP of Aurora B and p53. ( B ) GST pull-down assay was performed with combinations of in vitro translated Aurora B, GST, and GST-tagged p53 as labeled. Aurora B that was bound to GST-p53 was detected by IB. Coomassie staining of GST and GST-p53 inputs are in C . In vitro translated Aurora B was detected by immunoblot ( Lower ). ( C ) As presented in B , results of in vitro GST pull-down assay of immunopurified Flag-Aurora B with GST or GST-tagged p53 deletion constructs are shown. The asterisks indicate the stained bands of GST, GST-p53, and GST-p53 deletion mutants. ( D ) Hct116 cells were synchronized to S phase by double thymidine block. Cell samples at labeled time points after release of thymidine block were stained with PI and analyzed by FACS for DNA content. DNA content histograms are shown for the time points as labeled. ( E ) Lysates of synchronized Hct116 cells from D were analyzed by immunoblot with indicated antibodies. Aurora B–p53 interaction at various phases of the cell cycle (as labeled above) was detected by IP with anti-Aurora B antibody followed by IB for p53 and Aurora B (IP:AurB and IB:AurB).

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Aurora B kinase phosphorylates and instigates degradation of p53

    doi: 10.1073/pnas.1110287109

    Figure Lengend Snippet: Aurora B associates with p53 at various phases of the cell cycle. ( A ) Lysates of U2OS cells were IP with either anti-Aurora B (AB2254; Abcam) or anti-p53 antibodies (AB-2) or preimmune IgG (negative control) followed by immunoblotting (IB) with antibodies as labeled to show co-IP of Aurora B and p53. ( B ) GST pull-down assay was performed with combinations of in vitro translated Aurora B, GST, and GST-tagged p53 as labeled. Aurora B that was bound to GST-p53 was detected by IB. Coomassie staining of GST and GST-p53 inputs are in C . In vitro translated Aurora B was detected by immunoblot ( Lower ). ( C ) As presented in B , results of in vitro GST pull-down assay of immunopurified Flag-Aurora B with GST or GST-tagged p53 deletion constructs are shown. The asterisks indicate the stained bands of GST, GST-p53, and GST-p53 deletion mutants. ( D ) Hct116 cells were synchronized to S phase by double thymidine block. Cell samples at labeled time points after release of thymidine block were stained with PI and analyzed by FACS for DNA content. DNA content histograms are shown for the time points as labeled. ( E ) Lysates of synchronized Hct116 cells from D were analyzed by immunoblot with indicated antibodies. Aurora B–p53 interaction at various phases of the cell cycle (as labeled above) was detected by IP with anti-Aurora B antibody followed by IB for p53 and Aurora B (IP:AurB and IB:AurB).

    Article Snippet: The following antibodies were used in this study: 14-3-3σ (1433S01; RDI), Actin (A2066; Sigma), Annexin V-FITC (556419; BD Biosciences), Aurora B (Ab2254; Abcam), Bad ( ; BD Biosciences), Bax ( ; BD Transduction), Cyclin A (SC751; Santa Cruz), Cyclin B1 (SC245; Santa Cruz), Cyclin D (MS-2110; Neomarkers), Cyclin E (SC-247; Santa Cruz), Flag (A804-200; Sigma), GFP (SC-9996; Santa Cruz), HA (12CA5; Roche), His (SC-803; Santa Cruz), HH3 (p-S10, 05–817; Upstate), MDM2 (S3813; Santa Cruz), Mouse IgG (488; Alexa; ; Molecular Probes), Mouse IgG (568; Alexa; ; Molecular Probes), p53 for IP (AB-1, PAB1801; Oncogene Science), p53 for IF (SC-6243; Santa Cruz), p53 (610183; BD Biosciences), p53 (p-S315, 2528S0; Cell Signaling), P21 (610233; Transduction Labs), PUMA (SC-28226; Santa Cruz), Rabbit IgG (488; Alexa; A1103; Molecular Probes), rabbit IgG (568; Alexa; A11011; Molecular Probes), and Survivin (2808; Cell Signaling).

    Techniques: Negative Control, Labeling, Co-Immunoprecipitation Assay, Pull Down Assay, In Vitro, Staining, Construct, Blocking Assay, FACS

    Endogenous anti-FrCas E immunoglobulin response in infected/treated mice. Experiments were performed using litters of 9 to 10 animals. (A) Total anti-FrCas E IgG. Blood samples were collected from the infected/treated and noninfected/treated mice presented

    Journal: Journal of Virology

    Article Title: Induction of Long-Term Protective Antiviral Endogenous Immune Response by Short Neutralizing Monoclonal Antibody Treatment

    doi: 10.1128/JVI.79.10.6272-6280.2005

    Figure Lengend Snippet: Endogenous anti-FrCas E immunoglobulin response in infected/treated mice. Experiments were performed using litters of 9 to 10 animals. (A) Total anti-FrCas E IgG. Blood samples were collected from the infected/treated and noninfected/treated mice presented

    Article Snippet: Secondary peroxidase-conjugated anti-mouse IgG2a, IgG2b, IgG1, and IgM rabbit antisera (Serotec) were used as secondary antibodies.

    Techniques: Infection, Mouse Assay

    Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) rabbit-IgG and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.

    Journal: Veterinary Research

    Article Title: Immunobiotic lactic acid bacteria beneficially regulate immune response triggered by poly(I:C) in porcine intestinal epithelial cells

    doi: 10.1186/1297-9716-42-111

    Figure Lengend Snippet: Analysis of toll-like receptor 3 (TLR3) expression in porcine intestinal epithelial (PIE) cells . (A) Flow cytometric analysis of TLR3 in PIE cells. Histograms show flow cytometric analysis for TLR3 staining as follows: intracellular (open histogram), cell surface (broken lines) and isotype-matched controls (shaded histograms). The analysis of intracellular and cell surface expression of TLR3 is presented as the log of mean fluorescence intensity (MFI). The results represent three independent experiments. (B) Confocal microscopic analysis of the subcellular localization of TLR3 in PIE cells. Fixed and permeabilized cells were stained with anti-mouse TLR3(unlabeled) rabbit-IgG and goat anti-rabbit IgG (H+L) Alexa Fluor488 and Early Endosomes-RFP BacMam. The merged color (yellow) is indicative of co-localization. Bar, 2 um. PIE cells stained with rabbit IgG-Alexa Fluor488 Isotype were used as controls.

    Article Snippet: Cells stained with irrelevant mouse IgG2b-FITC (11-4732, eBioscience), IgG1-PerCP/Cy5.5 (45-4714, eBioscience), IgG2b-PE (12-4732, eBioscience), IgG2a-PE (12-4724, eBioscience), IgG1-PE (12-4714, eBioscience) and rabbit IgG-Alexa Fluor488 isotype control (4340S, Cell Signaling Technology Japan KK, Tokyo, Japan) antibodies were included as isotype controls.

    Techniques: Expressing, Flow Cytometry, Staining, Fluorescence

    Enhanced immunoglobulin generation in CGD mice: IgG subtype and adjuvant dependence. Mice were immunized by subcutaneous injection into the outer ear of ovalbumin with either alum (A–C) or curdlan (D–F) as adjuvant. Levels of Anti-ovalbumin IgG1 (A,D) , IgG2b (B,E) and IgG2c (C,F) were measured 10 and 14 days following immunization ( n = 12). * p

    Journal: Frontiers in Immunology

    Article Title: Altered Humoral Immune Responses and IgG Subtypes in NOX2-Deficient Mice and Patients: A Key Role for NOX2 in Antigen-Presenting Cells

    doi: 10.3389/fimmu.2018.01555

    Figure Lengend Snippet: Enhanced immunoglobulin generation in CGD mice: IgG subtype and adjuvant dependence. Mice were immunized by subcutaneous injection into the outer ear of ovalbumin with either alum (A–C) or curdlan (D–F) as adjuvant. Levels of Anti-ovalbumin IgG1 (A,D) , IgG2b (B,E) and IgG2c (C,F) were measured 10 and 14 days following immunization ( n = 12). * p

    Article Snippet: To measure ovalbumin-specific antibody, anti-mouse IgG2c, anti-mouse IgG2b, and anti-mouse IgG3 (Biolegend, USA) or anti-mouse IgG1 (ThermoFisher Scientific, USA) coupled to peroxidase was added to wells at the dilution of 1:1,000 for anti-mouse IgG2c and IgG1 and 1:500 for anti-mouse IgG2b and IgG3.

    Techniques: Mouse Assay, Injection

    Relative levels of IgG1 and IgG2 in CGD patients and healthy donors and basal levels of immunoglobulin subtypes in wild-type (WT) and NOX2-deficient mice. (A,B) Proportion of serum IgG1 and IgG2 subtypes relative to total IgG. Basal level of IgG1 (C) , IgG2c (D) , IgG2b (E) and IgG3 (F) in WT and NOX2 deficient mice (NOX2KO). * p

    Journal: Frontiers in Immunology

    Article Title: Altered Humoral Immune Responses and IgG Subtypes in NOX2-Deficient Mice and Patients: A Key Role for NOX2 in Antigen-Presenting Cells

    doi: 10.3389/fimmu.2018.01555

    Figure Lengend Snippet: Relative levels of IgG1 and IgG2 in CGD patients and healthy donors and basal levels of immunoglobulin subtypes in wild-type (WT) and NOX2-deficient mice. (A,B) Proportion of serum IgG1 and IgG2 subtypes relative to total IgG. Basal level of IgG1 (C) , IgG2c (D) , IgG2b (E) and IgG3 (F) in WT and NOX2 deficient mice (NOX2KO). * p

    Article Snippet: To measure ovalbumin-specific antibody, anti-mouse IgG2c, anti-mouse IgG2b, and anti-mouse IgG3 (Biolegend, USA) or anti-mouse IgG1 (ThermoFisher Scientific, USA) coupled to peroxidase was added to wells at the dilution of 1:1,000 for anti-mouse IgG2c and IgG1 and 1:500 for anti-mouse IgG2b and IgG3.

    Techniques: Mouse Assay

    Betacelluin, EGF, and HRGβ induce β1-integrin-dependent MDA-MB-435 cell migration on LAM. (A) Cells were grown to ∼75% confluency and placed in serum-free media for 16 h before harvesting as for adhesion assays. Polycarbonate filters (8 μm) were coated overnight at 4°C in PBS containing mouse EHS-LAM or EHS-COLL (our unpublished data) at 20 μg/ml. Forty-eight-well chemotaxis chambers were assembled with assay media alone or containing increasing amounts of growth factors in the lower chambers, as indicated. LAM-coated filters were placed over the lower wells and, ∼23,000 MDA-MB-435 cells were placed in the upper wells and allowed to migrate at 37°C for 4–6 h. Migrated cells in each well were quantitated on fixed and stained filters. The sum of four microscopic fields was taken for each well, and three wells were averaged for each stimulation condition. (B) Antibody blocking studies were carried out by preincubating cells with control IgG (open bars) or the inhibitory β1-integrin-specific mAb P5D2 (solid bars) at 1 μg/1 × 10 6 cells on ice for 10 min before adding the cells to the upper wells of chambers containing EGF or HRGβ and containing filters coated with LAM or COLL. Some variability was observed with the levels of basal migration in the data shown in A, because each growth factor titration was carried out in a separate chemotaxis chamber. However, the level of stimulation over that of basal migration for each growth factor was reproducible over at least three separate assays.

    Journal: Molecular Biology of the Cell

    Article Title: Stimulation of ?1-Integrin Function by Epidermal Growth Factor and Heregulin-? Has Distinct Requirements for erbB2 but a Similar Dependence on Phosphoinositide 3-OH Kinase

    doi:

    Figure Lengend Snippet: Betacelluin, EGF, and HRGβ induce β1-integrin-dependent MDA-MB-435 cell migration on LAM. (A) Cells were grown to ∼75% confluency and placed in serum-free media for 16 h before harvesting as for adhesion assays. Polycarbonate filters (8 μm) were coated overnight at 4°C in PBS containing mouse EHS-LAM or EHS-COLL (our unpublished data) at 20 μg/ml. Forty-eight-well chemotaxis chambers were assembled with assay media alone or containing increasing amounts of growth factors in the lower chambers, as indicated. LAM-coated filters were placed over the lower wells and, ∼23,000 MDA-MB-435 cells were placed in the upper wells and allowed to migrate at 37°C for 4–6 h. Migrated cells in each well were quantitated on fixed and stained filters. The sum of four microscopic fields was taken for each well, and three wells were averaged for each stimulation condition. (B) Antibody blocking studies were carried out by preincubating cells with control IgG (open bars) or the inhibitory β1-integrin-specific mAb P5D2 (solid bars) at 1 μg/1 × 10 6 cells on ice for 10 min before adding the cells to the upper wells of chambers containing EGF or HRGβ and containing filters coated with LAM or COLL. Some variability was observed with the levels of basal migration in the data shown in A, because each growth factor titration was carried out in a separate chemotaxis chamber. However, the level of stimulation over that of basal migration for each growth factor was reproducible over at least three separate assays.

    Article Snippet: For receptor blocking studies, cells were incubated in the presence of control mouse IgG (Caltag, South San Francisco, CA), the anti-β1-integrin antibody P5D2 (a kind gift from T. LeBien, University of Minnesota, Minneapolis, MN), the anti-erbB2 Ab-16, the anti-erbB3 Ab-5, or the anti-erbB4 Ab-3 (all from Lab Vision) at 1 μg antibody/1 × 106 cells or as indicated in figure legends.

    Techniques: Multiple Displacement Amplification, Migration, Laser Capture Microdissection, Chemotaxis Assay, Staining, Blocking Assay, Titration

    mRNP assay of Ras12V cell lysate to measure endogenous RBP binding to ODC RNA To determine endogenous binding of HuR to the ODC transcript, HuR was immunoprecipitated from Ras12V cells as described in the Methods. Cell lysates isolated in RLB were incubated with a 50% (v/v) suspension of Protein A-sepharose beads precoated with either IgG1 or anti-HuR (Santa Cruz Biotech). After washing in NP40-based buffer, beads were treated with RNase-free DNase I and proteinase K, then RNA was extracted and reverse transcribed to obtain cDNA. The presence of ODC was analyzed by conventional PCR using primer pairs corresponding to a 635 bp region within the ODC transcript (see Note 8 ). Lanes labeled “Input RNA” represent duplicate PCR reactions performed with the same ODC primers on cDNA prepared from cell lysate without immunoprecipitation, indicating the presence of ODC RNA in the lysate.

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Post-transcriptional regulation of ornithine decarboxylase

    doi: 10.1007/978-1-61779-034-8_17

    Figure Lengend Snippet: mRNP assay of Ras12V cell lysate to measure endogenous RBP binding to ODC RNA To determine endogenous binding of HuR to the ODC transcript, HuR was immunoprecipitated from Ras12V cells as described in the Methods. Cell lysates isolated in RLB were incubated with a 50% (v/v) suspension of Protein A-sepharose beads precoated with either IgG1 or anti-HuR (Santa Cruz Biotech). After washing in NP40-based buffer, beads were treated with RNase-free DNase I and proteinase K, then RNA was extracted and reverse transcribed to obtain cDNA. The presence of ODC was analyzed by conventional PCR using primer pairs corresponding to a 635 bp region within the ODC transcript (see Note 8 ). Lanes labeled “Input RNA” represent duplicate PCR reactions performed with the same ODC primers on cDNA prepared from cell lysate without immunoprecipitation, indicating the presence of ODC RNA in the lysate.

    Article Snippet: Mouse IgG1 antibody (Invitrogen, Carlsbad, CA).

    Techniques: Binding Assay, Immunoprecipitation, Isolation, Incubation, Polymerase Chain Reaction, Labeling

    (A) C. albicans -specific IgM, IgG, and IgA titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled sera of at least four mice/group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate. (B) C. albicans -specific IgG1, IgG3, IgG2a, and IgG2b titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled serum samples of at least four mice per group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate.

    Journal: Infection and Immunity

    Article Title: Characteristics of Invasive Candidiasis in Gamma Interferon- and Interleukin-4-Deficient Mice: Role of Macrophages in Host Defense against Candida albicans

    doi:

    Figure Lengend Snippet: (A) C. albicans -specific IgM, IgG, and IgA titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled sera of at least four mice/group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate. (B) C. albicans -specific IgG1, IgG3, IgG2a, and IgG2b titers in sera of mice infected i.p. with 10 8 Candida blastoconidia. Pooled serum samples of at least four mice per group were analyzed for specific antibodies by standard ELISA. The height of each bar represents the mean ± standard error of three experiments performed in duplicate.

    Article Snippet: After extensive washing, bound antibodies were revealed by the addition of alkaline phosphatase-conjugated rabbit anti-mouse IgG1, IgG2a, IgG2b, IgG3 (Zymed Laboratories, San Francisco, Calif.), goat anti-mouse IgG, IgM, IgA (Sigma), or peroxidase-conjugated rat anti-mouse IgE (Serotec) for 1 h at 37°C.

    Techniques: Mouse Assay, Infection, Enzyme-linked Immunosorbent Assay

    Generation of an antibody specific for CD300A or CD300C. A–C , relative expression levels of CD300C among human tissues ( A ), among human hematopoietic cell lines ( B ), or among human PB-derived B cells, T cells, monocytes, and granulocytes ( C ) were estimated by real time PCR. The amount of expression was indicated relative to that in PB ( A ), MOLM13 cell lines ( B ), or monocytes ( C ). The data are representative of three independent experiments. D , the sensitivity and specificity of anti-CD300A mAb or anti-CD300C mAb were examined by flow cytometry. Ba/F3 cells were transduced with FLAG-tagged CD300A, CD300B, CD300C, CD300D, CD300E, CD300F, or mock. The cells were stained with biotin-conjugated anti-CD300A mAb or rat IgG2a mAb ( first row ) or biotin-conjugated anti-CD300C mAb or mouse IgG1 mAb ( second row ), followed by R-PE-conjugated streptavidin. Alternatively, the cells were stained with FITC-conjugated anti-FLAG mAb or mouse IgG1 mAb ( third row ). The results of control staining are shown as filled histograms .

    Journal: The Journal of Biological Chemistry

    Article Title: Human CD300C Delivers an Fc Receptor-?-dependent Activating Signal in Mast Cells and Monocytes and Differs from CD300A in Ligand Recognition *

    doi: 10.1074/jbc.M112.434746

    Figure Lengend Snippet: Generation of an antibody specific for CD300A or CD300C. A–C , relative expression levels of CD300C among human tissues ( A ), among human hematopoietic cell lines ( B ), or among human PB-derived B cells, T cells, monocytes, and granulocytes ( C ) were estimated by real time PCR. The amount of expression was indicated relative to that in PB ( A ), MOLM13 cell lines ( B ), or monocytes ( C ). The data are representative of three independent experiments. D , the sensitivity and specificity of anti-CD300A mAb or anti-CD300C mAb were examined by flow cytometry. Ba/F3 cells were transduced with FLAG-tagged CD300A, CD300B, CD300C, CD300D, CD300E, CD300F, or mock. The cells were stained with biotin-conjugated anti-CD300A mAb or rat IgG2a mAb ( first row ) or biotin-conjugated anti-CD300C mAb or mouse IgG1 mAb ( second row ), followed by R-PE-conjugated streptavidin. Alternatively, the cells were stained with FITC-conjugated anti-FLAG mAb or mouse IgG1 mAb ( third row ). The results of control staining are shown as filled histograms .

    Article Snippet: Anti-CD300A mAb, mouse IgG1 mAb, anti-CD300C mAb, and rat IgG2a mAb were biotinylated by sulfo-NHS-LC-biotin (Pierce) according to the manufacturer's instructions.

    Techniques: Expressing, Derivative Assay, Real-time Polymerase Chain Reaction, Flow Cytometry, Cytometry, Transduction, Staining

    Specific engagement of CD300C activated human monocytes. A and B , human PB-derived monocytes were stimulated for 24 h with plate-coated anti-CD300C mAb, anti-TREM-1 mAb, or mouse IgG1 mAb. TNFα released into the culture supernatants was measured by ELISA ( A ). The cells were stained with R-PE-conjugated anti-CD83 or CD86 mAb. The results of control staining are shown as filled histograms ( B ). C , human PB-derived monocytes were stimulated for 24 h with plate-coated anti-CD300C mAb, anti-TREM-1 mAb, or mouse IgG1 mAb in the presence or absence of 10 ng/ml LPS. TNFα released into the culture supernatants was measured by ELISA. A and C , all of the data points correspond to the means ± S.D. of three independent experiments. Statistically significant differences are shown. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Human CD300C Delivers an Fc Receptor-?-dependent Activating Signal in Mast Cells and Monocytes and Differs from CD300A in Ligand Recognition *

    doi: 10.1074/jbc.M112.434746

    Figure Lengend Snippet: Specific engagement of CD300C activated human monocytes. A and B , human PB-derived monocytes were stimulated for 24 h with plate-coated anti-CD300C mAb, anti-TREM-1 mAb, or mouse IgG1 mAb. TNFα released into the culture supernatants was measured by ELISA ( A ). The cells were stained with R-PE-conjugated anti-CD83 or CD86 mAb. The results of control staining are shown as filled histograms ( B ). C , human PB-derived monocytes were stimulated for 24 h with plate-coated anti-CD300C mAb, anti-TREM-1 mAb, or mouse IgG1 mAb in the presence or absence of 10 ng/ml LPS. TNFα released into the culture supernatants was measured by ELISA. A and C , all of the data points correspond to the means ± S.D. of three independent experiments. Statistically significant differences are shown. *, p

    Article Snippet: Anti-CD300A mAb, mouse IgG1 mAb, anti-CD300C mAb, and rat IgG2a mAb were biotinylated by sulfo-NHS-LC-biotin (Pierce) according to the manufacturer's instructions.

    Techniques: Derivative Assay, Enzyme-linked Immunosorbent Assay, Staining

    Plate-coated PE induced GFP expression more strongly in 2B4-CD300A-GFP cells than in 2B4-CD300C-GFP cells. A , the schematic structure of the chimera receptor CD300A-CD3ζ expressed in 2B4-CD300A-GFP cells or the chimera receptor CD300C-CD3ζ expressed in 2B4-CD300C-GFP cells. B and C , flow cytometry of GFP expression of the reporter cells. 2B4-CD300A-GFP cells or 2B4-CD300C-GFP cells were incubated for 24 h on plates coated with C-24 ceramide, egg ceramide, phosphatidylcholine ( PC ), PE, PS, sphingomyelin ( SM ), sphyngosylphosphorylcholine ( SPC ), cholesterol, LDL, HDL, or anti-FLAG mAb ( B ). 2B4-CD300A-GFP cells or 2B4-CD300C-GFP cells were incubated for 24 h on plates coated with PE. After incubating the reporter cells, 20 μg/ml of either anti-CD300A mAb or rat IgG2a mAb or 20 μg/ml of either anti-CD300C mAb or mouse IgG1 mAb was added to the culture of 2B4-CD300A-GFP cells ( upper panel ) or 2B4-CD300C-GFP cells ( lower panel ), respectively ( C ). D , CD300A-Fc, CD300C-Fc, or Fc bound to wells was quantified by ELISA. Indicated concentrations of CD300A-Fc, CD300C-Fc, or Fc were incubated on plates coated with PE ( upper panel ) or PS ( lower panel ). All of the data points correspond to the means ± S.D. of three independent experiments. Statistically significant differences are shown. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Human CD300C Delivers an Fc Receptor-?-dependent Activating Signal in Mast Cells and Monocytes and Differs from CD300A in Ligand Recognition *

    doi: 10.1074/jbc.M112.434746

    Figure Lengend Snippet: Plate-coated PE induced GFP expression more strongly in 2B4-CD300A-GFP cells than in 2B4-CD300C-GFP cells. A , the schematic structure of the chimera receptor CD300A-CD3ζ expressed in 2B4-CD300A-GFP cells or the chimera receptor CD300C-CD3ζ expressed in 2B4-CD300C-GFP cells. B and C , flow cytometry of GFP expression of the reporter cells. 2B4-CD300A-GFP cells or 2B4-CD300C-GFP cells were incubated for 24 h on plates coated with C-24 ceramide, egg ceramide, phosphatidylcholine ( PC ), PE, PS, sphingomyelin ( SM ), sphyngosylphosphorylcholine ( SPC ), cholesterol, LDL, HDL, or anti-FLAG mAb ( B ). 2B4-CD300A-GFP cells or 2B4-CD300C-GFP cells were incubated for 24 h on plates coated with PE. After incubating the reporter cells, 20 μg/ml of either anti-CD300A mAb or rat IgG2a mAb or 20 μg/ml of either anti-CD300C mAb or mouse IgG1 mAb was added to the culture of 2B4-CD300A-GFP cells ( upper panel ) or 2B4-CD300C-GFP cells ( lower panel ), respectively ( C ). D , CD300A-Fc, CD300C-Fc, or Fc bound to wells was quantified by ELISA. Indicated concentrations of CD300A-Fc, CD300C-Fc, or Fc were incubated on plates coated with PE ( upper panel ) or PS ( lower panel ). All of the data points correspond to the means ± S.D. of three independent experiments. Statistically significant differences are shown. *, p

    Article Snippet: Anti-CD300A mAb, mouse IgG1 mAb, anti-CD300C mAb, and rat IgG2a mAb were biotinylated by sulfo-NHS-LC-biotin (Pierce) according to the manufacturer's instructions.

    Techniques: Expressing, Flow Cytometry, Cytometry, Incubation, Enzyme-linked Immunosorbent Assay

    ICP0 interacts with p65 and p50. The HEK 293T cells were cotransfected with ICP0-Myc and Flag-p65 expression plasmids (A) and ICP0-Myc and Flag-p50 expression plasmids (D). At 36 h after transfection, cells were harvested and lysed; the samples were then subjected to IP assays using anti-Myc MAb (IP:Myc) or nonspecific mouse monoclonal antibody (IgG). IP samples were separated by 10% SDS-PAGE, and proteins were transferred onto a PVDF membrane. WB were probed with the indicated Ab. (B, C, E, F) HEK 293T cells were transfected with Flag-ICP0 expression plasmid. At 24 h posttransfection, cells were mock treated (B and E) or treated (C and F) with TNF-α (10 ng/ml) and incubated for an additional 8 h, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). HEK 293T cells were infected with WT HSV-1 at an MOI of 10 for 16 h. The cells were then lysed, and the extracts were subjected to IP using anti-ICP0 pAb (IP:ICP0) or control IgG. Precipitates were analyzed by Western blotting (G and H).

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus 1 E3 Ubiquitin Ligase ICP0 Protein Inhibits Tumor Necrosis Factor Alpha-Induced NF-?B Activation by Interacting with p65/RelA and p50/NF-?B1

    doi: 10.1128/JVI.01952-13

    Figure Lengend Snippet: ICP0 interacts with p65 and p50. The HEK 293T cells were cotransfected with ICP0-Myc and Flag-p65 expression plasmids (A) and ICP0-Myc and Flag-p50 expression plasmids (D). At 36 h after transfection, cells were harvested and lysed; the samples were then subjected to IP assays using anti-Myc MAb (IP:Myc) or nonspecific mouse monoclonal antibody (IgG). IP samples were separated by 10% SDS-PAGE, and proteins were transferred onto a PVDF membrane. WB were probed with the indicated Ab. (B, C, E, F) HEK 293T cells were transfected with Flag-ICP0 expression plasmid. At 24 h posttransfection, cells were mock treated (B and E) or treated (C and F) with TNF-α (10 ng/ml) and incubated for an additional 8 h, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). HEK 293T cells were infected with WT HSV-1 at an MOI of 10 for 16 h. The cells were then lysed, and the extracts were subjected to IP using anti-ICP0 pAb (IP:ICP0) or control IgG. Precipitates were analyzed by Western blotting (G and H).

    Article Snippet: Mouse monoclonal IgG1 and IgG2b isotype control antibodies were purchased from eBioscience Inc. (San Diego, CA).

    Techniques: Expressing, Transfection, SDS Page, Western Blot, Plasmid Preparation, Incubation, Infection

    The RF domain of ICP0 is required for its interaction with p50. The HEK 293T cells were transfected with ICP0(1-241aa)-Flag or ICP0-ΔRF-Myc expression plasmids. At 24 h after transfection, cells were mock treated (A and C) or treated (B and D) with TNF-α (10 ng/ml) and incubated for an additional 8 h. Cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag or anti-Myc MAb (IP:Flag or Myc) or nonspecific mouse monoclonal antibody (IgG2b or IgG1). WB were probed with the indicated Ab. (E) HEK293T cells were infected with ICP0-RF mutant HSV-1 at an MOI of 10 for 16 h. The cells were then lysed, and the extracts were subjected to IP using anti-p50 pAb (IP:p50) or control IgG. Precipitates were analyzed by WB analysis with the indicated Ab.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus 1 E3 Ubiquitin Ligase ICP0 Protein Inhibits Tumor Necrosis Factor Alpha-Induced NF-?B Activation by Interacting with p65/RelA and p50/NF-?B1

    doi: 10.1128/JVI.01952-13

    Figure Lengend Snippet: The RF domain of ICP0 is required for its interaction with p50. The HEK 293T cells were transfected with ICP0(1-241aa)-Flag or ICP0-ΔRF-Myc expression plasmids. At 24 h after transfection, cells were mock treated (A and C) or treated (B and D) with TNF-α (10 ng/ml) and incubated for an additional 8 h. Cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag or anti-Myc MAb (IP:Flag or Myc) or nonspecific mouse monoclonal antibody (IgG2b or IgG1). WB were probed with the indicated Ab. (E) HEK293T cells were infected with ICP0-RF mutant HSV-1 at an MOI of 10 for 16 h. The cells were then lysed, and the extracts were subjected to IP using anti-p50 pAb (IP:p50) or control IgG. Precipitates were analyzed by WB analysis with the indicated Ab.

    Article Snippet: Mouse monoclonal IgG1 and IgG2b isotype control antibodies were purchased from eBioscience Inc. (San Diego, CA).

    Techniques: Transfection, Expressing, Incubation, Western Blot, Infection, Mutagenesis

    ICP0 interacts with the RHD of p65 and blocks TNF-α-induced p65 nuclear translocation. (A) The HEK 293T cells were cotransfected with ICP0-Myc and Flag-p65 RHD expression plasmids. At 36 h after transfection, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). WB were probed with the indicated Ab. (B) The HEK 293T cells were transfected with Flag-p65 RHD expression plasmid. At 24 h after transfection, the cells were infected with WT HSV-1 at an MOI of 10; after 16 h postinfection, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). WB were probed with the indicated Ab. (C) HeLa cells were transfected with control vector, Flag-tagged ICP0 WT, or Myc-tagged ICP0-ΔRF mutant expression plasmid. At 24 h posttransfection, cells were treated with TNF-α (10 ng/ml) or mock treated for 30 min as indicated. Cells were stained with mouse anti-Flag or mouse anti-Myc MAb and rabbit anti-p65 pAb. FITC-conjugated goat anti-rabbit (green) and TRITC-conjugated goat anti-mouse (red) were used as the secondary antibodies. Cell nuclei (blue) were stained with Hoechst 33258. The images were obtained by fluorescence microscopy using a 40× objective.

    Journal: Journal of Virology

    Article Title: Herpes Simplex Virus 1 E3 Ubiquitin Ligase ICP0 Protein Inhibits Tumor Necrosis Factor Alpha-Induced NF-?B Activation by Interacting with p65/RelA and p50/NF-?B1

    doi: 10.1128/JVI.01952-13

    Figure Lengend Snippet: ICP0 interacts with the RHD of p65 and blocks TNF-α-induced p65 nuclear translocation. (A) The HEK 293T cells were cotransfected with ICP0-Myc and Flag-p65 RHD expression plasmids. At 36 h after transfection, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). WB were probed with the indicated Ab. (B) The HEK 293T cells were transfected with Flag-p65 RHD expression plasmid. At 24 h after transfection, the cells were infected with WT HSV-1 at an MOI of 10; after 16 h postinfection, cells were harvested and lysed, and the samples were then subjected to IP assays using anti-Flag MAb (IP:Flag) or nonspecific mouse monoclonal antibody (IgG2b). WB were probed with the indicated Ab. (C) HeLa cells were transfected with control vector, Flag-tagged ICP0 WT, or Myc-tagged ICP0-ΔRF mutant expression plasmid. At 24 h posttransfection, cells were treated with TNF-α (10 ng/ml) or mock treated for 30 min as indicated. Cells were stained with mouse anti-Flag or mouse anti-Myc MAb and rabbit anti-p65 pAb. FITC-conjugated goat anti-rabbit (green) and TRITC-conjugated goat anti-mouse (red) were used as the secondary antibodies. Cell nuclei (blue) were stained with Hoechst 33258. The images were obtained by fluorescence microscopy using a 40× objective.

    Article Snippet: Mouse monoclonal IgG1 and IgG2b isotype control antibodies were purchased from eBioscience Inc. (San Diego, CA).

    Techniques: Translocation Assay, Expressing, Transfection, Western Blot, Plasmid Preparation, Infection, Mutagenesis, Staining, Fluorescence, Microscopy