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  • 99
    Thermo Fisher anti human ab
    Anti Human Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore anti human antibody
    Anti Human Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Santa Cruz Biotechnology anti human egfr antibody
    P. aeruginosa –induced <t>EGFR,</t> ERK1/2, and Akt phosphorylation. HUCL cells were grown to ~90% confluence on 100-mm plates and serum-starved overnight. Cells were then infected with P. aeruginosa at a cell-to-bacterium ratio of 1:25 over a 4-hour time course. Cell lysates were prepared at the designated time points PI. ( A ) For <t>immunoprecipitation,</t> 800 μ g protein for each sample was immunoprecipitated (IP) with 2.5 μ g agarose-conjugated EGFR antibodies, subjected to SDS-PAGE, and probed (WB) with mouse anti-PY99 antibody ( top ); after stripping, reproved with mouse anti-EGFR ( bottom ). ( B ) To assess phosphorylation of ERK1/2 and Akt, 10 and 30 μ g cell lysates of the same samples were subjected to Western blot analysis (WB) with either anti-phospho-ERK1/2 (pERK) or anti-phospho-Akt (pAKT). To normalize protein loading onto blots, anti-ERK2 (ERK2), and anti-Akt (AKT) antibodies were used as probes. The results are representative of three independent experiments.
    Anti Human Egfr Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Abcam anti human mmp25 ab
    Immunohistochemical staining for conventional EMPD ( A , C , E ) and ectopic EMPD ( B , D , F ). Paraffin-embedded tissue samples were deparaffinized and stained with anti-CCL17 Ab ( A , B ), anti-CCL5 Ab ( C , D ), and <t>anti-MMP25</t> Ab ( E , F ). The sections were developed with liquid permanent red. Original magnification. ×200 ( A , B , D ), ×100 ( C ).
    Anti Human Mmp25 Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Quidel anti human c5 ab
    Generation of C5a by activated human PMNs, human PBMCs, or rat AMs. Cells (1 × 10 7 ) were incubated at pH 7.4 with 90 μg of <t>human</t> C5 and (where indicated) PMA (100 ng/ml) or LPS (0.5 μg/ml) for 4 hours at 37°C and then Western blot analysis with anti-human C5a was performed. Positions of the molecular weight markers are shown at the extreme left region of the figure. Data are representative of three or more separate and independent experiments.
    Anti Human C5 Ab, supplied by Quidel, 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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    91
    Becton Dickinson anti human cd69 antibodies
    PRLR-DbsAb activates T cells resulting in Cytokine release. Effector cells (huPBMCs) and target cells (T47D) were incubated with 100 ng/ml recombinant antibodies (PRLR mAb and PRLR-DbsAb) for 20 h (effect-to-target ratio of 10:1). The cells were stained by FACS antibody to analyze the expression of activation marker protein <t>CD69</t> on the surface of PBMCs ( a ), CD4 ( b ) and CD8 ( c ) T cells. And the secreted levels of IFN- γ ( d ), TNF- α ( e ) and IL10 ( f ) in the culture supernatant were detected by Elisa method. The experiment was repeated three times and the data was expressed as the Mean ±SEM, *** P
    Anti Human Cd69 Antibodies, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher anti human opn ab
    Correlation between adiponectin (AD) and osteopontin <t>(OPN)</t> expression in serum and synovial tissue of patients with rheumatoid arthritis (RA). a Serum AD levels were determined in patients with RA ( n = 38) and in healthy controls (HC) ( n = 20) by <t>ELISA.</t> b Serum OPN levels were measured in patients with RA ( n = 38) and HC ( n = 20) by ELISA. c The positive relationship between serum AD and OPN levels in patients with RA. d Serum AD levels were examined in patients with osteoarthritis (OA) ( n = 40) and in HC ( n = 20) by ELISA. e Serum OPN levels were tested in patients with OA ( n = 40) and in HC ( n = 20) by ELISA. f No relationship is observed between serum AD and OPN levels in patients with OA. g Double immunofluorescence analysis of AD and OPN expression in RA and OA synovial tissue ( n = 3). Each section was merged with 4’,6-diamidino-2-phenylindole (DAPI) (magnifications: ×20). Bars show the mean ± SD. The degree of linearity between the two variables was compared using Spearman’s correlation test (two-tailed). ** p
    Anti Human Opn Ab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Becton Dickinson anti human tfr1 ab
    Correlation between adiponectin (AD) and osteopontin <t>(OPN)</t> expression in serum and synovial tissue of patients with rheumatoid arthritis (RA). a Serum AD levels were determined in patients with RA ( n = 38) and in healthy controls (HC) ( n = 20) by <t>ELISA.</t> b Serum OPN levels were measured in patients with RA ( n = 38) and HC ( n = 20) by ELISA. c The positive relationship between serum AD and OPN levels in patients with RA. d Serum AD levels were examined in patients with osteoarthritis (OA) ( n = 40) and in HC ( n = 20) by ELISA. e Serum OPN levels were tested in patients with OA ( n = 40) and in HC ( n = 20) by ELISA. f No relationship is observed between serum AD and OPN levels in patients with OA. g Double immunofluorescence analysis of AD and OPN expression in RA and OA synovial tissue ( n = 3). Each section was merged with 4’,6-diamidino-2-phenylindole (DAPI) (magnifications: ×20). Bars show the mean ± SD. The degree of linearity between the two variables was compared using Spearman’s correlation test (two-tailed). ** p
    Anti Human Tfr1 Ab, supplied by Becton Dickinson, 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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    92
    Abcam anti human fd ab
    Correlation between adiponectin (AD) and osteopontin <t>(OPN)</t> expression in serum and synovial tissue of patients with rheumatoid arthritis (RA). a Serum AD levels were determined in patients with RA ( n = 38) and in healthy controls (HC) ( n = 20) by <t>ELISA.</t> b Serum OPN levels were measured in patients with RA ( n = 38) and HC ( n = 20) by ELISA. c The positive relationship between serum AD and OPN levels in patients with RA. d Serum AD levels were examined in patients with osteoarthritis (OA) ( n = 40) and in HC ( n = 20) by ELISA. e Serum OPN levels were tested in patients with OA ( n = 40) and in HC ( n = 20) by ELISA. f No relationship is observed between serum AD and OPN levels in patients with OA. g Double immunofluorescence analysis of AD and OPN expression in RA and OA synovial tissue ( n = 3). Each section was merged with 4’,6-diamidino-2-phenylindole (DAPI) (magnifications: ×20). Bars show the mean ± SD. The degree of linearity between the two variables was compared using Spearman’s correlation test (two-tailed). ** p
    Anti Human Fd Ab, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    YMC America anti human gd1a ab
    GBM derived gangliosides interact with TNFR1 to induce recruitment of FADD and TRADD leading eventually to downstream activation of caspases. Differential profiles of ganglioside isolates from GBM cell lines CCF52 and CCF4 were obtained by HPTLC using procedure described earlier, as shown in Fig 6A. ELISA assay was also used to detect GM2 and <t>GD1a</t> in extracted gangliosides from CCF52 cell line (Fig 6B). Wells of a 96 well ELISA plate were coated with varying concentrations of CCF52 gangliosides as indicated in the figure legend (Fig 6B). Ganglioside GM2 shed by tumors are taken up by T cells (around 35% GM2-+ve T cells) when cultured with CCF52 supernatants as shown in Fig 6C. Co-localization of GM2 (green) and TNFR1 (red) in T cells treated with CCF52 ganglioside (15μg/ml) for 24hrs was demonstrated from overlay by confocal microscopy (Fig 6D). T cells from normal volunteers were co-cultured with CCF52 gangliosides for 6, 12, 24 and 48hrs. Cells were washed, lysed and co-immunoprecipitated with anti-human TNFR1 Ab. Western immunoblot analysis confirmed that TRADD and FADD co-immunoprecipitated with TNFR1 (Fig 6E), indicating recruitment of the DISC. Representative data from one of 3 experiments is shown.
    Anti Human Gd1a Ab, supplied by YMC America, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Cayman Chemical anti human tp ab
    GBM derived gangliosides interact with TNFR1 to induce recruitment of FADD and TRADD leading eventually to downstream activation of caspases. Differential profiles of ganglioside isolates from GBM cell lines CCF52 and CCF4 were obtained by HPTLC using procedure described earlier, as shown in Fig 6A. ELISA assay was also used to detect GM2 and <t>GD1a</t> in extracted gangliosides from CCF52 cell line (Fig 6B). Wells of a 96 well ELISA plate were coated with varying concentrations of CCF52 gangliosides as indicated in the figure legend (Fig 6B). Ganglioside GM2 shed by tumors are taken up by T cells (around 35% GM2-+ve T cells) when cultured with CCF52 supernatants as shown in Fig 6C. Co-localization of GM2 (green) and TNFR1 (red) in T cells treated with CCF52 ganglioside (15μg/ml) for 24hrs was demonstrated from overlay by confocal microscopy (Fig 6D). T cells from normal volunteers were co-cultured with CCF52 gangliosides for 6, 12, 24 and 48hrs. Cells were washed, lysed and co-immunoprecipitated with anti-human TNFR1 Ab. Western immunoblot analysis confirmed that TRADD and FADD co-immunoprecipitated with TNFR1 (Fig 6E), indicating recruitment of the DISC. Representative data from one of 3 experiments is shown.
    Anti Human Tp Ab, supplied by Cayman Chemical, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Cell Signaling Technology Inc anti human p21 ab
    hUHRF1 suppresses <t>p21</t> expression in cooperation with G9a. ( A ) Quantitative RT–PCR analysis of p21 expression. Total RNA was isolated from HeLa cells transfected with siRNAs as indicated. The Q-PCR data normalized by GAPDH control are shown as the means ± SD of triplicate determinations from four independent experiments. Statistical significance of the differences among the groups was determined by Student's t -test. * P
    Anti Human P21 Ab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Agilent technologies rabbit anti human antibody
    hUHRF1 suppresses <t>p21</t> expression in cooperation with G9a. ( A ) Quantitative RT–PCR analysis of p21 expression. Total RNA was isolated from HeLa cells transfected with siRNAs as indicated. The Q-PCR data normalized by GAPDH control are shown as the means ± SD of triplicate determinations from four independent experiments. Statistical significance of the differences among the groups was determined by Student's t -test. * P
    Rabbit Anti Human Antibody, supplied by Agilent technologies, 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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    88
    R&D Systems anti human β2 gpi ab
    hUHRF1 suppresses <t>p21</t> expression in cooperation with G9a. ( A ) Quantitative RT–PCR analysis of p21 expression. Total RNA was isolated from HeLa cells transfected with siRNAs as indicated. The Q-PCR data normalized by GAPDH control are shown as the means ± SD of triplicate determinations from four independent experiments. Statistical significance of the differences among the groups was determined by Student's t -test. * P
    Anti Human β2 Gpi Ab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    R&D Systems anti human angptl4 antibody ab
    Proteomic expression analysis of <t>ANGPTL4</t> high and low expressing cells The expression of 305 proteins was examined using RPPA analysis in the ANGPTL4 hi and ANGPTL4 lo cells vs. their corresponding control cells. A. , B. , C. Comparisons were done for each pair of cells: (A) cutaneous ANGPTL4 hi vs. CON pQC cells, (B) brain metastasizing ANGPTL4 hi vs. CON pQC cells and (C) brain metastasizing ANGPTL4 lo vs. CON sh cells. The tables show the normalized expression of differentially expressed proteins with FC
    Anti Human Angptl4 Antibody Ab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    GE Healthcare anti human igg ab
    Proteomic expression analysis of <t>ANGPTL4</t> high and low expressing cells The expression of 305 proteins was examined using RPPA analysis in the ANGPTL4 hi and ANGPTL4 lo cells vs. their corresponding control cells. A. , B. , C. Comparisons were done for each pair of cells: (A) cutaneous ANGPTL4 hi vs. CON pQC cells, (B) brain metastasizing ANGPTL4 hi vs. CON pQC cells and (C) brain metastasizing ANGPTL4 lo vs. CON sh cells. The tables show the normalized expression of differentially expressed proteins with FC
    Anti Human Igg Ab, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Mab Technologies anti human perforin ab
    Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); <t>perforin</t> + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).
    Anti Human Perforin Ab, supplied by Mab Technologies, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Jackson Immuno anti human fcγ specific ab
    Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); <t>perforin</t> + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).
    Anti Human Fcγ Specific Ab, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore anti human polyclonal ab
    Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); <t>perforin</t> + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).
    Anti Human Polyclonal Ab, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher anti human gzmb ab
    Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); <t>perforin</t> + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).
    Anti Human Gzmb Ab, supplied by Thermo Fisher, 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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    91
    Agilent technologies anti human igg antibodies
    <t>IgG,</t> <t>IgA,</t> and IgM reactivity to B. adolescentis DSM 20086 proteins among IA-positive and IA-negative individuals.
    Anti Human Igg Antibodies, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 91/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore anti human igg antibody
    <t>LL37,</t> cit-LL37- and LL37-DNA complexes are present in SLE affected tissues. ( A ) Dose response reactivity (expressed as Optical Density, OD) of Mab142 and Mab139, to LL37, cit-LL37 and control peptides (vimentin, VIM, eolase, ENO, vinculin, VINC, scramble LL37, SCR, in their native or citrullinated (citr) forms. ( B ) Number of LL37-positive and cit-LL37 positive spots in CLE and HD dermis assessed by immunohistochemistry. For quantification at least 3 sections for each patients (n = 5) and HD (N = 3) were assessed. Data represent mean ± SE. ( C ) Representative image of immunoistochemistry of the skin of one CLE, upper panels or one HD, lower panels, assessed for expression of native LL37 or cit-LL37. ( D ) Quantification of LL37 and cit-LL37 in 10 SLE-affected kidney biopsies. For quantification at least 3 sections for each patients (n = 10) were assessed. Data represent mean ± SE. ( E ) representative confocal images of staining of SLE kidney biopsies assessed for presence of LL37 or cit-LL37 (magnification 600×). ( F ) Representative confocal images of two out of seven SLE affected renal biopsies showing expression of native or cit-LL37 and DNA filaments (DAPI). ( G ) Confocal images showing expression of LL37, immune-complexes <t>(IgG)</t> and the IFN-induced Mx1. The panels on the left show magnification of two areas to show colocalization (yellow) of IgG staining with LL37 staining. ( H ) Quantification (as percentage) of co-localization between IgG staining and LL37 staining, in SLE renal biopsies from three different patients. For quantification 3 sections for each patient were assessed. Data represent mean ± SE. All biopsies were from lupus nephritis (class IV). Skin biopsies were form CLE patients.
    Anti Human Igg Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 143 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Miltenyi Biotec anti human cd133 ab
    Characteristics of myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells. (a) Expression of CD106 and <t>CD133.</t> After selected with anti-human CD34 Ab-coated magnetic beads cells were further separated with anti-human D7-FIB Ab-coated magnetic beads, and analyzed. (b) Microscopical appearance of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells (×400). May-Giemsa, and immunocytochemical staining of S100, human fibronectin, and human SMA. (c) FISH analysis of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow. BCR-ABL fusion signal is indicated with an arrow. 83 cells are positive in total 100 cells analyzed.
    Anti Human Cd133 Ab, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 85/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Pharmingen anti human vβ3pe ab s
    Characteristics of myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells. (a) Expression of CD106 and <t>CD133.</t> After selected with anti-human CD34 Ab-coated magnetic beads cells were further separated with anti-human D7-FIB Ab-coated magnetic beads, and analyzed. (b) Microscopical appearance of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells (×400). May-Giemsa, and immunocytochemical staining of S100, human fibronectin, and human SMA. (c) FISH analysis of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow. BCR-ABL fusion signal is indicated with an arrow. 83 cells are positive in total 100 cells analyzed.
    Anti Human Vβ3pe Ab S, supplied by Pharmingen, 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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    Cell Signaling Technology Inc rabbit anti human ab
    Characteristics of myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells. (a) Expression of CD106 and <t>CD133.</t> After selected with anti-human CD34 Ab-coated magnetic beads cells were further separated with anti-human D7-FIB Ab-coated magnetic beads, and analyzed. (b) Microscopical appearance of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells (×400). May-Giemsa, and immunocytochemical staining of S100, human fibronectin, and human SMA. (c) FISH analysis of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow. BCR-ABL fusion signal is indicated with an arrow. 83 cells are positive in total 100 cells analyzed.
    Rabbit Anti Human Ab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    P. aeruginosa –induced EGFR, ERK1/2, and Akt phosphorylation. HUCL cells were grown to ~90% confluence on 100-mm plates and serum-starved overnight. Cells were then infected with P. aeruginosa at a cell-to-bacterium ratio of 1:25 over a 4-hour time course. Cell lysates were prepared at the designated time points PI. ( A ) For immunoprecipitation, 800 μ g protein for each sample was immunoprecipitated (IP) with 2.5 μ g agarose-conjugated EGFR antibodies, subjected to SDS-PAGE, and probed (WB) with mouse anti-PY99 antibody ( top ); after stripping, reproved with mouse anti-EGFR ( bottom ). ( B ) To assess phosphorylation of ERK1/2 and Akt, 10 and 30 μ g cell lysates of the same samples were subjected to Western blot analysis (WB) with either anti-phospho-ERK1/2 (pERK) or anti-phospho-Akt (pAKT). To normalize protein loading onto blots, anti-ERK2 (ERK2), and anti-Akt (AKT) antibodies were used as probes. The results are representative of three independent experiments.

    Journal: Investigative ophthalmology & visual science

    Article Title: Role of EGFR Transactivation in Preventing Apoptosis in Pseudomonas aeruginosa-Infected Human Corneal Epithelial Cells

    doi: 10.1167/iovs.03-1323

    Figure Lengend Snippet: P. aeruginosa –induced EGFR, ERK1/2, and Akt phosphorylation. HUCL cells were grown to ~90% confluence on 100-mm plates and serum-starved overnight. Cells were then infected with P. aeruginosa at a cell-to-bacterium ratio of 1:25 over a 4-hour time course. Cell lysates were prepared at the designated time points PI. ( A ) For immunoprecipitation, 800 μ g protein for each sample was immunoprecipitated (IP) with 2.5 μ g agarose-conjugated EGFR antibodies, subjected to SDS-PAGE, and probed (WB) with mouse anti-PY99 antibody ( top ); after stripping, reproved with mouse anti-EGFR ( bottom ). ( B ) To assess phosphorylation of ERK1/2 and Akt, 10 and 30 μ g cell lysates of the same samples were subjected to Western blot analysis (WB) with either anti-phospho-ERK1/2 (pERK) or anti-phospho-Akt (pAKT). To normalize protein loading onto blots, anti-ERK2 (ERK2), and anti-Akt (AKT) antibodies were used as probes. The results are representative of three independent experiments.

    Article Snippet: Equal amounts of protein (800 μ g) were subjected to immunoprecipitation with 3 μ g anti-human EGFR antibody and 20 μ L protein G beads (Santa Cruz Biotechnology, Santa Cruz, CA) at 4°C overnight.

    Techniques: Infection, Immunoprecipitation, SDS Page, Western Blot, Stripping Membranes

    Immunohistochemical staining for conventional EMPD ( A , C , E ) and ectopic EMPD ( B , D , F ). Paraffin-embedded tissue samples were deparaffinized and stained with anti-CCL17 Ab ( A , B ), anti-CCL5 Ab ( C , D ), and anti-MMP25 Ab ( E , F ). The sections were developed with liquid permanent red. Original magnification. ×200 ( A , B , D ), ×100 ( C ).

    Journal: Case Reports in Dermatology

    Article Title: RANKL-Expressing Ectopic Extramammary Paget's Disease on the Lower Abdomen

    doi: 10.1159/000445992

    Figure Lengend Snippet: Immunohistochemical staining for conventional EMPD ( A , C , E ) and ectopic EMPD ( B , D , F ). Paraffin-embedded tissue samples were deparaffinized and stained with anti-CCL17 Ab ( A , B ), anti-CCL5 Ab ( C , D ), and anti-MMP25 Ab ( E , F ). The sections were developed with liquid permanent red. Original magnification. ×200 ( A , B , D ), ×100 ( C ).

    Article Snippet: The following antibodies (Abs) were used for immunofluorescence staining: mouse monoclonal anti-human CD163 Ab (clone: 10D6; Novocastra, UK), and anti-human CCL5 Ab (clone: 50013–5; LifeSpan BioScience, Seattle, Wash., USA), rabbit polyclonal anti-human RANKL Ab (LifeSpan BioScience), anti-human MMP7 Ab (LifeSpan BioScience), and anti-human MMP25 Ab (Abcam, Tokyo, Japan), and goat polyclonal anti-human CCL17 Ab (R & D Systems, Tokyo, Japan).

    Techniques: Immunohistochemistry, Staining

    Generation of C5a by activated human PMNs, human PBMCs, or rat AMs. Cells (1 × 10 7 ) were incubated at pH 7.4 with 90 μg of human C5 and (where indicated) PMA (100 ng/ml) or LPS (0.5 μg/ml) for 4 hours at 37°C and then Western blot analysis with anti-human C5a was performed. Positions of the molecular weight markers are shown at the extreme left region of the figure. Data are representative of three or more separate and independent experiments.

    Journal: The American Journal of Pathology

    Article Title: Generation of C5a by Phagocytic Cells

    doi:

    Figure Lengend Snippet: Generation of C5a by activated human PMNs, human PBMCs, or rat AMs. Cells (1 × 10 7 ) were incubated at pH 7.4 with 90 μg of human C5 and (where indicated) PMA (100 ng/ml) or LPS (0.5 μg/ml) for 4 hours at 37°C and then Western blot analysis with anti-human C5a was performed. Positions of the molecular weight markers are shown at the extreme left region of the figure. Data are representative of three or more separate and independent experiments.

    Article Snippet: Anti-human C5 Ab was obtained from Quidel.

    Techniques: Affinity Magnetic Separation, Incubation, Western Blot, Molecular Weight

    A and B: Western blot detection of human C5a in supernatant fluids obtained up to 4 hours after addition of 90 μg of human C5 to 10 × 10 6 AMs ( A ) or 10 × 10 6 PMNs ( B ) in the presence of PMA (100 ng/ml). Positions of molecular weight markers are shown in the extreme right lane . C: Western blot analysis of supernatant fluids from PMA-stimulated rat AMs in the presence of increasing amounts (30 to 120 μg) of C5. Western blots in A , B , and C were all probed with anti-human C5a. Data are representative of four or more separate and independent experiments.

    Journal: The American Journal of Pathology

    Article Title: Generation of C5a by Phagocytic Cells

    doi:

    Figure Lengend Snippet: A and B: Western blot detection of human C5a in supernatant fluids obtained up to 4 hours after addition of 90 μg of human C5 to 10 × 10 6 AMs ( A ) or 10 × 10 6 PMNs ( B ) in the presence of PMA (100 ng/ml). Positions of molecular weight markers are shown in the extreme right lane . C: Western blot analysis of supernatant fluids from PMA-stimulated rat AMs in the presence of increasing amounts (30 to 120 μg) of C5. Western blots in A , B , and C were all probed with anti-human C5a. Data are representative of four or more separate and independent experiments.

    Article Snippet: Anti-human C5 Ab was obtained from Quidel.

    Techniques: Western Blot, Affinity Magnetic Separation, Molecular Weight

    PRLR-DbsAb activates T cells resulting in Cytokine release. Effector cells (huPBMCs) and target cells (T47D) were incubated with 100 ng/ml recombinant antibodies (PRLR mAb and PRLR-DbsAb) for 20 h (effect-to-target ratio of 10:1). The cells were stained by FACS antibody to analyze the expression of activation marker protein CD69 on the surface of PBMCs ( a ), CD4 ( b ) and CD8 ( c ) T cells. And the secreted levels of IFN- γ ( d ), TNF- α ( e ) and IL10 ( f ) in the culture supernatant were detected by Elisa method. The experiment was repeated three times and the data was expressed as the Mean ±SEM, *** P

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: A novel bispecific antibody targeting CD3 and prolactin receptor (PRLR) against PRLR-expression breast cancer

    doi: 10.1186/s13046-020-01564-4

    Figure Lengend Snippet: PRLR-DbsAb activates T cells resulting in Cytokine release. Effector cells (huPBMCs) and target cells (T47D) were incubated with 100 ng/ml recombinant antibodies (PRLR mAb and PRLR-DbsAb) for 20 h (effect-to-target ratio of 10:1). The cells were stained by FACS antibody to analyze the expression of activation marker protein CD69 on the surface of PBMCs ( a ), CD4 ( b ) and CD8 ( c ) T cells. And the secreted levels of IFN- γ ( d ), TNF- α ( e ) and IL10 ( f ) in the culture supernatant were detected by Elisa method. The experiment was repeated three times and the data was expressed as the Mean ±SEM, *** P

    Article Snippet: Cells were also harvested and analyzed for activation with anti-human CD4, anti-human CD8 and anti-human CD69 antibodies (BD Biosciences).

    Techniques: Incubation, Recombinant, Staining, FACS, Expressing, Activation Assay, Marker, Enzyme-linked Immunosorbent Assay

    Correlation between adiponectin (AD) and osteopontin (OPN) expression in serum and synovial tissue of patients with rheumatoid arthritis (RA). a Serum AD levels were determined in patients with RA ( n = 38) and in healthy controls (HC) ( n = 20) by ELISA. b Serum OPN levels were measured in patients with RA ( n = 38) and HC ( n = 20) by ELISA. c The positive relationship between serum AD and OPN levels in patients with RA. d Serum AD levels were examined in patients with osteoarthritis (OA) ( n = 40) and in HC ( n = 20) by ELISA. e Serum OPN levels were tested in patients with OA ( n = 40) and in HC ( n = 20) by ELISA. f No relationship is observed between serum AD and OPN levels in patients with OA. g Double immunofluorescence analysis of AD and OPN expression in RA and OA synovial tissue ( n = 3). Each section was merged with 4’,6-diamidino-2-phenylindole (DAPI) (magnifications: ×20). Bars show the mean ± SD. The degree of linearity between the two variables was compared using Spearman’s correlation test (two-tailed). ** p

    Journal: Arthritis Research & Therapy

    Article Title: Adiponectin aggravates bone erosion by promoting osteopontin production in synovial tissue of rheumatoid arthritis

    doi: 10.1186/s13075-018-1526-y

    Figure Lengend Snippet: Correlation between adiponectin (AD) and osteopontin (OPN) expression in serum and synovial tissue of patients with rheumatoid arthritis (RA). a Serum AD levels were determined in patients with RA ( n = 38) and in healthy controls (HC) ( n = 20) by ELISA. b Serum OPN levels were measured in patients with RA ( n = 38) and HC ( n = 20) by ELISA. c The positive relationship between serum AD and OPN levels in patients with RA. d Serum AD levels were examined in patients with osteoarthritis (OA) ( n = 40) and in HC ( n = 20) by ELISA. e Serum OPN levels were tested in patients with OA ( n = 40) and in HC ( n = 20) by ELISA. f No relationship is observed between serum AD and OPN levels in patients with OA. g Double immunofluorescence analysis of AD and OPN expression in RA and OA synovial tissue ( n = 3). Each section was merged with 4’,6-diamidino-2-phenylindole (DAPI) (magnifications: ×20). Bars show the mean ± SD. The degree of linearity between the two variables was compared using Spearman’s correlation test (two-tailed). ** p

    Article Snippet: The human AD and OPN enzyme-linked immunosorbent assay (ELISA) kits and anti-human OPN Ab were obtained from eBioscience (Los Angeles, CA, USA).

    Techniques: Expressing, Enzyme-linked Immunosorbent Assay, Immunofluorescence, Two Tailed Test

    GBM derived gangliosides interact with TNFR1 to induce recruitment of FADD and TRADD leading eventually to downstream activation of caspases. Differential profiles of ganglioside isolates from GBM cell lines CCF52 and CCF4 were obtained by HPTLC using procedure described earlier, as shown in Fig 6A. ELISA assay was also used to detect GM2 and GD1a in extracted gangliosides from CCF52 cell line (Fig 6B). Wells of a 96 well ELISA plate were coated with varying concentrations of CCF52 gangliosides as indicated in the figure legend (Fig 6B). Ganglioside GM2 shed by tumors are taken up by T cells (around 35% GM2-+ve T cells) when cultured with CCF52 supernatants as shown in Fig 6C. Co-localization of GM2 (green) and TNFR1 (red) in T cells treated with CCF52 ganglioside (15μg/ml) for 24hrs was demonstrated from overlay by confocal microscopy (Fig 6D). T cells from normal volunteers were co-cultured with CCF52 gangliosides for 6, 12, 24 and 48hrs. Cells were washed, lysed and co-immunoprecipitated with anti-human TNFR1 Ab. Western immunoblot analysis confirmed that TRADD and FADD co-immunoprecipitated with TNFR1 (Fig 6E), indicating recruitment of the DISC. Representative data from one of 3 experiments is shown.

    Journal: PLoS ONE

    Article Title: GBM Derived Gangliosides Induce T Cell Apoptosis through Activation of the Caspase Cascade Involving Both the Extrinsic and the Intrinsic Pathway

    doi: 10.1371/journal.pone.0134425

    Figure Lengend Snippet: GBM derived gangliosides interact with TNFR1 to induce recruitment of FADD and TRADD leading eventually to downstream activation of caspases. Differential profiles of ganglioside isolates from GBM cell lines CCF52 and CCF4 were obtained by HPTLC using procedure described earlier, as shown in Fig 6A. ELISA assay was also used to detect GM2 and GD1a in extracted gangliosides from CCF52 cell line (Fig 6B). Wells of a 96 well ELISA plate were coated with varying concentrations of CCF52 gangliosides as indicated in the figure legend (Fig 6B). Ganglioside GM2 shed by tumors are taken up by T cells (around 35% GM2-+ve T cells) when cultured with CCF52 supernatants as shown in Fig 6C. Co-localization of GM2 (green) and TNFR1 (red) in T cells treated with CCF52 ganglioside (15μg/ml) for 24hrs was demonstrated from overlay by confocal microscopy (Fig 6D). T cells from normal volunteers were co-cultured with CCF52 gangliosides for 6, 12, 24 and 48hrs. Cells were washed, lysed and co-immunoprecipitated with anti-human TNFR1 Ab. Western immunoblot analysis confirmed that TRADD and FADD co-immunoprecipitated with TNFR1 (Fig 6E), indicating recruitment of the DISC. Representative data from one of 3 experiments is shown.

    Article Snippet: Briefly, CCF52 gangliosides were coated on a 96 well flat bottomed ELISA plate and immunostained with 1μg/ml of both hamster human GM2 Ab (DMF10.167.4) or anti-human GD1a Ab (Seika Gaku) followed by staining with HRP-conjugated goat anti-hamster IgG or rabbit anti-mouse IgM, respectively.

    Techniques: Derivative Assay, Activation Assay, High Performance Thin Layer Chromatography, Enzyme-linked Immunosorbent Assay, Cell Culture, Confocal Microscopy, Immunoprecipitation, Western Blot

    hUHRF1 suppresses p21 expression in cooperation with G9a. ( A ) Quantitative RT–PCR analysis of p21 expression. Total RNA was isolated from HeLa cells transfected with siRNAs as indicated. The Q-PCR data normalized by GAPDH control are shown as the means ± SD of triplicate determinations from four independent experiments. Statistical significance of the differences among the groups was determined by Student's t -test. * P

    Journal: Nucleic Acids Research

    Article Title: UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells

    doi: 10.1093/nar/gkn961

    Figure Lengend Snippet: hUHRF1 suppresses p21 expression in cooperation with G9a. ( A ) Quantitative RT–PCR analysis of p21 expression. Total RNA was isolated from HeLa cells transfected with siRNAs as indicated. The Q-PCR data normalized by GAPDH control are shown as the means ± SD of triplicate determinations from four independent experiments. Statistical significance of the differences among the groups was determined by Student's t -test. * P

    Article Snippet: Antibodies (Ab) used for immunoprecipitation and western analyses were as follows: anti-GFP Ab (Roche Applied Science), anti-hUHRF1 Ab (BD Biosciences), anti-G9a Ab (Sigma), anti-human p21 Ab (Cell Signaling Technology), anti-mouse p21 Ab (Abcam), anti-dimethyl histone H3 (Lys9) Ab (Millipore), anti-histone H3 Ab (Cell Signaling Technology), anti-phospho-histone H3 (Ser10) Ab (Cell Signaling Technology), anti-actin Ab (Sigma) and anti-DNMT1 Ab (New England Biolabs).

    Techniques: Expressing, Quantitative RT-PCR, Isolation, Transfection, Polymerase Chain Reaction

    hUHRF1 recruits G9a and other chromatin modification enzymes to p21 promoter. ( A ) Linearity of PCR amplification using primer sets for proximal (−385 to −240) and distal (−4164 to −3959) regions of p21 promoter with increasing amount of input DNA. ( B ) ChIP analysis of p21 promoter after KD of hUHRF1. HeLa cells were transfected with either control siRNA (CTL KD) or hUHRF1 siRNA (hUHRF1 KD). Using the chromatin isolated from the KD cells, ChIP was performed to detect the proteins or histone modification as indicated at the top of the panel. 5% input is shown. ( C ) Quantitative ChIP analysis for relative p21 promoter occupancy of hUHRF1, G9a and dimethylated H3K9 (H3K9me2) after KD of hUHRF1 or G9a. Q-PCR data of each group were normalized to its input as % input. The relative p21 promoter occupancy of hUHRF1 or G9a KD samples represents the fold change in percentage input over that of the CTL KD. Error bars indicate standard deviation of three independent experiments. ( D ) ChIP analysis of p21 promoter after KD of DNMT1. HeLa cells were transfected with either control siRNA (CTL KD) or DNMT1 siRNA (DNMT1 KD). CHIP was performed as described in (B) and 5% input is shown.

    Journal: Nucleic Acids Research

    Article Title: UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells

    doi: 10.1093/nar/gkn961

    Figure Lengend Snippet: hUHRF1 recruits G9a and other chromatin modification enzymes to p21 promoter. ( A ) Linearity of PCR amplification using primer sets for proximal (−385 to −240) and distal (−4164 to −3959) regions of p21 promoter with increasing amount of input DNA. ( B ) ChIP analysis of p21 promoter after KD of hUHRF1. HeLa cells were transfected with either control siRNA (CTL KD) or hUHRF1 siRNA (hUHRF1 KD). Using the chromatin isolated from the KD cells, ChIP was performed to detect the proteins or histone modification as indicated at the top of the panel. 5% input is shown. ( C ) Quantitative ChIP analysis for relative p21 promoter occupancy of hUHRF1, G9a and dimethylated H3K9 (H3K9me2) after KD of hUHRF1 or G9a. Q-PCR data of each group were normalized to its input as % input. The relative p21 promoter occupancy of hUHRF1 or G9a KD samples represents the fold change in percentage input over that of the CTL KD. Error bars indicate standard deviation of three independent experiments. ( D ) ChIP analysis of p21 promoter after KD of DNMT1. HeLa cells were transfected with either control siRNA (CTL KD) or DNMT1 siRNA (DNMT1 KD). CHIP was performed as described in (B) and 5% input is shown.

    Article Snippet: Antibodies (Ab) used for immunoprecipitation and western analyses were as follows: anti-GFP Ab (Roche Applied Science), anti-hUHRF1 Ab (BD Biosciences), anti-G9a Ab (Sigma), anti-human p21 Ab (Cell Signaling Technology), anti-mouse p21 Ab (Abcam), anti-dimethyl histone H3 (Lys9) Ab (Millipore), anti-histone H3 Ab (Cell Signaling Technology), anti-phospho-histone H3 (Ser10) Ab (Cell Signaling Technology), anti-actin Ab (Sigma) and anti-DNMT1 Ab (New England Biolabs).

    Techniques: Modification, Polymerase Chain Reaction, Amplification, Chromatin Immunoprecipitation, Transfection, CTL Assay, Isolation, Standard Deviation

    hUHRF1 cooperates with G9a to enhance the transcriptional repression of p21 promoter. ( A ) hUHRF1-mediated transcriptional repression of the p21 promoter-luciferase reporter. COS-7 cells were cotransfected with the reporter (2 μg) and increasing amounts of EGFP-hUHRF1 as indicated at the bottom of the panel. ( B ) Enhanced transcriptional repression by G9a in the presence of exogenous hUHRF1. Luciferase activities were measured from COS-7 cells cotransfected with the same reporter described earlier and increasing amounts of EGFP-G9a (0.1–1 μg) with or without a constant amount (0.4 μg) of EGFP-hUHRF1. The luciferase assays were performed as described in Figure 4, and the data represent the means ± SD of duplicate determinations from three separate experiments. Western blot analyses of hUHRF1 and G9a expression by anti-GFP antibody are shown for each cotransfection group. ( C ) Loss of interaction between UHRF1 and G9a abolishes the UHRF1/G9a-mediated repression of p21 promoter. Reporter assays were performed as described in (B), using the wild-type G9a plasmid (EGFP-G9a) and its deletion mutant lacking the N-terminal UHRF1-interacting region (EGFP-NΔG9a). Expression of hUHRF1 and G9a/NΔG9a is shown by western blot analyses with anti-GFP antibody.

    Journal: Nucleic Acids Research

    Article Title: UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells

    doi: 10.1093/nar/gkn961

    Figure Lengend Snippet: hUHRF1 cooperates with G9a to enhance the transcriptional repression of p21 promoter. ( A ) hUHRF1-mediated transcriptional repression of the p21 promoter-luciferase reporter. COS-7 cells were cotransfected with the reporter (2 μg) and increasing amounts of EGFP-hUHRF1 as indicated at the bottom of the panel. ( B ) Enhanced transcriptional repression by G9a in the presence of exogenous hUHRF1. Luciferase activities were measured from COS-7 cells cotransfected with the same reporter described earlier and increasing amounts of EGFP-G9a (0.1–1 μg) with or without a constant amount (0.4 μg) of EGFP-hUHRF1. The luciferase assays were performed as described in Figure 4, and the data represent the means ± SD of duplicate determinations from three separate experiments. Western blot analyses of hUHRF1 and G9a expression by anti-GFP antibody are shown for each cotransfection group. ( C ) Loss of interaction between UHRF1 and G9a abolishes the UHRF1/G9a-mediated repression of p21 promoter. Reporter assays were performed as described in (B), using the wild-type G9a plasmid (EGFP-G9a) and its deletion mutant lacking the N-terminal UHRF1-interacting region (EGFP-NΔG9a). Expression of hUHRF1 and G9a/NΔG9a is shown by western blot analyses with anti-GFP antibody.

    Article Snippet: Antibodies (Ab) used for immunoprecipitation and western analyses were as follows: anti-GFP Ab (Roche Applied Science), anti-hUHRF1 Ab (BD Biosciences), anti-G9a Ab (Sigma), anti-human p21 Ab (Cell Signaling Technology), anti-mouse p21 Ab (Abcam), anti-dimethyl histone H3 (Lys9) Ab (Millipore), anti-histone H3 Ab (Cell Signaling Technology), anti-phospho-histone H3 (Ser10) Ab (Cell Signaling Technology), anti-actin Ab (Sigma) and anti-DNMT1 Ab (New England Biolabs).

    Techniques: Luciferase, Western Blot, Expressing, Cotransfection, Plasmid Preparation, Mutagenesis

    Proteomic expression analysis of ANGPTL4 high and low expressing cells The expression of 305 proteins was examined using RPPA analysis in the ANGPTL4 hi and ANGPTL4 lo cells vs. their corresponding control cells. A. , B. , C. Comparisons were done for each pair of cells: (A) cutaneous ANGPTL4 hi vs. CON pQC cells, (B) brain metastasizing ANGPTL4 hi vs. CON pQC cells and (C) brain metastasizing ANGPTL4 lo vs. CON sh cells. The tables show the normalized expression of differentially expressed proteins with FC

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: Proteomic expression analysis of ANGPTL4 high and low expressing cells The expression of 305 proteins was examined using RPPA analysis in the ANGPTL4 hi and ANGPTL4 lo cells vs. their corresponding control cells. A. , B. , C. Comparisons were done for each pair of cells: (A) cutaneous ANGPTL4 hi vs. CON pQC cells, (B) brain metastasizing ANGPTL4 hi vs. CON pQC cells and (C) brain metastasizing ANGPTL4 lo vs. CON sh cells. The tables show the normalized expression of differentially expressed proteins with FC

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques: Expressing

    ANGPTL4 controls the malignancy phenotype of cutaneous and brain metastasizing melanoma variants A. - C. Cutaneous (CUT) and melanoma brain metastasizing (MBM) variants were transduced with an ANGPTL4 cDNA-containing construct (ANGPTL4 hi ) or with the backbone construct pQCXIP (CON pQC ). MBM cells were transduced with a mixture of 4 different shANGPTL4-containing constructs (ANGPTL4 lo ), or with the control construct (CON sh ). The efficacy of ANGPTL4 over-expression or down-regulation was verified: (A) RT-qPCR analysis was performed to determine the mRNA expression level of ANGPTL4. The bars represent the relative ANGPTL4 expression (normalized to RS9) in ANGPTL4 hi or ANGPTL4 lo cells compared to control cells + SEM obtained in one measurement in at least three independent experiments. * P

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: ANGPTL4 controls the malignancy phenotype of cutaneous and brain metastasizing melanoma variants A. - C. Cutaneous (CUT) and melanoma brain metastasizing (MBM) variants were transduced with an ANGPTL4 cDNA-containing construct (ANGPTL4 hi ) or with the backbone construct pQCXIP (CON pQC ). MBM cells were transduced with a mixture of 4 different shANGPTL4-containing constructs (ANGPTL4 lo ), or with the control construct (CON sh ). The efficacy of ANGPTL4 over-expression or down-regulation was verified: (A) RT-qPCR analysis was performed to determine the mRNA expression level of ANGPTL4. The bars represent the relative ANGPTL4 expression (normalized to RS9) in ANGPTL4 hi or ANGPTL4 lo cells compared to control cells + SEM obtained in one measurement in at least three independent experiments. * P

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques: Transduction, Construct, Over Expression, Quantitative RT-PCR, Expressing

    Secretion of bioactive factors from melanoma cells is dependent on ANGPTL4 expression level A. - C. Melanoma cells were cultured for 24 hrs, then starved for additional 24 hrs, to allow secretion of melanoma-soluble factors. CM was collected and added to BEC. Cell viability of BEC grown with CM of cutaneous CON pQC and ANGPTL4 hi melanoma cells (A) or MBM CON pQC and ANGPTL4 hi melanoma cells (B) was monitored after 24, 48 and 120 hrs. Cell viability of BEC grown with CM of MBM CON sh and ANGPTL4 lo melanoma cells (C) was monitored after 72 hrs. Viability was determined using XTT-based assay. Absorbance at 450 nm was determined for each well, and subtraction of nonspecific readings (measured at 630 nm) was calculated. The bars represent the average viability of the BEC grown with ANGPTL4 hi or ANGPTL4 lo melanoma CM relative to those grown in control melanoma CM + SD in three independent experiments. Six replicates were performed in each experiment. * P

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: Secretion of bioactive factors from melanoma cells is dependent on ANGPTL4 expression level A. - C. Melanoma cells were cultured for 24 hrs, then starved for additional 24 hrs, to allow secretion of melanoma-soluble factors. CM was collected and added to BEC. Cell viability of BEC grown with CM of cutaneous CON pQC and ANGPTL4 hi melanoma cells (A) or MBM CON pQC and ANGPTL4 hi melanoma cells (B) was monitored after 24, 48 and 120 hrs. Cell viability of BEC grown with CM of MBM CON sh and ANGPTL4 lo melanoma cells (C) was monitored after 72 hrs. Viability was determined using XTT-based assay. Absorbance at 450 nm was determined for each well, and subtraction of nonspecific readings (measured at 630 nm) was calculated. The bars represent the average viability of the BEC grown with ANGPTL4 hi or ANGPTL4 lo melanoma CM relative to those grown in control melanoma CM + SD in three independent experiments. Six replicates were performed in each experiment. * P

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques: Expressing, Cell Culture, XTT Assay

    ANGPTL4 alters the tumorigenic potential of melanoma cells A. Volume of cutaneous tumors following subdermal implantation of CON pQC vs. ANGPTL4 hi cutaneous cells. Tumor dimensions were measured using a caliper and volume was obtained as described in Materials and Methods. The average tumor volume + SEM is presented. * P

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: ANGPTL4 alters the tumorigenic potential of melanoma cells A. Volume of cutaneous tumors following subdermal implantation of CON pQC vs. ANGPTL4 hi cutaneous cells. Tumor dimensions were measured using a caliper and volume was obtained as described in Materials and Methods. The average tumor volume + SEM is presented. * P

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques:

    A proposed mechanism for ANGPTL4-mediated melanoma malignancy progression A soluble factor in the microenvironment of the primary tumor transforming growth factor β1 (TGFβ1) induces the expression of ANGPTL4 in primary melanoma tumor cells. ANGPTL4 enhances their ability to migrate through extracellular matrix (ECM) components and to adhere and invade brain vasculature, for example by down-regulating the expression of cell-cell adhesion tight junction (TJ) molecules such as claudin-1 (CLDN1). Once arriving the brain, brain-derived soluble factors secreted by microglia, brain endothelial cells (BEC) and astrocytes, induce ANGPTL4 expression by brain metastasizing cells, what contributes to different phenotypes, such as resistance against brain-derived cytotoxic factors, enhancement of BEC growth and induction of angiogenesis-related genes such as angiopoietin 1 (ANG1) (data not shown) in BEC subjected to factors released from brain metastasizing cells, expressing high ANGPTL4 levels.

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: A proposed mechanism for ANGPTL4-mediated melanoma malignancy progression A soluble factor in the microenvironment of the primary tumor transforming growth factor β1 (TGFβ1) induces the expression of ANGPTL4 in primary melanoma tumor cells. ANGPTL4 enhances their ability to migrate through extracellular matrix (ECM) components and to adhere and invade brain vasculature, for example by down-regulating the expression of cell-cell adhesion tight junction (TJ) molecules such as claudin-1 (CLDN1). Once arriving the brain, brain-derived soluble factors secreted by microglia, brain endothelial cells (BEC) and astrocytes, induce ANGPTL4 expression by brain metastasizing cells, what contributes to different phenotypes, such as resistance against brain-derived cytotoxic factors, enhancement of BEC growth and induction of angiogenesis-related genes such as angiopoietin 1 (ANG1) (data not shown) in BEC subjected to factors released from brain metastasizing cells, expressing high ANGPTL4 levels.

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques: Expressing, Derivative Assay

    ANGPTL4 expression during melanoma progression to brain metastasis A. ANGPTL4 protein expression level in UCLA-SO-M12, UCLA-SO-M16 and DP-0574-Me cutaneous (CUT) and melanoma brain metastasizing (MBM) variants of first and second IC inoculation cycle was analyzed using Western blotting. The obtained values were normalized to β-Tubulin. The bars represent the relative expression of ANGPTL4 (normalized to RS9), compared to control, untreated cells + SD obtained in one measurement in at least three independent experiments. * P

    Journal: Oncotarget

    Article Title: ANGPTL4 promotes the progression of cutaneous melanoma to brain metastasis

    doi: 10.18632/oncotarget.19018

    Figure Lengend Snippet: ANGPTL4 expression during melanoma progression to brain metastasis A. ANGPTL4 protein expression level in UCLA-SO-M12, UCLA-SO-M16 and DP-0574-Me cutaneous (CUT) and melanoma brain metastasizing (MBM) variants of first and second IC inoculation cycle was analyzed using Western blotting. The obtained values were normalized to β-Tubulin. The bars represent the relative expression of ANGPTL4 (normalized to RS9), compared to control, untreated cells + SD obtained in one measurement in at least three independent experiments. * P

    Article Snippet: For detection of the target proteins, membranes were incubated with relevant primary antibodies: Anti-human ANGPTL4 antibody (Ab) (1:350, R & D Systems, Inc., Minneapolis, MA, USA) and rabbit polyclonal to beta Tubulin (1:500, Abcam, Cambridge, UK).

    Techniques: Expressing, Western Blot

    Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); perforin + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).

    Journal: Frontiers in Immunology

    Article Title: Differentially Expressed Potassium Channels Are Associated with Function of Human Effector Memory CD8+ T Cells

    doi: 10.3389/fimmu.2017.00859

    Figure Lengend Snippet: Greater numbers of interleukin (IL)-7Rα high effector memory (EM) CD8 + T cells than IL-7Rα low EM CD8 + T cells in the skin. (A) Immunofluorescence staining (40×) of CD8 + T cells (green) from non-lesional (healthy, HC) or lesional atopic dermatitis skin. IL-7Rα + CD8 + T cells (upper panel) representing IL-7Rα high EM CD8 + T cells were stained with antibodies (Abs) to IL-7Rα (red); perforin + CD8 + T cells (lower panel) representing IL-7Rα low EM CD8 + T cells, were stained with Abs to perforin (red). The image of the box was magnified twice and placed to the right of each image. (B) A quantitative measurement of IL-7Rα + and perforin + CD8 + T cells (frequency and number per tissue) in panel (A) , representing IL-7Rα high and IL-7Rα low EM CD8 + T cells, respectively. Four images per slide were evaluated for quantification. Data are representative of four independent experiments. Bars represent the mean, and p -values were obtained using the Wilcoxon matched pairs test (for comparing frequency and number between the two CD8 + T cell subsets) and Mann–Whitney U test (for comparing IL-7Rα + /perforin + ratio between HC and dermatitis).

    Article Snippet: Tissue sections (7 µm) were fixed in 4% paraformaldehyde, blocked with a blocking buffer (5% goat serum and 5% BSA in PBS) for 30 min at room temperature, and stained with purified anti-human perforin Ab (Mabtech, Nacka Strand, Sweden), Alexa647-conjugated anti-human CD8 Ab (BD Biosciences), biotin-conjugated anti-human IL-7Rα Ab (13-1278, eBioscience), Streptavidin-Cy3 (Life Technologies), and Alexa488-conjugated anti-mouse IgG Ab (Life Technologies) at 4°C overnight.

    Techniques: Immunofluorescence, Staining, MANN-WHITNEY

    IgG, IgA, and IgM reactivity to B. adolescentis DSM 20086 proteins among IA-positive and IA-negative individuals.

    Journal: Journal of Immunology Research

    Article Title: Antibodies to Lactobacilli and Bifidobacteria in Young Children with Different Propensity to Develop Islet Autoimmunity

    doi: 10.1155/2014/325938

    Figure Lengend Snippet: IgG, IgA, and IgM reactivity to B. adolescentis DSM 20086 proteins among IA-positive and IA-negative individuals.

    Article Snippet: Strips were then incubated with either secondary anti-human IgA, anti-human IgM, or anti-human IgG antibodies labelled with horse-radish peroxidase (HRP) (diluted 1 : 500; Dako, Denmark) for 1 h and subsequently developed in substrate solution comprised of 0.04% carbazole in 50 mM sodium acetate buffer (pH = 5.0) and hydrogen peroxide (0.015%) for 30 min at room temperature.

    Techniques: IA

    IgG, IgA, and IgM reactivity to B. adolescentis DSM 20083 proteins among IA-positive and IA-negative individuals.

    Journal: Journal of Immunology Research

    Article Title: Antibodies to Lactobacilli and Bifidobacteria in Young Children with Different Propensity to Develop Islet Autoimmunity

    doi: 10.1155/2014/325938

    Figure Lengend Snippet: IgG, IgA, and IgM reactivity to B. adolescentis DSM 20083 proteins among IA-positive and IA-negative individuals.

    Article Snippet: Strips were then incubated with either secondary anti-human IgA, anti-human IgM, or anti-human IgG antibodies labelled with horse-radish peroxidase (HRP) (diluted 1 : 500; Dako, Denmark) for 1 h and subsequently developed in substrate solution comprised of 0.04% carbazole in 50 mM sodium acetate buffer (pH = 5.0) and hydrogen peroxide (0.015%) for 30 min at room temperature.

    Techniques: IA

    IgA and IgG reactivity against B. longum DSM 20088 proteins among IA-positive and IA-negative individuals.

    Journal: Journal of Immunology Research

    Article Title: Antibodies to Lactobacilli and Bifidobacteria in Young Children with Different Propensity to Develop Islet Autoimmunity

    doi: 10.1155/2014/325938

    Figure Lengend Snippet: IgA and IgG reactivity against B. longum DSM 20088 proteins among IA-positive and IA-negative individuals.

    Article Snippet: Strips were then incubated with either secondary anti-human IgA, anti-human IgM, or anti-human IgG antibodies labelled with horse-radish peroxidase (HRP) (diluted 1 : 500; Dako, Denmark) for 1 h and subsequently developed in substrate solution comprised of 0.04% carbazole in 50 mM sodium acetate buffer (pH = 5.0) and hydrogen peroxide (0.015%) for 30 min at room temperature.

    Techniques: IA

    LL37, cit-LL37- and LL37-DNA complexes are present in SLE affected tissues. ( A ) Dose response reactivity (expressed as Optical Density, OD) of Mab142 and Mab139, to LL37, cit-LL37 and control peptides (vimentin, VIM, eolase, ENO, vinculin, VINC, scramble LL37, SCR, in their native or citrullinated (citr) forms. ( B ) Number of LL37-positive and cit-LL37 positive spots in CLE and HD dermis assessed by immunohistochemistry. For quantification at least 3 sections for each patients (n = 5) and HD (N = 3) were assessed. Data represent mean ± SE. ( C ) Representative image of immunoistochemistry of the skin of one CLE, upper panels or one HD, lower panels, assessed for expression of native LL37 or cit-LL37. ( D ) Quantification of LL37 and cit-LL37 in 10 SLE-affected kidney biopsies. For quantification at least 3 sections for each patients (n = 10) were assessed. Data represent mean ± SE. ( E ) representative confocal images of staining of SLE kidney biopsies assessed for presence of LL37 or cit-LL37 (magnification 600×). ( F ) Representative confocal images of two out of seven SLE affected renal biopsies showing expression of native or cit-LL37 and DNA filaments (DAPI). ( G ) Confocal images showing expression of LL37, immune-complexes (IgG) and the IFN-induced Mx1. The panels on the left show magnification of two areas to show colocalization (yellow) of IgG staining with LL37 staining. ( H ) Quantification (as percentage) of co-localization between IgG staining and LL37 staining, in SLE renal biopsies from three different patients. For quantification 3 sections for each patient were assessed. Data represent mean ± SE. All biopsies were from lupus nephritis (class IV). Skin biopsies were form CLE patients.

    Journal: Scientific Reports

    Article Title: Native/citrullinated LL37-specific T-cells help autoantibody production in Systemic Lupus Erythematosus

    doi: 10.1038/s41598-020-62480-3

    Figure Lengend Snippet: LL37, cit-LL37- and LL37-DNA complexes are present in SLE affected tissues. ( A ) Dose response reactivity (expressed as Optical Density, OD) of Mab142 and Mab139, to LL37, cit-LL37 and control peptides (vimentin, VIM, eolase, ENO, vinculin, VINC, scramble LL37, SCR, in their native or citrullinated (citr) forms. ( B ) Number of LL37-positive and cit-LL37 positive spots in CLE and HD dermis assessed by immunohistochemistry. For quantification at least 3 sections for each patients (n = 5) and HD (N = 3) were assessed. Data represent mean ± SE. ( C ) Representative image of immunoistochemistry of the skin of one CLE, upper panels or one HD, lower panels, assessed for expression of native LL37 or cit-LL37. ( D ) Quantification of LL37 and cit-LL37 in 10 SLE-affected kidney biopsies. For quantification at least 3 sections for each patients (n = 10) were assessed. Data represent mean ± SE. ( E ) representative confocal images of staining of SLE kidney biopsies assessed for presence of LL37 or cit-LL37 (magnification 600×). ( F ) Representative confocal images of two out of seven SLE affected renal biopsies showing expression of native or cit-LL37 and DNA filaments (DAPI). ( G ) Confocal images showing expression of LL37, immune-complexes (IgG) and the IFN-induced Mx1. The panels on the left show magnification of two areas to show colocalization (yellow) of IgG staining with LL37 staining. ( H ) Quantification (as percentage) of co-localization between IgG staining and LL37 staining, in SLE renal biopsies from three different patients. For quantification 3 sections for each patient were assessed. Data represent mean ± SE. All biopsies were from lupus nephritis (class IV). Skin biopsies were form CLE patients.

    Article Snippet: Briefly, 96-well flat-bottom plates (Non-Binding surface polystyrene, Corning, USA) are coated with 2 μg/mL of native LL37/cit-LL37 or control proteins or human DNA or human RNA or anti-human IgG antibody (Sigma) in carbonate buffer (0.1 M NaHCHO3 , pH 9) for 2 hours (or over night) and washed four times with PBS 0.1% Tween-20.

    Techniques: Immunohistochemistry, Expressing, Staining

    Characteristics of myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells. (a) Expression of CD106 and CD133. After selected with anti-human CD34 Ab-coated magnetic beads cells were further separated with anti-human D7-FIB Ab-coated magnetic beads, and analyzed. (b) Microscopical appearance of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells (×400). May-Giemsa, and immunocytochemical staining of S100, human fibronectin, and human SMA. (c) FISH analysis of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow. BCR-ABL fusion signal is indicated with an arrow. 83 cells are positive in total 100 cells analyzed.

    Journal: Journal of Oncology

    Article Title: Chronic Myelogenous Leukemia Cells Contribute to the Stromal Myofibroblasts in Leukemic NOD/SCID Mouse In Vivo

    doi: 10.1155/2012/901783

    Figure Lengend Snippet: Characteristics of myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells. (a) Expression of CD106 and CD133. After selected with anti-human CD34 Ab-coated magnetic beads cells were further separated with anti-human D7-FIB Ab-coated magnetic beads, and analyzed. (b) Microscopical appearance of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow cells (×400). May-Giemsa, and immunocytochemical staining of S100, human fibronectin, and human SMA. (c) FISH analysis of the separated myofibroblasts from CML cell-engrafted NOD/SCID murine bone marrow. BCR-ABL fusion signal is indicated with an arrow. 83 cells are positive in total 100 cells analyzed.

    Article Snippet: Anti-human CD133 Ab (Miltenyi), CD106 Ab (BD), were employed for the detection of human Fibs and analyzed with Cell Sorter (Beckman Coulter (BC), CA, USA).

    Techniques: Expressing, Magnetic Beads, Staining, Fluorescence In Situ Hybridization

    Analysis of the engrafted CML cells in the transplanted NOD/SCID murine bone marrow. (a) RT-PCR analyses of the indicated cells. Bcr-Abl was analyzed for the detection of fusion molecule; CD13 and CD33, human myeloid markers that are also expressed in the injected CML cells; CD34 and CD133, human stem cell markers that are expressed in the injected CML cells; CD106 and FSP1, human stromal markers that are expressed in human bone marrow adherent cells; GAPDH, RT-PCR control. MW indicates molecular weight marker; BM, bone marrow; CML whole, bone marrow mononuclear cells from CML patient with no processing; Fib, myofibroblasts. (b) Appearance of the spleen from the control NOD/SCID mouse and from human CML cell-engrafted NOD/SCID mouse. (c) CD34 and CD133 expressions of the CML cell-engrafted NOD/SCID murine bone marrow. (d) Expression of CD13 and CD33 after the engrafted NOD/SCID murine bone marrow cells were separated with anti-human CD34 Ab-coated magnetic beads. (e) Morphology of NOD/SCID murine bone marrow cells after engraftment of human CML cells. Cells were stained with May-Giemsa solution (×400, ×1000).

    Journal: Journal of Oncology

    Article Title: Chronic Myelogenous Leukemia Cells Contribute to the Stromal Myofibroblasts in Leukemic NOD/SCID Mouse In Vivo

    doi: 10.1155/2012/901783

    Figure Lengend Snippet: Analysis of the engrafted CML cells in the transplanted NOD/SCID murine bone marrow. (a) RT-PCR analyses of the indicated cells. Bcr-Abl was analyzed for the detection of fusion molecule; CD13 and CD33, human myeloid markers that are also expressed in the injected CML cells; CD34 and CD133, human stem cell markers that are expressed in the injected CML cells; CD106 and FSP1, human stromal markers that are expressed in human bone marrow adherent cells; GAPDH, RT-PCR control. MW indicates molecular weight marker; BM, bone marrow; CML whole, bone marrow mononuclear cells from CML patient with no processing; Fib, myofibroblasts. (b) Appearance of the spleen from the control NOD/SCID mouse and from human CML cell-engrafted NOD/SCID mouse. (c) CD34 and CD133 expressions of the CML cell-engrafted NOD/SCID murine bone marrow. (d) Expression of CD13 and CD33 after the engrafted NOD/SCID murine bone marrow cells were separated with anti-human CD34 Ab-coated magnetic beads. (e) Morphology of NOD/SCID murine bone marrow cells after engraftment of human CML cells. Cells were stained with May-Giemsa solution (×400, ×1000).

    Article Snippet: Anti-human CD133 Ab (Miltenyi), CD106 Ab (BD), were employed for the detection of human Fibs and analyzed with Cell Sorter (Beckman Coulter (BC), CA, USA).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Injection, Molecular Weight, Marker, Expressing, Magnetic Beads, Staining