human actionable solid tumor Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    New England Biolabs direct cancer hotspot panel
    Direct Cancer Hotspot Panel, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/direct cancer hotspot panel/product/New England Biolabs
    Average 99 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    direct cancer hotspot panel - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    Thermo Fisher qubit dsdna high sensitivity assay kit
    Qubit Dsdna High Sensitivity Assay Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1030 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/qubit dsdna high sensitivity assay kit/product/Thermo Fisher
    Average 99 stars, based on 1030 article reviews
    Price from $9.99 to $1999.99
    qubit dsdna high sensitivity assay kit - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    94
    Qiagen human actionable solid tumor
    Human Actionable Solid Tumor, supplied by Qiagen, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human actionable solid tumor/product/Qiagen
    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    human actionable solid tumor - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

    94
    Qiagen human actionable solid tumor panel
    Human Actionable Solid Tumor Panel, supplied by Qiagen, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human actionable solid tumor panel/product/Qiagen
    Average 94 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    human actionable solid tumor panel - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

    94
    Qiagen human actionable solid tumor panel kit
    Human Actionable Solid Tumor Panel Kit, supplied by Qiagen, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human actionable solid tumor panel kit/product/Qiagen
    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    human actionable solid tumor panel kit - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

    86
    Synergys Biotherapeutics solid tumors
    Solid Tumors, supplied by Synergys Biotherapeutics, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/solid tumors/product/Synergys Biotherapeutics
    Average 86 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    solid tumors - by Bioz Stars, 2020-04
    86/100 stars
      Buy from Supplier

    94
    Thermo Fisher ce ivd oncomine solid tumor
    Ce Ivd Oncomine Solid Tumor, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ce ivd oncomine solid tumor/product/Thermo Fisher
    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    ce ivd oncomine solid tumor - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

    95
    Qiagen protocol human actionable solid tumor mutations qiaseq dna panel
    Protocol Human Actionable Solid Tumor Mutations Qiaseq Dna Panel, supplied by Qiagen, used in various techniques. Bioz Stars score: 95/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protocol human actionable solid tumor mutations qiaseq dna panel/product/Qiagen
    Average 95 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    protocol human actionable solid tumor mutations qiaseq dna panel - by Bioz Stars, 2020-04
    95/100 stars
      Buy from Supplier

    95
    Qiagen human comprehensive cancer panel
    Human Comprehensive Cancer Panel, supplied by Qiagen, used in various techniques. Bioz Stars score: 95/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human comprehensive cancer panel/product/Qiagen
    Average 95 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    human comprehensive cancer panel - by Bioz Stars, 2020-04
    95/100 stars
      Buy from Supplier

    94
    Qiagen human comprehensive cancer panel hccp
    Human Comprehensive Cancer Panel Hccp, supplied by Qiagen, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human comprehensive cancer panel hccp/product/Qiagen
    Average 94 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    human comprehensive cancer panel hccp - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

    93
    CEM Corporation human tumor cell lines
    Human Tumor Cell Lines, supplied by CEM Corporation, used in various techniques. Bioz Stars score: 93/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human tumor cell lines/product/CEM Corporation
    Average 93 stars, based on 49 article reviews
    Price from $9.99 to $1999.99
    human tumor cell lines - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    99
    BioLegend recombinant human gm csf
    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in <t>GM-CSF/IL-4</t> for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, <t>IL-1β,</t> and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value
    Recombinant Human Gm Csf, supplied by BioLegend, used in various techniques. Bioz Stars score: 99/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human gm csf/product/BioLegend
    Average 99 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    recombinant human gm csf - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    86
    Neopharm human anti ang 1 2 igg1
    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in <t>GM-CSF/IL-4</t> for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, <t>IL-1β,</t> and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value
    Human Anti Ang 1 2 Igg1, supplied by Neopharm, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human anti ang 1 2 igg1/product/Neopharm
    Average 86 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    human anti ang 1 2 igg1 - by Bioz Stars, 2020-04
    86/100 stars
      Buy from Supplier

    99
    Cell Signaling Technology Inc β actin antibody
    PTL induced apoptosis in MCF-7 and MDA-MB-231 cells. (B) The RIP3-MCF7/231 cells and vector-MCF-7/MDA-MB-231 cells were treated with 12.5 and 25 μmol/L PTL for 48 h, the cellular morphologic changes were observed by phase contrast microscope (×200 magnification). (C) The RIP3-MCF-7/MDA-MB-231 cells and control cells were treated with 25 μmol/L PTL for 24 h and the changes in cellular morphology were observed by fluorescence microscope with Hoechst 3342 staining (×400 magnification). (D) Western blot analysis of lysates from vector or RIP3 transfected MCF-7 and MDA-MB-231cells, followed by treatment with 12.5 μmol/L PTL for 24 h. An antibody recognizing PARP was used with <t>β-actin</t> as a loading control. PTL treatment induced PARP cleavage in RIP3 overexpressing MCF-7 and MDA-MB-231 cells but did not induce PARP cleavage in wild type MCF-7 and MDA-MB-231 cells.
    β Actin Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1585 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β actin antibody/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1585 article reviews
    Price from $9.99 to $1999.99
    β actin antibody - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    Millipore recombinant tumor necrosis factor alpha tnf α
    Effect of IFN-γ and <t>IFN-γ-TNF-α-IL-1β-LPS</t> on the growth of C. trachomatis L2 and C. muridarum MoPn (A and D) and on the expression of iNOS and IDO (B and C) in RT-4 cells. RT-4 cells were untreated or pretreated with IFN-γ
    Recombinant Tumor Necrosis Factor Alpha Tnf α, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant tumor necrosis factor alpha tnf α/product/Millipore
    Average 99 stars, based on 31 article reviews
    Price from $9.99 to $1999.99
    recombinant tumor necrosis factor alpha tnf α - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    Millipore anti β actin monoclonal antibody
    Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. <t>β-Actin</t> was used as the loading control.
    Anti β Actin Monoclonal Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1257 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti β actin monoclonal antibody/product/Millipore
    Average 99 stars, based on 1257 article reviews
    Price from $9.99 to $1999.99
    anti β actin monoclonal antibody - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    Proteintech rabbit polyclonal antibody against α smooth muscle actin α sma
    Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. <t>β-Actin</t> was used as the loading control.
    Rabbit Polyclonal Antibody Against α Smooth Muscle Actin α Sma, supplied by Proteintech, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antibody against α smooth muscle actin α sma/product/Proteintech
    Average 99 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antibody against α smooth muscle actin α sma - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    85
    Genentech humanized anti vegf monoclonal antibody
    Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. <t>β-Actin</t> was used as the loading control.
    Humanized Anti Vegf Monoclonal Antibody, supplied by Genentech, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/humanized anti vegf monoclonal antibody/product/Genentech
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    humanized anti vegf monoclonal antibody - by Bioz Stars, 2020-04
    85/100 stars
      Buy from Supplier

    99
    Millipore protoporphyrin ix disodium salt
    Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. <t>β-Actin</t> was used as the loading control.
    Protoporphyrin Ix Disodium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/protoporphyrin ix disodium salt/product/Millipore
    Average 99 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    protoporphyrin ix disodium salt - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    Millipore mouse tnf α
    Primed neutrophils stimulated with mAbs to MPO, PR3, and human ANCA IgG activate endothelial NF- κ B in cocultures. A typical example for I κ B α immunoblotting and the corresponding ODs (OD as arbitrary units) of the I κ B α bands are provided for (A) lysates obtained from neutrophils stimulated with buffer control (Bu) or primed with 0.1 ng/ml <t>TNF-</t> α and subsequently treated for 60 minutes with Bu, an isotype control (iso), or mAbs to MPO ( α MPO) and PR3 ( α PR3), respectively ( n =4); and (B) lysates obtained from ECs after 2 hours coculture with neutrophils that were treated with Bu or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, iso, or α MPO and α PR3, respectively ( n =8 for conditions shown in lanes 1–5, and n =4 for lanes 6–8). α -Actin served as a loading control. (C and D) OD measurements of the I κ B α bands in lysates from ECs cocultured with neutrophils for 2 hours. (C) Neutrophils were either not primed or primed with 0.1 µ g/ml LPS (black) or 10 −8 M fMLP (gray) as indicated, subsequently incubated with α MPO and α PR3, respectively and added to the EC monolayers ( n =6). (D) Neutrophils were either not primed or primed with TNF- α and subsequently incubated with Bu, human control IgG (huCtrl), MPO-ANCA (huMPO), or PR3-ANCA (huPR3), respectively, and added to the EC monolayers ( n =5). * P
    Mouse Tnf α, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 109 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse tnf α/product/Millipore
    Average 99 stars, based on 109 article reviews
    Price from $9.99 to $1999.99
    mouse tnf α - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    99
    BioLegend tnf α
    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing <t>TNF-α,</t> PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value
    Tnf α, supplied by BioLegend, used in various techniques. Bioz Stars score: 99/100, based on 3059 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tnf α/product/BioLegend
    Average 99 stars, based on 3059 article reviews
    Price from $9.99 to $1999.99
    tnf α - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    98
    IDAC Theranostics it1208
    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing <t>TNF-α,</t> PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value
    It1208, supplied by IDAC Theranostics, used in various techniques. Bioz Stars score: 98/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/it1208/product/IDAC Theranostics
    Average 98 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    it1208 - by Bioz Stars, 2020-04
    98/100 stars
      Buy from Supplier

    93
    CEM Corporation lymphoid
    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing <t>TNF-α,</t> PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value
    Lymphoid, supplied by CEM Corporation, used in various techniques. Bioz Stars score: 93/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lymphoid/product/CEM Corporation
    Average 93 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    lymphoid - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    92
    Immune System Key dtcapfs
    <t>dTCApFs</t> is located in the Golgi apparatus of treated cells. In PANC-1 cells treated with dTCApFs (25 µg/ml) for 72 h, IF staining showed that dTCApFs was localized in/next to the Golgi apparatus. dTCApFs, red; 58 kDa golgi protein, green; DAPI (DNA), blue. Scale bar, 25 µm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; IF, immunofluorescence; DAPI, 4′,6-diamidino-2-phenylindole.
    Dtcapfs, supplied by Immune System Key, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dtcapfs/product/Immune System Key
    Average 92 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    dtcapfs - by Bioz Stars, 2020-04
    92/100 stars
      Buy from Supplier

    99
    Millipore sotalol hydrochloride
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Sotalol Hydrochloride, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sotalol hydrochloride/product/Millipore
    Average 99 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    sotalol hydrochloride - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    93
    ArcherDX archer reveal ctdna 28 kit
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Archer Reveal Ctdna 28 Kit, supplied by ArcherDX, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/archer reveal ctdna 28 kit/product/ArcherDX
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    archer reveal ctdna 28 kit - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    99
    Millipore phorbol myristate acetate pma
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Phorbol Myristate Acetate Pma, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3672 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phorbol myristate acetate pma/product/Millipore
    Average 99 stars, based on 3672 article reviews
    Price from $9.99 to $1999.99
    phorbol myristate acetate pma - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    95
    Nugen ovation custom target enrichment system
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Ovation Custom Target Enrichment System, supplied by Nugen, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ovation custom target enrichment system/product/Nugen
    Average 95 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    ovation custom target enrichment system - by Bioz Stars, 2020-04
    95/100 stars
      Buy from Supplier

    99
    Millipore monoclonal anti acetylated tubulin antibody
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Monoclonal Anti Acetylated Tubulin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2301 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/monoclonal anti acetylated tubulin antibody/product/Millipore
    Average 99 stars, based on 2301 article reviews
    Price from $9.99 to $1999.99
    monoclonal anti acetylated tubulin antibody - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    96
    Novartis everolimus
    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and <t>sotalol</t> hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.
    Everolimus, supplied by Novartis, used in various techniques. Bioz Stars score: 96/100, based on 810 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/everolimus/product/Novartis
    Average 96 stars, based on 810 article reviews
    Price from $9.99 to $1999.99
    everolimus - by Bioz Stars, 2020-04
    96/100 stars
      Buy from Supplier

    Image Search Results


    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value

    Journal: Cellular immunology

    Article Title: Downregulating Galectin-3 Inhibits Proinflammatory Cytokine Production by Human Monocyte-Derived Dendritic Cells

    doi: 10.1016/j.cellimm.2015.01.017

    Figure Lengend Snippet: Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value

    Article Snippet: Recombinant cytokines: recombinant human GM-CSF, IL-1β, IFN-γ, TNF-α (BioLegend, San Diego; PreproTech, Rocky Hill, NJ); recombinant human IL-6, human SCF, human TSLP (PreproTech); PGE2 (Sigma, St Louis, MO); recombinant human Gal-3; ELISA kits for human cytokines : IL-1β, TGF-β, p19 (IL-23), p35 (IL-12), IL-10, IL-17A, and were obtained from eBioscience and PreproTech; anti-actin (Sigma).

    Techniques: Construct, Cell Culture, Incubation, Transfection, Western Blot, Expressing, Quantitative RT-PCR, MANN-WHITNEY

    Differential IL-23 p19 versus IL-12 p35 production in Gal-3 siRNA-treated MoDCs stimulated with TLR/NOD and innate immunity ligands. GM-CSF/IL-4 cultured MoDCs were matured with a full cocktail (TNF-α, PGE2, IL-1β, and IL-6). MoDCs were treated with Gal-3 siRNA-4 or scRNA for 2 h and then stimulated for 48 h with different innate immunity ligands, e.g., LPS (250 ng/ml) and/or R848 (5 µg/ml), Pam3CSK4 (10 µg/ml), MDP (2 µg/ml), zymosan (25 µg/ml), or house dust mites (HDM, 25 µg/ml). Levels of secreted IL-23 p19 (Panel A) and IL-12 p35 (Panel B) were evaluated by ELISAs. Experiments were repeated three times. The results of the representative experiments in triplicates as means+/−SE, and the p value computed.

    Journal: Cellular immunology

    Article Title: Downregulating Galectin-3 Inhibits Proinflammatory Cytokine Production by Human Monocyte-Derived Dendritic Cells

    doi: 10.1016/j.cellimm.2015.01.017

    Figure Lengend Snippet: Differential IL-23 p19 versus IL-12 p35 production in Gal-3 siRNA-treated MoDCs stimulated with TLR/NOD and innate immunity ligands. GM-CSF/IL-4 cultured MoDCs were matured with a full cocktail (TNF-α, PGE2, IL-1β, and IL-6). MoDCs were treated with Gal-3 siRNA-4 or scRNA for 2 h and then stimulated for 48 h with different innate immunity ligands, e.g., LPS (250 ng/ml) and/or R848 (5 µg/ml), Pam3CSK4 (10 µg/ml), MDP (2 µg/ml), zymosan (25 µg/ml), or house dust mites (HDM, 25 µg/ml). Levels of secreted IL-23 p19 (Panel A) and IL-12 p35 (Panel B) were evaluated by ELISAs. Experiments were repeated three times. The results of the representative experiments in triplicates as means+/−SE, and the p value computed.

    Article Snippet: Recombinant cytokines: recombinant human GM-CSF, IL-1β, IFN-γ, TNF-α (BioLegend, San Diego; PreproTech, Rocky Hill, NJ); recombinant human IL-6, human SCF, human TSLP (PreproTech); PGE2 (Sigma, St Louis, MO); recombinant human Gal-3; ELISA kits for human cytokines : IL-1β, TGF-β, p19 (IL-23), p35 (IL-12), IL-10, IL-17A, and were obtained from eBioscience and PreproTech; anti-actin (Sigma).

    Techniques: Cell Culture

    PTL induced apoptosis in MCF-7 and MDA-MB-231 cells. (B) The RIP3-MCF7/231 cells and vector-MCF-7/MDA-MB-231 cells were treated with 12.5 and 25 μmol/L PTL for 48 h, the cellular morphologic changes were observed by phase contrast microscope (×200 magnification). (C) The RIP3-MCF-7/MDA-MB-231 cells and control cells were treated with 25 μmol/L PTL for 24 h and the changes in cellular morphology were observed by fluorescence microscope with Hoechst 3342 staining (×400 magnification). (D) Western blot analysis of lysates from vector or RIP3 transfected MCF-7 and MDA-MB-231cells, followed by treatment with 12.5 μmol/L PTL for 24 h. An antibody recognizing PARP was used with β-actin as a loading control. PTL treatment induced PARP cleavage in RIP3 overexpressing MCF-7 and MDA-MB-231 cells but did not induce PARP cleavage in wild type MCF-7 and MDA-MB-231 cells.

    Journal: Acta Pharmacologica Sinica

    Article Title: RIP3 overexpression sensitizes human breast cancer cells to parthenolide in vitro via intracellular ROS accumulation

    doi: 10.1038/aps.2014.31

    Figure Lengend Snippet: PTL induced apoptosis in MCF-7 and MDA-MB-231 cells. (B) The RIP3-MCF7/231 cells and vector-MCF-7/MDA-MB-231 cells were treated with 12.5 and 25 μmol/L PTL for 48 h, the cellular morphologic changes were observed by phase contrast microscope (×200 magnification). (C) The RIP3-MCF-7/MDA-MB-231 cells and control cells were treated with 25 μmol/L PTL for 24 h and the changes in cellular morphology were observed by fluorescence microscope with Hoechst 3342 staining (×400 magnification). (D) Western blot analysis of lysates from vector or RIP3 transfected MCF-7 and MDA-MB-231cells, followed by treatment with 12.5 μmol/L PTL for 24 h. An antibody recognizing PARP was used with β-actin as a loading control. PTL treatment induced PARP cleavage in RIP3 overexpressing MCF-7 and MDA-MB-231 cells but did not induce PARP cleavage in wild type MCF-7 and MDA-MB-231 cells.

    Article Snippet: The RIP3 antibody was purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA), and the PARP antibody and β-actin antibody were obtained from Cell Signaling Technology (Boston, CA, USA).

    Techniques: Multiple Displacement Amplification, Plasmid Preparation, Microscopy, Fluorescence, Staining, Western Blot, Transfection

    (A) Expression of RIP3 mRNA in different breast cell lines was determined by RT-PCR. Products of RT-PCR were analyzed by agarose gel elecrophoresis. GAPDH was used as internal control. (B) RIP3 mRNA expressions in MCF-7 and MDA-MB-231 cells were detected by RT-PCR. GAPDH was used as internal control. (C) RIP3 protein expressions in MCF-7 and MDA-MB-231 cells were detected by Western blotting. β-Actin was used as loading control. RIP3 mRNA and protein expression considerably increased in RIP3-MCF-7/MDA-MB-231 cells compared with vector-MCF-7/MDA-MB-231 cells. (D) RIP3 expression and cellular distribution were observed by fluorescent microscope. (a) Light microscope (b) fluorescence microscope (×200 magnification).

    Journal: Acta Pharmacologica Sinica

    Article Title: RIP3 overexpression sensitizes human breast cancer cells to parthenolide in vitro via intracellular ROS accumulation

    doi: 10.1038/aps.2014.31

    Figure Lengend Snippet: (A) Expression of RIP3 mRNA in different breast cell lines was determined by RT-PCR. Products of RT-PCR were analyzed by agarose gel elecrophoresis. GAPDH was used as internal control. (B) RIP3 mRNA expressions in MCF-7 and MDA-MB-231 cells were detected by RT-PCR. GAPDH was used as internal control. (C) RIP3 protein expressions in MCF-7 and MDA-MB-231 cells were detected by Western blotting. β-Actin was used as loading control. RIP3 mRNA and protein expression considerably increased in RIP3-MCF-7/MDA-MB-231 cells compared with vector-MCF-7/MDA-MB-231 cells. (D) RIP3 expression and cellular distribution were observed by fluorescent microscope. (a) Light microscope (b) fluorescence microscope (×200 magnification).

    Article Snippet: The RIP3 antibody was purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA), and the PARP antibody and β-actin antibody were obtained from Cell Signaling Technology (Boston, CA, USA).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Agarose Gel Electrophoresis, Multiple Displacement Amplification, Western Blot, Plasmid Preparation, Microscopy, Light Microscopy, Fluorescence

    Effect of IFN-γ and IFN-γ-TNF-α-IL-1β-LPS on the growth of C. trachomatis L2 and C. muridarum MoPn (A and D) and on the expression of iNOS and IDO (B and C) in RT-4 cells. RT-4 cells were untreated or pretreated with IFN-γ

    Journal: Infection and Immunity

    Article Title: Comparison of Gamma Interferon-Mediated Antichlamydial Defense Mechanisms in Human and Mouse Cells

    doi: 10.1128/IAI.74.1.225-238.2006

    Figure Lengend Snippet: Effect of IFN-γ and IFN-γ-TNF-α-IL-1β-LPS on the growth of C. trachomatis L2 and C. muridarum MoPn (A and D) and on the expression of iNOS and IDO (B and C) in RT-4 cells. RT-4 cells were untreated or pretreated with IFN-γ

    Article Snippet: Recombinant human IL-1β, recombinant tumor necrosis factor alpha (TNF-α), the iNOS inhibitor N -monomethyl- l -arginine (NMMA), nitric oxide donor sodium nitroprusside (SNP), arginine, tryptophan, modified Griess reagent, and various tissue culture medium supplements, including recombinant keratinocyte growth factor, β-estradiol, recombinant epidermal growth factor, transferrin, bovine insulin, progesterone, and hydrocortisone, were purchased from Sigma Chemical Co., St. Louis, MO.

    Techniques: Expressing

    Reduction of NF-κB activation when porcine Coro1A was overexpressed. (A) PK-15 cells were co-transfected with the pNF-κB-luc reporter plasmid (0.2 µg), pRL-TK plasmid (0.05 µg), along with 0.6 µg of the expression plasmid encoding porcine Coro1A protein. Selected cells were stimulated by 20 ng/ml TNF-α at 18 h post-transfection, and cell extracts were prepared for the dual-luciferase activity at 6 h after this treatment. *** P

    Journal: PLoS ONE

    Article Title: Porcine Coronin 1A Contributes to Nuclear Factor-Kappa B (NF-κB) Inactivation during Haemophilus parasuis Infection

    doi: 10.1371/journal.pone.0103904

    Figure Lengend Snippet: Reduction of NF-κB activation when porcine Coro1A was overexpressed. (A) PK-15 cells were co-transfected with the pNF-κB-luc reporter plasmid (0.2 µg), pRL-TK plasmid (0.05 µg), along with 0.6 µg of the expression plasmid encoding porcine Coro1A protein. Selected cells were stimulated by 20 ng/ml TNF-α at 18 h post-transfection, and cell extracts were prepared for the dual-luciferase activity at 6 h after this treatment. *** P

    Article Snippet: TNF-α, LPS and poly (I:C) were purchased from Sigma-Aldrich (St.Louis, MO, USA).

    Techniques: Activation Assay, Transfection, Plasmid Preparation, Expressing, Luciferase, Activity Assay

    Western blot analysis of TNF-α, Caspase 3, and Bcl-2 expression in iPS-Mφ and THP-1-Mφ treated with BCG (BCG) for 24 h, untreated iPS-Mφ and THP-1-Mφ were used as controls (Con; upper panel ). TNF-α, Caspase 3, and Bcl-2 were analyzed in whole-cell protein extracts. Actin was used as the loading control. All expression values were normalized against actin as the endogenous control. The results were the average of three independent experiments.*** P

    Journal: Stem Cell Research & Therapy

    Article Title: Human-induced pluripotent stem cell-derived macrophages and their immunological function in response to tuberculosis infection

    doi: 10.1186/s13287-018-0800-x

    Figure Lengend Snippet: Western blot analysis of TNF-α, Caspase 3, and Bcl-2 expression in iPS-Mφ and THP-1-Mφ treated with BCG (BCG) for 24 h, untreated iPS-Mφ and THP-1-Mφ were used as controls (Con; upper panel ). TNF-α, Caspase 3, and Bcl-2 were analyzed in whole-cell protein extracts. Actin was used as the loading control. All expression values were normalized against actin as the endogenous control. The results were the average of three independent experiments.*** P

    Article Snippet: Detailed antibody information is provided below: anti-Actin (Sigma-Aldrich, dilution ratio 1:1000), anti-TNF-α (Sigma-Aldrich, dilution ratio 1:1000), anti-apoptosis-related protein cysteine-3 (Caspase-3) (Sigma-Aldrich, dilution ratio 1:1000), and anti-B-cell lymphoma-2 (Bcl-2) (Sigma-Aldrich, dilution ratio 1:1000).

    Techniques: Western Blot, Expressing

    Effects of BCG on TNF-α expression in iPS-Mφ and THP-1-Mφ. The upper panel shows the standard curve of TNF-α. The expression of TNF-α protein in iPS-Mφ and THP-1-Mφ was significantly increased after BCG treatment ( P

    Journal: Stem Cell Research & Therapy

    Article Title: Human-induced pluripotent stem cell-derived macrophages and their immunological function in response to tuberculosis infection

    doi: 10.1186/s13287-018-0800-x

    Figure Lengend Snippet: Effects of BCG on TNF-α expression in iPS-Mφ and THP-1-Mφ. The upper panel shows the standard curve of TNF-α. The expression of TNF-α protein in iPS-Mφ and THP-1-Mφ was significantly increased after BCG treatment ( P

    Article Snippet: Detailed antibody information is provided below: anti-Actin (Sigma-Aldrich, dilution ratio 1:1000), anti-TNF-α (Sigma-Aldrich, dilution ratio 1:1000), anti-apoptosis-related protein cysteine-3 (Caspase-3) (Sigma-Aldrich, dilution ratio 1:1000), and anti-B-cell lymphoma-2 (Bcl-2) (Sigma-Aldrich, dilution ratio 1:1000).

    Techniques: Expressing

    Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. β-Actin was used as the loading control.

    Journal: Nanomaterials

    Article Title: Fluorescein- and EGFR-Antibody Conjugated Silica Nanoparticles for Enhancement of Real-time Tumor Border Definition Using Confocal Laser Endomicroscopy in Squamous Cell Carcinoma of the Head and Neck

    doi: 10.3390/nano9101378

    Figure Lengend Snippet: Comparison of AF555-EGFR-FITC-SiO 2 -NPs and AF555-EGFR-Ab immunostaining in HNSCCUM-02T and human fibroblasts. ( A ) HNSCCUM-02T cells and primary human fibroblasts were incubated with 100 µg/mL AF555-EGFR-FITC-SiO 2 -NPs or the corresponding amount of AF555-EGFR-Ab for 30 min at 37 °C. Then, the cells were washed, fixed, and embedded in DAPI-containing mounting medium. The nuclei are shown in blue, the FITC-SiO 2 -NPs in green, the AF555-EGFR-Ab in red, and the co-localization in yellow. More AF555-EGFR-FITC-SiO 2 -NPs attached to the cellular membranes of HNSCCUM-02T cells than primary human fibroblasts. The AF555-EGFR-Ab alone did not stain the cells. Thus, FITC-SiO 2 -NPs are required for contrast enhancement and antibody-conjugation improved the specificity. Scale: 20 µm. ( B ) Immunoblot analysis of EGFR expression in HNSCCUM-02T cells and primary human fibroblasts. HNSCCUM-02T cells express much more EGFR than the used primary human fibroblasts. β-Actin was used as the loading control.

    Article Snippet: For the detection of β-actin, the membrane was blocked with 5% dry-milk in TBS-T20 (1 h at RT), washed with TBS-T20 (3 × 5 min), incubated with anti-β-actin monoclonal antibody, clone AC-15 (Sigma-Aldrich, St. Louis, MO, USA) 1:10,000 in 5% BSA in TBS-T20 overnight at 4 °C, washed again thrice, incubated with anti-mouse IgG, HRP-linked antibody (Cell Signaling Technologies Inc, Danvers, MA, USA) 1:5000 in 5% dry-milk in TBS-T20 (1 h, RT) and visualized with Western Lightning® Plus ECL reagent at ChemiDoc™MP Imaging System.

    Techniques: Immunostaining, Incubation, Staining, Conjugation Assay, Expressing

    Primed neutrophils stimulated with mAbs to MPO, PR3, and human ANCA IgG activate endothelial NF- κ B in cocultures. A typical example for I κ B α immunoblotting and the corresponding ODs (OD as arbitrary units) of the I κ B α bands are provided for (A) lysates obtained from neutrophils stimulated with buffer control (Bu) or primed with 0.1 ng/ml TNF- α and subsequently treated for 60 minutes with Bu, an isotype control (iso), or mAbs to MPO ( α MPO) and PR3 ( α PR3), respectively ( n =4); and (B) lysates obtained from ECs after 2 hours coculture with neutrophils that were treated with Bu or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, iso, or α MPO and α PR3, respectively ( n =8 for conditions shown in lanes 1–5, and n =4 for lanes 6–8). α -Actin served as a loading control. (C and D) OD measurements of the I κ B α bands in lysates from ECs cocultured with neutrophils for 2 hours. (C) Neutrophils were either not primed or primed with 0.1 µ g/ml LPS (black) or 10 −8 M fMLP (gray) as indicated, subsequently incubated with α MPO and α PR3, respectively and added to the EC monolayers ( n =6). (D) Neutrophils were either not primed or primed with TNF- α and subsequently incubated with Bu, human control IgG (huCtrl), MPO-ANCA (huMPO), or PR3-ANCA (huPR3), respectively, and added to the EC monolayers ( n =5). * P

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Endothelial NF-κB Blockade Abrogates ANCA-Induced GN

    doi: 10.1681/ASN.2016060690

    Figure Lengend Snippet: Primed neutrophils stimulated with mAbs to MPO, PR3, and human ANCA IgG activate endothelial NF- κ B in cocultures. A typical example for I κ B α immunoblotting and the corresponding ODs (OD as arbitrary units) of the I κ B α bands are provided for (A) lysates obtained from neutrophils stimulated with buffer control (Bu) or primed with 0.1 ng/ml TNF- α and subsequently treated for 60 minutes with Bu, an isotype control (iso), or mAbs to MPO ( α MPO) and PR3 ( α PR3), respectively ( n =4); and (B) lysates obtained from ECs after 2 hours coculture with neutrophils that were treated with Bu or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, iso, or α MPO and α PR3, respectively ( n =8 for conditions shown in lanes 1–5, and n =4 for lanes 6–8). α -Actin served as a loading control. (C and D) OD measurements of the I κ B α bands in lysates from ECs cocultured with neutrophils for 2 hours. (C) Neutrophils were either not primed or primed with 0.1 µ g/ml LPS (black) or 10 −8 M fMLP (gray) as indicated, subsequently incubated with α MPO and α PR3, respectively and added to the EC monolayers ( n =6). (D) Neutrophils were either not primed or primed with TNF- α and subsequently incubated with Bu, human control IgG (huCtrl), MPO-ANCA (huMPO), or PR3-ANCA (huPR3), respectively, and added to the EC monolayers ( n =5). * P

    Article Snippet: Human and mouse TNF- α , LPS (O26:B6), fMLP, the IKK β inhibitor BMS 345541, diphenyleneiodonium, and Ficoll–Hypaque were from Sigma (Deisenhofen, Germany).

    Techniques: Incubation

    Endothelial NF- κ B activation by ANCA-stimulated primed neutrophils does not require direct neutrophil/EC contact and leads to upregulation of IL-8, and increased neutrophil adhesion. (A–D) ECs were incubated with cellfree SN harvested from neutrophils treated for 5 hours with buffer (Bu) or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, an isotype control (iso), or mAbs to MPO ( α MPO) and PR3 ( α PR3), respectively. All samples were analyzed on the same SDS gel and membrane. (A) ECs were incubated with cellfree neutrophil SN for 60 minutes and I κ B α was assessed by immunoblotting. A typical example and the corresponding ODs (OD as arbitrary units) of the I κ B α bands from all experiments are shown ( n =5). α -Actin served as a loading control. (B) ECs were incubated with cellfree neutrophil SN for 6 hours and IL-8 mRNA was assessed by quantitative RT-PCR ( n =5). (C) ECs were incubated with cellfree neutrophil SN for 18 hours and IL-8 protein was assessed in EC SN by ELISA ( n =5). (D) ECs were preincubated with Bu (black) or the specific IKK β inhibitor BMS (gray) for 60 minutes before cellfree neutrophil SN were added. After 18 hours, freshly isolated neutrophils were added, and neutrophil adhesion was determined after 120 minutes ( n =5). * P

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Endothelial NF-κB Blockade Abrogates ANCA-Induced GN

    doi: 10.1681/ASN.2016060690

    Figure Lengend Snippet: Endothelial NF- κ B activation by ANCA-stimulated primed neutrophils does not require direct neutrophil/EC contact and leads to upregulation of IL-8, and increased neutrophil adhesion. (A–D) ECs were incubated with cellfree SN harvested from neutrophils treated for 5 hours with buffer (Bu) or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, an isotype control (iso), or mAbs to MPO ( α MPO) and PR3 ( α PR3), respectively. All samples were analyzed on the same SDS gel and membrane. (A) ECs were incubated with cellfree neutrophil SN for 60 minutes and I κ B α was assessed by immunoblotting. A typical example and the corresponding ODs (OD as arbitrary units) of the I κ B α bands from all experiments are shown ( n =5). α -Actin served as a loading control. (B) ECs were incubated with cellfree neutrophil SN for 6 hours and IL-8 mRNA was assessed by quantitative RT-PCR ( n =5). (C) ECs were incubated with cellfree neutrophil SN for 18 hours and IL-8 protein was assessed in EC SN by ELISA ( n =5). (D) ECs were preincubated with Bu (black) or the specific IKK β inhibitor BMS (gray) for 60 minutes before cellfree neutrophil SN were added. After 18 hours, freshly isolated neutrophils were added, and neutrophil adhesion was determined after 120 minutes ( n =5). * P

    Article Snippet: Human and mouse TNF- α , LPS (O26:B6), fMLP, the IKK β inhibitor BMS 345541, diphenyleneiodonium, and Ficoll–Hypaque were from Sigma (Deisenhofen, Germany).

    Techniques: Activation Assay, Incubation, SDS-Gel, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay, Isolation

    TNF- α released from ANCA-activated primed neutrophils contributes to endothelial NF- κ B activation. (A) ECs were incubated for 60 minutes with cellfree SN harvested from neutrophils treated for 5 hours with buffer (Bu), or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, an isotype control (iso), or mAb to MPO ( α MPO), respectively (lanes 1–3). Microparticles were isolated from these SN, and either the microparticles or the microparticle-free SN were added to the ECs for 60 minutes (lane 4–9). I κ B α was assessed by immunoblotting. A typical example and the corresponding ODs (OD as arbitrary units) of the I κ B α bands from all experiments are shown ( n =3). α -Actin served as a loading control. (B) Neutrophil SN preparation and EC treatment for samples in lane 1–3 was as described in (A). When indicated, SN were heat-inactivated or generated from 10 μ M DPI-treated neutrophils ( n =3). (C) Neutrophil SN preparation and EC treatment for samples in lane 1–3 were as described in (A). When indicated, SN were treated for 60 minutes with control IgG (IgG) or neutralizing antibodies for TNF- α ( α TNF, left panel) or IL-8 ( α IL-8, right panel). Note, fMLP was used as the priming agent in these experiments ( n =4). * P

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Endothelial NF-κB Blockade Abrogates ANCA-Induced GN

    doi: 10.1681/ASN.2016060690

    Figure Lengend Snippet: TNF- α released from ANCA-activated primed neutrophils contributes to endothelial NF- κ B activation. (A) ECs were incubated for 60 minutes with cellfree SN harvested from neutrophils treated for 5 hours with buffer (Bu), or primed with 0.1 ng/ml TNF- α and subsequently incubated with Bu, an isotype control (iso), or mAb to MPO ( α MPO), respectively (lanes 1–3). Microparticles were isolated from these SN, and either the microparticles or the microparticle-free SN were added to the ECs for 60 minutes (lane 4–9). I κ B α was assessed by immunoblotting. A typical example and the corresponding ODs (OD as arbitrary units) of the I κ B α bands from all experiments are shown ( n =3). α -Actin served as a loading control. (B) Neutrophil SN preparation and EC treatment for samples in lane 1–3 was as described in (A). When indicated, SN were heat-inactivated or generated from 10 μ M DPI-treated neutrophils ( n =3). (C) Neutrophil SN preparation and EC treatment for samples in lane 1–3 were as described in (A). When indicated, SN were treated for 60 minutes with control IgG (IgG) or neutralizing antibodies for TNF- α ( α TNF, left panel) or IL-8 ( α IL-8, right panel). Note, fMLP was used as the priming agent in these experiments ( n =4). * P

    Article Snippet: Human and mouse TNF- α , LPS (O26:B6), fMLP, the IKK β inhibitor BMS 345541, diphenyleneiodonium, and Ficoll–Hypaque were from Sigma (Deisenhofen, Germany).

    Techniques: Activation Assay, Incubation, Isolation, Generated

    NF- κ B activity correlates with glomerular crescent formation in mice with anti-MPO antibody-induced NCGN. (A and B) Nuclear kidney extracts from untreated ( n =6) or bortezomib (BTZ)-treated mice ( n =22) in which we had induced NCGN using an anti-MPO antibody disease model were analyzed by EMSA. (A) Examples from a BTZ-treated mouse with 0% crescent formation (BTZ 0%) and an untreated mouse with 35% crescents (no 35%) are shown. Using the latter sample, we performed competition with a cold probe (comp) and supershift experiments using antibodies to p50, p65, c-Rel, and RelB as indicated. Note that longer exposure was needed to detect the p65 shift (p65*). (B) OD of the p50/p65 heterodimer was assessed in each sample using arbitrary units, and plotted against the percentage of glomerular crescents ( n =28, correlation coefficient R 2 =0.65). (C) mRNA was prepared from the kidney of each mouse shown in (B), TNF- α mRNA expression was analyzed by quantitative RT-PCR and plotted against the percentage of glomerular crescents ( n =28, correlation coefficient R 2 =0.77). (D) OD of the p50/p65 heterodimer was assessed in samples from NCGN mice that had not received active treatments and plotted against the percentage of glomerular crescents ( n =14, correlation coefficient R 2 =0.60). The insert shows significantly less NF- κ B activity in mice with

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Endothelial NF-κB Blockade Abrogates ANCA-Induced GN

    doi: 10.1681/ASN.2016060690

    Figure Lengend Snippet: NF- κ B activity correlates with glomerular crescent formation in mice with anti-MPO antibody-induced NCGN. (A and B) Nuclear kidney extracts from untreated ( n =6) or bortezomib (BTZ)-treated mice ( n =22) in which we had induced NCGN using an anti-MPO antibody disease model were analyzed by EMSA. (A) Examples from a BTZ-treated mouse with 0% crescent formation (BTZ 0%) and an untreated mouse with 35% crescents (no 35%) are shown. Using the latter sample, we performed competition with a cold probe (comp) and supershift experiments using antibodies to p50, p65, c-Rel, and RelB as indicated. Note that longer exposure was needed to detect the p65 shift (p65*). (B) OD of the p50/p65 heterodimer was assessed in each sample using arbitrary units, and plotted against the percentage of glomerular crescents ( n =28, correlation coefficient R 2 =0.65). (C) mRNA was prepared from the kidney of each mouse shown in (B), TNF- α mRNA expression was analyzed by quantitative RT-PCR and plotted against the percentage of glomerular crescents ( n =28, correlation coefficient R 2 =0.77). (D) OD of the p50/p65 heterodimer was assessed in samples from NCGN mice that had not received active treatments and plotted against the percentage of glomerular crescents ( n =14, correlation coefficient R 2 =0.60). The insert shows significantly less NF- κ B activity in mice with

    Article Snippet: Human and mouse TNF- α , LPS (O26:B6), fMLP, the IKK β inhibitor BMS 345541, diphenyleneiodonium, and Ficoll–Hypaque were from Sigma (Deisenhofen, Germany).

    Techniques: Activity Assay, Mouse Assay, Expressing, Quantitative RT-PCR

    Preemptive SOS p65 siRNA treatment of mice inhibited glomerular NF- κ B activation by EMSA and NF- κ B–dependent TNF- α mRNA expression by quantitative RT-PCR that correlated with crescent formation. (A) Glomeruli were prepared from two control-treated (SOS ctrl) and two SOS p65 siRNA-treated (SOS siRNA) mice and NF- κ B was assessed by EMSA. (B) Nuclear kidney extracts from SOS ctrl (black, n =5) and SOS siRNA (gray, n =5) mice were subjected to EMSA and the OD of the p50/65 heterodimer was assessed. (C) mRNA was prepared from the kidney of each mouse shown in (B), TNF- α mRNA expression was determined by qRT-PCR and plotted against the percentage of crescents. (D) Costaining using fluorescence-labeled antibodies to the EC marker CD31 (red), phospho-p65 (green), and DAPI staining for nuclei (blue) was performed in renal tissue from SOS ctrl– and SOS siRNA–treated mice. A typical microscopy example (original magnification, ×40) together with the corresponding quantitative assessment of nuclear phospho-p65 staining within CD31-positive glomerular ECs using Image J is depicted. ** P

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Endothelial NF-κB Blockade Abrogates ANCA-Induced GN

    doi: 10.1681/ASN.2016060690

    Figure Lengend Snippet: Preemptive SOS p65 siRNA treatment of mice inhibited glomerular NF- κ B activation by EMSA and NF- κ B–dependent TNF- α mRNA expression by quantitative RT-PCR that correlated with crescent formation. (A) Glomeruli were prepared from two control-treated (SOS ctrl) and two SOS p65 siRNA-treated (SOS siRNA) mice and NF- κ B was assessed by EMSA. (B) Nuclear kidney extracts from SOS ctrl (black, n =5) and SOS siRNA (gray, n =5) mice were subjected to EMSA and the OD of the p50/65 heterodimer was assessed. (C) mRNA was prepared from the kidney of each mouse shown in (B), TNF- α mRNA expression was determined by qRT-PCR and plotted against the percentage of crescents. (D) Costaining using fluorescence-labeled antibodies to the EC marker CD31 (red), phospho-p65 (green), and DAPI staining for nuclei (blue) was performed in renal tissue from SOS ctrl– and SOS siRNA–treated mice. A typical microscopy example (original magnification, ×40) together with the corresponding quantitative assessment of nuclear phospho-p65 staining within CD31-positive glomerular ECs using Image J is depicted. ** P

    Article Snippet: Human and mouse TNF- α , LPS (O26:B6), fMLP, the IKK β inhibitor BMS 345541, diphenyleneiodonium, and Ficoll–Hypaque were from Sigma (Deisenhofen, Germany).

    Techniques: Mouse Assay, Activation Assay, Expressing, Quantitative RT-PCR, Fluorescence, Labeling, Marker, Staining, Microscopy

    Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value

    Journal: Cellular immunology

    Article Title: Downregulating Galectin-3 Inhibits Proinflammatory Cytokine Production by Human Monocyte-Derived Dendritic Cells

    doi: 10.1016/j.cellimm.2015.01.017

    Figure Lengend Snippet: Gal-3 knockdown in MoDCs by four Gal-3 siRNA constructs. Adherent monocytes from PBMC were cultured in GM-CSF/IL-4 for 7 days, and then incubated in maturation cocktail containing TNF-α, PGE2, IL-1β, and IL-6 for 24 h. MoDCs were transfected at 1 nmol with 4 respective siRNAs targeting Gal-3 or with a non-targeting scramble control RNA (scRNA) in lipofectamine for 2 h, washed and then incubated in media for 72 h. Western blot was then performed in Gal-3 siRNA-transfected MoDCs. The experiment was independently confirmed ( A ). Gal-3 expression siRNA-4 transfected MoDCs stimulated with LPS (250 ng/ml) and/or R848 (5 µg/ml) for 72 h was evaluated by qRT-PCR with arbitrary units or fold against endogenous actin. Experiments were repeated three times from different donors with consistent results. The results of the representative experiments in triplicate determination as means and SE. The p value was computed with a Mann-Whitney U test with a p value

    Article Snippet: Recombinant cytokines: recombinant human GM-CSF, IL-1β, IFN-γ, TNF-α (BioLegend, San Diego; PreproTech, Rocky Hill, NJ); recombinant human IL-6, human SCF, human TSLP (PreproTech); PGE2 (Sigma, St Louis, MO); recombinant human Gal-3; ELISA kits for human cytokines : IL-1β, TGF-β, p19 (IL-23), p35 (IL-12), IL-10, IL-17A, and were obtained from eBioscience and PreproTech; anti-actin (Sigma).

    Techniques: Construct, Cell Culture, Incubation, Transfection, Western Blot, Expressing, Quantitative RT-PCR, MANN-WHITNEY

    Production of IL-1β, IL-6, TGF-β and IL-10 in Gal-3 siRNA-treated MoDCs. MoDCs, matured in TNF-α/PGE2 were treated with 1 nmol Gal-3 siRNA-4 or scRNA for 2 h, and then stimulated for 48 h with LPS (250 ng/ml) and/or R848 (5 µg/ml). Levels of cytokines that were secreted in the supernatants, were evaluated by ELISAs (Panel A-D). Experiments were repeated three times from different donors. The results of the representative experiments in triplicates as means+/−SE and the p value computed.

    Journal: Cellular immunology

    Article Title: Downregulating Galectin-3 Inhibits Proinflammatory Cytokine Production by Human Monocyte-Derived Dendritic Cells

    doi: 10.1016/j.cellimm.2015.01.017

    Figure Lengend Snippet: Production of IL-1β, IL-6, TGF-β and IL-10 in Gal-3 siRNA-treated MoDCs. MoDCs, matured in TNF-α/PGE2 were treated with 1 nmol Gal-3 siRNA-4 or scRNA for 2 h, and then stimulated for 48 h with LPS (250 ng/ml) and/or R848 (5 µg/ml). Levels of cytokines that were secreted in the supernatants, were evaluated by ELISAs (Panel A-D). Experiments were repeated three times from different donors. The results of the representative experiments in triplicates as means+/−SE and the p value computed.

    Article Snippet: Recombinant cytokines: recombinant human GM-CSF, IL-1β, IFN-γ, TNF-α (BioLegend, San Diego; PreproTech, Rocky Hill, NJ); recombinant human IL-6, human SCF, human TSLP (PreproTech); PGE2 (Sigma, St Louis, MO); recombinant human Gal-3; ELISA kits for human cytokines : IL-1β, TGF-β, p19 (IL-23), p35 (IL-12), IL-10, IL-17A, and were obtained from eBioscience and PreproTech; anti-actin (Sigma).

    Techniques:

    dTCApFs is located in the Golgi apparatus of treated cells. In PANC-1 cells treated with dTCApFs (25 µg/ml) for 72 h, IF staining showed that dTCApFs was localized in/next to the Golgi apparatus. dTCApFs, red; 58 kDa golgi protein, green; DAPI (DNA), blue. Scale bar, 25 µm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; IF, immunofluorescence; DAPI, 4′,6-diamidino-2-phenylindole.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: dTCApFs is located in the Golgi apparatus of treated cells. In PANC-1 cells treated with dTCApFs (25 µg/ml) for 72 h, IF staining showed that dTCApFs was localized in/next to the Golgi apparatus. dTCApFs, red; 58 kDa golgi protein, green; DAPI (DNA), blue. Scale bar, 25 µm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; IF, immunofluorescence; DAPI, 4′,6-diamidino-2-phenylindole.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Staining, Immunofluorescence

    PANC-1 xenograft murine model studies showing that dTCApFs causes a structural change in the ER/Golgi, ER stress, and decreased tumor size. (A) IHC staining using anti-β COP antibody (ER marker) or anti-γ-adaptin (Golgi marker) of tumor sections from untreated and dTCApFs-treated PANC-1 xenograft mice model demonstrating diffused ER/Golgi with dTCApFs treatment. Scale bar, 12 µm. (B) IHC staining with anti-pIER1 or anti-BiP of tumor sections from untreated and dTCApFs-treated PANC-1 murine xenograft model demonstrating increase in the number of cells expressing these ER stress markers. Scale bar, 50 µm. (C) Tumor size over time in PANC-1 mouse xenograft model that were dTCApFs-treated (15 mg/kg intraperitoneally twice a week) vs. controls (treatment with 5% mannitol). Eight nude mice were inoculated subcutaneously with 1 million PANC-1 cells. When the tumor size exceeded 64 mm 3 , the animals were randomly assigned to treatment vs. control and tumor size was measured over time. Each line represents one animal in the experiment. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; IHC, immunohistochemistry; β-COP, coatomer subunit β; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: PANC-1 xenograft murine model studies showing that dTCApFs causes a structural change in the ER/Golgi, ER stress, and decreased tumor size. (A) IHC staining using anti-β COP antibody (ER marker) or anti-γ-adaptin (Golgi marker) of tumor sections from untreated and dTCApFs-treated PANC-1 xenograft mice model demonstrating diffused ER/Golgi with dTCApFs treatment. Scale bar, 12 µm. (B) IHC staining with anti-pIER1 or anti-BiP of tumor sections from untreated and dTCApFs-treated PANC-1 murine xenograft model demonstrating increase in the number of cells expressing these ER stress markers. Scale bar, 50 µm. (C) Tumor size over time in PANC-1 mouse xenograft model that were dTCApFs-treated (15 mg/kg intraperitoneally twice a week) vs. controls (treatment with 5% mannitol). Eight nude mice were inoculated subcutaneously with 1 million PANC-1 cells. When the tumor size exceeded 64 mm 3 , the animals were randomly assigned to treatment vs. control and tumor size was measured over time. Each line represents one animal in the experiment. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; IHC, immunohistochemistry; β-COP, coatomer subunit β; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Immunohistochemistry, Staining, Marker, Mouse Assay, Expressing, Binding Assay

    Long-term exposure to dTCApFs downregulates the ER stress repair mechanism and as a result apoptosis is induced. In treated cells, the sXBP1 and GAAP levels decreased. Cell viability also decreased. (A) RT-PCR-detected sXBP1 levels in OV-90, PANC-1 and MDA-MB-23 cells treated with dTCApFs for 72 h decreased with increasing dTCApFs concentrations (equal amounts of RNA/cDNA were used in the analysis). (B) The GAAP levels were higher in dTCApFs-treated PANC-1 cells (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h) compared with untreated cells (IF staining). Scale bar, 25 µm. (C) Apoptosis was observed in PANC-1, OV-90 and MDA-MB-231 cells treated with increasing concentrations of dTCApFs for 24 h followed by another dTCApFs dose for 72 h. Viability was measured with the Annexin V FITC assay. Error bars, standard deviation. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; RT-PCR, reverse transcription-polymerase chain reaction; sXBP1, spliced X-box-binding protein 1; GAAP, Golgi anti-apoptotic protein; IF, immunofluorescence.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: Long-term exposure to dTCApFs downregulates the ER stress repair mechanism and as a result apoptosis is induced. In treated cells, the sXBP1 and GAAP levels decreased. Cell viability also decreased. (A) RT-PCR-detected sXBP1 levels in OV-90, PANC-1 and MDA-MB-23 cells treated with dTCApFs for 72 h decreased with increasing dTCApFs concentrations (equal amounts of RNA/cDNA were used in the analysis). (B) The GAAP levels were higher in dTCApFs-treated PANC-1 cells (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h) compared with untreated cells (IF staining). Scale bar, 25 µm. (C) Apoptosis was observed in PANC-1, OV-90 and MDA-MB-231 cells treated with increasing concentrations of dTCApFs for 24 h followed by another dTCApFs dose for 72 h. Viability was measured with the Annexin V FITC assay. Error bars, standard deviation. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; RT-PCR, reverse transcription-polymerase chain reaction; sXBP1, spliced X-box-binding protein 1; GAAP, Golgi anti-apoptotic protein; IF, immunofluorescence.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Multiple Displacement Amplification, Staining, Standard Deviation, Binding Assay, Immunofluorescence

    The dTCApFs-induced structural change in the Golgi apparatus results in loss of Golgi function and ER stress, In treated cells, the cellular levels of proteins (soluble T1/ST2) remain the same, whereas their secretion from the cells decreases, and molecular effects associated with ER stress are observed. (A) The soluble T1/ST2 levels were similar between untreated and treated (dTCApFs 50 µg/ml for 24 h) PANC-1 cells (IF staining). Soluble T1/ST2; red; DAPI (DNA), blue. Scale bar, 25 µm. (B) Soluble T1/ST2 levels in the supernatant of cells treated with dTCApFs for 24 h followed by another dose for 72 h, decreased with increasing concentrations of dTCApFs (ELISA). (C-E) IF/IHC staining of untreated and treated cells. For PANC-1 cells, treatment involved incubation with dTCApFs 50 µg/ml for 48 h, followed by an additional dose of 50 µg/ml for 24 h. For the OV-90 and MDA-MB-231 cell lines, the dTCApFs concentration was 25 µg/ml. The cells exhibited increased levels of (C) CHOP, (D) BiP and (E) pIRE1 in the cytoplasm and (F) e1F2a phosphorylation with dTCApFs treatment. (G) The Golgi apparatus became diffused in OV-90 cells treated with dTCApFs (50 µg/ml for 24 h followed by an additional dose of 50 µg/ml for 72 h) compared with controls. Treatment with PBA (5 µM for 48 h) did not affect the Golgi apparatus, and treatment with both dTCApFs and PBA (in the concentrations described above) attenuated the effect of dTCApFs. Scale bars, 25 µm. (H) PANC-1, OV-90 and MDA-MB-231 cells were treated with dTCApFs (50 µg/ml) overnight, after which ROS levels were determined using the DHE assay and compared to untreated cells (controls). Treatment with dTCApFs (50 µg/ml) plus 5 µM PBA attenuated the observed ROS increase. Experiments were performed in triplicate. Error bars represent standard deviation (SD). (I) NF-κB and pNF-κB levels increased with dTCApFs treatment. OV-90, and the MDA-MB-231 cells were treated with dTCApFs (50 µg/ml) for the times indicated (for control, cells were incubated with 5% mannitol for 24 h) and cell lysates were subjected to western blot analysis. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; CHOP, C/EBP homologous protein; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1; eIF2α, eukaryotic translation initiation factor 2α; PBA, 4-phenylbutyrate; DHE, dihydroethidium; ER, endoplasmic reticulum; DAPI, 4′,6-diamidino-2-phenylindole; β-COP, coatomer subunit β; IF, immunofluorescence; IHC, immunohistochemistry; ROS, reactive oxygen species; NF-κB, nuclear factor-κB.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: The dTCApFs-induced structural change in the Golgi apparatus results in loss of Golgi function and ER stress, In treated cells, the cellular levels of proteins (soluble T1/ST2) remain the same, whereas their secretion from the cells decreases, and molecular effects associated with ER stress are observed. (A) The soluble T1/ST2 levels were similar between untreated and treated (dTCApFs 50 µg/ml for 24 h) PANC-1 cells (IF staining). Soluble T1/ST2; red; DAPI (DNA), blue. Scale bar, 25 µm. (B) Soluble T1/ST2 levels in the supernatant of cells treated with dTCApFs for 24 h followed by another dose for 72 h, decreased with increasing concentrations of dTCApFs (ELISA). (C-E) IF/IHC staining of untreated and treated cells. For PANC-1 cells, treatment involved incubation with dTCApFs 50 µg/ml for 48 h, followed by an additional dose of 50 µg/ml for 24 h. For the OV-90 and MDA-MB-231 cell lines, the dTCApFs concentration was 25 µg/ml. The cells exhibited increased levels of (C) CHOP, (D) BiP and (E) pIRE1 in the cytoplasm and (F) e1F2a phosphorylation with dTCApFs treatment. (G) The Golgi apparatus became diffused in OV-90 cells treated with dTCApFs (50 µg/ml for 24 h followed by an additional dose of 50 µg/ml for 72 h) compared with controls. Treatment with PBA (5 µM for 48 h) did not affect the Golgi apparatus, and treatment with both dTCApFs and PBA (in the concentrations described above) attenuated the effect of dTCApFs. Scale bars, 25 µm. (H) PANC-1, OV-90 and MDA-MB-231 cells were treated with dTCApFs (50 µg/ml) overnight, after which ROS levels were determined using the DHE assay and compared to untreated cells (controls). Treatment with dTCApFs (50 µg/ml) plus 5 µM PBA attenuated the observed ROS increase. Experiments were performed in triplicate. Error bars represent standard deviation (SD). (I) NF-κB and pNF-κB levels increased with dTCApFs treatment. OV-90, and the MDA-MB-231 cells were treated with dTCApFs (50 µg/ml) for the times indicated (for control, cells were incubated with 5% mannitol for 24 h) and cell lysates were subjected to western blot analysis. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; CHOP, C/EBP homologous protein; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1; eIF2α, eukaryotic translation initiation factor 2α; PBA, 4-phenylbutyrate; DHE, dihydroethidium; ER, endoplasmic reticulum; DAPI, 4′,6-diamidino-2-phenylindole; β-COP, coatomer subunit β; IF, immunofluorescence; IHC, immunohistochemistry; ROS, reactive oxygen species; NF-κB, nuclear factor-κB.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Staining, Enzyme-linked Immunosorbent Assay, Immunohistochemistry, Incubation, Multiple Displacement Amplification, Concentration Assay, Standard Deviation, Western Blot, Binding Assay, Immunofluorescence

    dTCApFs-induced ER stress in tumor samples from a patient treated with dTCApFs. IHC-stained samples pre- and post-treatment from a patient with spinal cord neoplasm who received dTCApFs 3 times a week at increasing concentrations of 12, 24, and 48 mg/m 2 for 11 months showing an increase in the number of cells expressing pIRE1 and BiP. Scale bars, 50 µm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; IHC, immunohistochemistry; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: dTCApFs-induced ER stress in tumor samples from a patient treated with dTCApFs. IHC-stained samples pre- and post-treatment from a patient with spinal cord neoplasm who received dTCApFs 3 times a week at increasing concentrations of 12, 24, and 48 mg/m 2 for 11 months showing an increase in the number of cells expressing pIRE1 and BiP. Scale bars, 50 µm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; IHC, immunohistochemistry; BiP, binding immunoglobulin protein; pIRE1, phosphorylated inositol-requiring enzyme 1.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Immunohistochemistry, Staining, Expressing, Binding Assay

    Schematic model of the mechanism of action of dTCApFs. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; sXBP1, spliced X-box-binding protein 1.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: Schematic model of the mechanism of action of dTCApFs. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; sXBP1, spliced X-box-binding protein 1.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Binding Assay

    dTCApFs causes a structural change in the Golgi apparatus, in untreated cells, soluble T1/ST2 is in the ER/Golgi, whereas in dTCApFs-treated cells it is in the nucleus, and the Golgi apparatus is diffused and separated from the ER. (A) Soluble T1/ST2 was detected in the ER of untreated PANC-1 cells (IF staining). Soluble T1/ST2, red; DAPI (DNA), blue, β-COP (ER marker), green. (B) Soluble T1/ST2 was detected in the Golgi apparatus of untreated PANC-1 cells (IF staining). Soluble T1/ST2, red; DAPI (DNA), blue; 58 kDa Golgi protein, green. (C) Soluble T1/ST2 was detected (IF staining) only in the nucleus of PANC-1 cells treated with dTCApFs (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h). Soluble T1/ST2, red; DAPI (DNA), blue; γ-adaptin (a Golgi marker), green. (D) In MDA-MB-231 cells treated with dTCApFs (25 or 50 µg/ml for 24 h followed by an additional dose of 25 or 50 µg/ml for a further 72 h), the Golgi apparatus structure was diffused, compared with controls (no dTCApFs treatment). DAPI (DNA), blue; 58 kDa Golgi protein, green. (E) In PANC-1 cells treated with dTCApFs (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h), the Golgi apparatus structure was separated from the ER. DAPI (DNA), blue; γ-adaptin (a Golgi marker), red; β-COP (ER marker), green. Scale bars in all the panels, 25 μm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; DAPI, 4′,6-diamidino-2-phenylindole; β-COP, coatomer subunit β; IF, immunofluorescence.

    Journal: Molecular and Clinical Oncology

    Article Title: dTCApFs, a derivative of a novel human hormone peptide, induces apoptosis in cancer cells through a mechanism involving loss of Golgi function

    doi: 10.3892/mco.2017.1453

    Figure Lengend Snippet: dTCApFs causes a structural change in the Golgi apparatus, in untreated cells, soluble T1/ST2 is in the ER/Golgi, whereas in dTCApFs-treated cells it is in the nucleus, and the Golgi apparatus is diffused and separated from the ER. (A) Soluble T1/ST2 was detected in the ER of untreated PANC-1 cells (IF staining). Soluble T1/ST2, red; DAPI (DNA), blue, β-COP (ER marker), green. (B) Soluble T1/ST2 was detected in the Golgi apparatus of untreated PANC-1 cells (IF staining). Soluble T1/ST2, red; DAPI (DNA), blue; 58 kDa Golgi protein, green. (C) Soluble T1/ST2 was detected (IF staining) only in the nucleus of PANC-1 cells treated with dTCApFs (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h). Soluble T1/ST2, red; DAPI (DNA), blue; γ-adaptin (a Golgi marker), green. (D) In MDA-MB-231 cells treated with dTCApFs (25 or 50 µg/ml for 24 h followed by an additional dose of 25 or 50 µg/ml for a further 72 h), the Golgi apparatus structure was diffused, compared with controls (no dTCApFs treatment). DAPI (DNA), blue; 58 kDa Golgi protein, green. (E) In PANC-1 cells treated with dTCApFs (25 µg/ml for 48 h followed by an additional dose of 25 µg/ml for a further 24 h), the Golgi apparatus structure was separated from the ER. DAPI (DNA), blue; γ-adaptin (a Golgi marker), red; β-COP (ER marker), green. Scale bars in all the panels, 25 μm. dTCApFs, 14-amino acid derivative of tumor-cells apoptosis factor; ER, endoplasmic reticulum; DAPI, 4′,6-diamidino-2-phenylindole; β-COP, coatomer subunit β; IF, immunofluorescence.

    Article Snippet: The activation of the T1/ST2 receptor has been shown to lead to apoptosis in proliferating cells (but not in non-proliferating cells) through activation of caspases 8 and B-cell lymphoma (Bcl)-2-mediated apoptotic pathways ( ). dTCApFs (Nerofe™, Immune System Key Ltd., Jerusalem, Israel) is a short, 14-amino acid derivative of TCApF that retains its anticancer activity.

    Techniques: Staining, Marker, Multiple Displacement Amplification, Immunofluorescence

    Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: Capture-SELEX: Selection of DNA Aptamers for Aminoglycoside Antibiotics

    doi: 10.1155/2012/415697

    Figure Lengend Snippet: Groups and orphans of oligonucleotides (5′ → 3′) obtained after cloning and sequencing of the single stranded DNA that was selected by the target mixture (kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride, each 1 mM in selection buffer) during 13 Capture-SELEX rounds. The representative of each group is printed in red. Each group could be divided into subgroups of totally identical sequences. The number of sequences in each subgroup is given (qty), and the representative is printed in black. Green: binding site for primer AP60 (18mer), magenta: docking sequence, originally: TGAGGCTCGATC, blue: binding site for primer AP20 (18mer), yellow marking: sites of base exchange or deletion, and underlined: possible G-quadruplex area.

    Article Snippet: Kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride were purchased from Sigma-Aldrich (Germany).

    Techniques: Clone Assay, Sequencing, Selection, Binding Assay

    Enrichment of fluorescein-labeled aptamers during 13 rounds of Capture-SELEX for the target mixture consisting of kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride, each 1 mM in selection buffer. Amounts of eluted single stranded DNA (ssDNA) in the target binding step (dark red) and in the background elution step (blue) are shown. As the starting oligonucleotide library initially was not fluorescein labeled, there are no bars for round 1.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: Capture-SELEX: Selection of DNA Aptamers for Aminoglycoside Antibiotics

    doi: 10.1155/2012/415697

    Figure Lengend Snippet: Enrichment of fluorescein-labeled aptamers during 13 rounds of Capture-SELEX for the target mixture consisting of kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride, each 1 mM in selection buffer. Amounts of eluted single stranded DNA (ssDNA) in the target binding step (dark red) and in the background elution step (blue) are shown. As the starting oligonucleotide library initially was not fluorescein labeled, there are no bars for round 1.

    Article Snippet: Kanamycin A disulfate salt dihydrate, sulfacarbamide, sulfamethoxazole, and sotalol hydrochloride were purchased from Sigma-Aldrich (Germany).

    Techniques: Labeling, Selection, Binding Assay