fascin  (Millipore)


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    Name:
    Fascin 55k 2 Mouse Monoclonal Antibody
    Description:
    Anti fascin is a very sensitive marker for Reed Sternberg cells and variants in nodular sclerosis mixed cellularity and lymphocyte depletion Hodgkin disease It is uniformly negative in lymphoid cells plasma cells and myeloid cells Anti fascin is positive in dendritic cells This marker may be helpful to distinguish between Hodgkin lymphoma and non Hodgkin lymphoma in difficult cases Also the lack of expression of fascin in the neoplastic follicles in follicular lymphoma can be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased
    Catalog Number:
    252m-1
    Price:
    None
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    Structured Review

    Millipore fascin
    Fascin 55k 2 Mouse Monoclonal Antibody
    Anti fascin is a very sensitive marker for Reed Sternberg cells and variants in nodular sclerosis mixed cellularity and lymphocyte depletion Hodgkin disease It is uniformly negative in lymphoid cells plasma cells and myeloid cells Anti fascin is positive in dendritic cells This marker may be helpful to distinguish between Hodgkin lymphoma and non Hodgkin lymphoma in difficult cases Also the lack of expression of fascin in the neoplastic follicles in follicular lymphoma can be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased
    https://www.bioz.com/result/fascin/product/Millipore
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fascin - by Bioz Stars, 2020-07
    94/100 stars

    Images

    1) Product Images from "Coordinated Regulation of Intracellular Fascin Distribution Governs Tumor Microvesicle Release and Invasive Cell Capacity"

    Article Title: Coordinated Regulation of Intracellular Fascin Distribution Governs Tumor Microvesicle Release and Invasive Cell Capacity

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.00264-18

    Loss of Rab35 alters intracellular fascin localization. (A) Parental LOX cells plated on unlabeled gelatin were fixed, stained, and analyzed by confocal microscopy to examine the localization of endogenous fascin at the invasive, ventral surfaces of the cells. (B) Fascin localization and cortactin localization were examined together in cells transiently expressing mEmerald-fascin on unlabeled gelatin. Colocalization of both markers is indicative of localization of both components to invadopodia. (C) Invadopodium-mediated degradation, together with the intracellular distribution of endogenous fascin or cortactin, was examined in mesenchymal LOX cells transfected with myc–Rab35-Q67L. Matrix degradation appears as dark spots on the fluorescent background. (D) LOX cells stably expressing dominant-negative ARF6-T27N were plated in a mesenchymal invasion assay and allowed to degrade matrix overnight before being fixed, stained as indicated, and analyzed by confocal microscopy. (E) Confocal immunofluorescent analysis of fascin distribution and invasive capacity in cells subjected to dominant inhibition of Rab35. (F) LOX cells were transfected with dominant-negative Rab35-S22N and used in an invadopodium invasion assay. Scale bar, 25 µm. (G) LOX and LOX Rab35KO cells were plated in an in vitro mesenchymal invasion assay and allowed to degrade matrix overnight before being counterstained for actin and β 1 -integrin to define cell boundaries; they were then imaged by confocal microscopy. Depletion of Rab35 blocks invadopodium-mediated matrix degradation, which appears as dark spots in the control image. (H) Immunofluorescent staining of endogenous fascin at the invasive surface revealed that the intracellular distribution associated with invadopodium formation is lost with depletion of Rab35 and that fascin has a predominantly peripheral localization. (I) Expression of wild-type Rab35 rescues invadopodium-mediated invasive capacity in LOX Rab35KO cells. Unless otherwise indicated, scale bars indicate 20 µm.
    Figure Legend Snippet: Loss of Rab35 alters intracellular fascin localization. (A) Parental LOX cells plated on unlabeled gelatin were fixed, stained, and analyzed by confocal microscopy to examine the localization of endogenous fascin at the invasive, ventral surfaces of the cells. (B) Fascin localization and cortactin localization were examined together in cells transiently expressing mEmerald-fascin on unlabeled gelatin. Colocalization of both markers is indicative of localization of both components to invadopodia. (C) Invadopodium-mediated degradation, together with the intracellular distribution of endogenous fascin or cortactin, was examined in mesenchymal LOX cells transfected with myc–Rab35-Q67L. Matrix degradation appears as dark spots on the fluorescent background. (D) LOX cells stably expressing dominant-negative ARF6-T27N were plated in a mesenchymal invasion assay and allowed to degrade matrix overnight before being fixed, stained as indicated, and analyzed by confocal microscopy. (E) Confocal immunofluorescent analysis of fascin distribution and invasive capacity in cells subjected to dominant inhibition of Rab35. (F) LOX cells were transfected with dominant-negative Rab35-S22N and used in an invadopodium invasion assay. Scale bar, 25 µm. (G) LOX and LOX Rab35KO cells were plated in an in vitro mesenchymal invasion assay and allowed to degrade matrix overnight before being counterstained for actin and β 1 -integrin to define cell boundaries; they were then imaged by confocal microscopy. Depletion of Rab35 blocks invadopodium-mediated matrix degradation, which appears as dark spots in the control image. (H) Immunofluorescent staining of endogenous fascin at the invasive surface revealed that the intracellular distribution associated with invadopodium formation is lost with depletion of Rab35 and that fascin has a predominantly peripheral localization. (I) Expression of wild-type Rab35 rescues invadopodium-mediated invasive capacity in LOX Rab35KO cells. Unless otherwise indicated, scale bars indicate 20 µm.

    Techniques Used: Staining, Confocal Microscopy, Expressing, Transfection, Stable Transfection, Dominant Negative Mutation, Invasion Assay, Inhibition, In Vitro

    2) Product Images from "β-Catenin/CBP–Dependent Signaling Regulates TGF-β–Induced Epithelial to Mesenchymal Transition of Lens Epithelial Cells"

    Article Title: β-Catenin/CBP–Dependent Signaling Regulates TGF-β–Induced Epithelial to Mesenchymal Transition of Lens Epithelial Cells

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.16-20162

    Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.
    Figure Legend Snippet: Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.

    Techniques Used: Expressing, Inhibition

    Related Articles

    Incubation:

    Article Title: The use of mixed collagen-Matrigel matrices of increasing complexity recapitulates the biphasic role of cell adhesion in cancer cell migration: ECM sensing, remodeling and forces at the leading edge of cancer invasion
    Article Snippet: .. Non-specific interactions were blocked with 3% BSA and subsequently were incubated overnight at 4°C with the primary antibody Anti-Fascin (clone 55k2, Millipore, Billerica, MA, USA) at a dilution 1:200. .. The following day, samples were rinsed with PBS and incubated for two hours at room temperature with a secondary Donkey Anti-Mouse antibody conjugated with AlexaFluor 488 (1:400, Thermo Fisher, Waltham, MA, USA) and rhodamine-labeled phalloidin (1:75, Sigma Aldrich, Steinheim, Germany).

    other:

    Article Title: The key feature for early migratory processes
    Article Snippet: Used primary antibodies were against vinculin (clone hVIN-1, Sigma), fascin (clone 55K2, Chemicon, Temecula, CA, USA) and myosin IIa (M8064, Sigma).

    Article Title: Arp2/3 Complex Is Important for Filopodia Formation, Growth Cone Motility, and Neuritogenesis in Neuronal Cells
    Article Snippet: The following mouse monoclonal antibodies were used: cortactin (clone 411F; Upstate Biotechnology), fascin (clone 55K2; Chemicon International), and vinculin (Sigma-Aldrich, St. Louis, MO).

    Expressing:

    Article Title: Regulation of podocalyxin trafficking by Rab small GTPases in 2D and 3D epithelial cell cultures
    Article Snippet: .. Anti–E-cadherin rat monoclonal antibody (Takara Bio Inc.), anti-EEA1, anti-GM130, and anti-Rab11 mouse monoclonal antibodies (BD), anti-Rab10 rabbit monoclonal antibody (Cell Signaling Technology), anti-TfR mouse monoclonal antibody (Invitrogen), HRP-conjugated anti-FLAG tag (M2) mouse monoclonal antibody (Sigma-Aldrich), anti–β-actin mouse monoclonal antibody (Applied Biological Materials), anti-ACAP2/centaurin-β2 goat polyclonal antibody (Abcam), anti-Fascin mouse monoclonal antibody (EMD Millipore), and anti–MICAL-L1 mouse polyclonal antibody (Abnova) were obtained commercially. pEGFP-C1 (Takara Bio Inc.) or pEF-FLAG tag expression vectors carrying cDNAs of mouse Rabs were prepared as described previously ( ; ). .. A mutant mouse Rab35(TS/TA) carrying a Thr-to-Ser and Thr-to-Ala double mutation at aa positions 76 and 81, respectively, and Rab35(S5A) carrying a swapping mutation in the switch II region between Rab35 (aa 70–76) and Rab5A (aa 82–88) were also prepared as described previously ( ).

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  • 94
    Millipore fascin
    Loss of Rab35 alters intracellular <t>fascin</t> localization. (A) Parental LOX cells plated on unlabeled gelatin were fixed, stained, and analyzed by confocal microscopy to examine the localization of endogenous fascin at the invasive, ventral surfaces of the cells. (B) Fascin localization and cortactin localization were examined together in cells transiently expressing mEmerald-fascin on unlabeled gelatin. Colocalization of both markers is indicative of localization of both components to invadopodia. (C) Invadopodium-mediated degradation, together with the intracellular distribution of endogenous fascin or cortactin, was examined in mesenchymal LOX cells transfected with myc–Rab35-Q67L. Matrix degradation appears as dark spots on the fluorescent background. (D) LOX cells stably expressing dominant-negative ARF6-T27N were plated in a mesenchymal invasion assay and allowed to degrade matrix overnight before being fixed, stained as indicated, and analyzed by confocal microscopy. (E) Confocal immunofluorescent analysis of fascin distribution and invasive capacity in cells subjected to dominant inhibition of Rab35. (F) LOX cells were transfected with dominant-negative Rab35-S22N and used in an invadopodium invasion assay. Scale bar, 25 µm. (G) LOX and LOX Rab35KO cells were plated in an in vitro mesenchymal invasion assay and allowed to degrade matrix overnight before being counterstained for actin and β 1 <t>-integrin</t> to define cell boundaries; they were then imaged by confocal microscopy. Depletion of Rab35 blocks invadopodium-mediated matrix degradation, which appears as dark spots in the control image. (H) Immunofluorescent staining of endogenous fascin at the invasive surface revealed that the intracellular distribution associated with invadopodium formation is lost with depletion of Rab35 and that fascin has a predominantly peripheral localization. (I) Expression of wild-type Rab35 rescues invadopodium-mediated invasive capacity in LOX Rab35KO cells. Unless otherwise indicated, scale bars indicate 20 µm.
    Fascin, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Millipore
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fascin - by Bioz Stars, 2020-07
    94/100 stars
      Buy from Supplier

    85
    Millipore gst fascin
    Identification of <t>fascin</t> as a macroketone target. a, Diagram of the structures of migrastatin, one of its analogue (the macroketone core), and the biotin-conjugated macroketone core. b, Coomassie blue stain of the SDS/PAGE gel after protein affinity purification. The arrow indicated the band identified as mouse fascin 1. c, Direct interaction of fascin with macroketone. Agarose beads with biotin-conjugated macroketone (10 μM) or biotin (10 μM) were mixed with <t>GST-fascin</t> or GST. Data are representative of three experiments with similar results. d, Assay of the actin-bundling activity by the low-speed co-sedimentation assay. Polymerized F-actin (1 μM) was incubated with 0.125 μM or 0.25 μM purified fascin in the presence or absence of macroketone (10 μM). Supernatants (S) or pellets (P) were analyzed by SDS-PAGE followed by Coomassie blue staining. A representative of five experiments with similar outcomes was shown. e, Quantification of F-actin bundling assays from d . Results are mean ± SD (n=5, *, p
    Gst Fascin, supplied by Millipore, 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/gst fascin/product/Millipore
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gst fascin - by Bioz Stars, 2020-07
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    91
    Millipore fascia tubes
    Functional analysis of T‐and B‐cells in stem cells products. Proliferation of T‐and B‐cells in donor stem cell products was analysed using the <t>FASCIA</t> method. B‐cell proliferation was only measured upon stimulation with <t>PWM</t> and EBV , depicted PMW (b) and EBV (b) in 1 a. Cells were unstimulated or stimulated with PWM , SEA / SEB , CMV , VZV , HSV , EBV , tetanus toxoid, candida, influenza antigen or adenovirus antigen. Proliferation was expressed as stimulation indices ( SI ) with an SI > 4 considered positive. A: Proliferation against antigens, horizontal line represents mean SI and the dotted line represents cut‐off. B: Stem cell products were divided into two groups, ‘infection’ (I, n = 12) and ‘no infection’ ( NI , n = 9) based on patients’ clinical outcome. A composite analysis was performed where a positive response against any of HSV , EBV , CMV , VZV , candida or adenovirus rendered 1 point with a maximum of 6 points. ** P ‐value
    Fascia Tubes, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascia tubes/product/Millipore
    Average 91 stars, based on 1 article reviews
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    Image Search Results


    Loss of Rab35 alters intracellular fascin localization. (A) Parental LOX cells plated on unlabeled gelatin were fixed, stained, and analyzed by confocal microscopy to examine the localization of endogenous fascin at the invasive, ventral surfaces of the cells. (B) Fascin localization and cortactin localization were examined together in cells transiently expressing mEmerald-fascin on unlabeled gelatin. Colocalization of both markers is indicative of localization of both components to invadopodia. (C) Invadopodium-mediated degradation, together with the intracellular distribution of endogenous fascin or cortactin, was examined in mesenchymal LOX cells transfected with myc–Rab35-Q67L. Matrix degradation appears as dark spots on the fluorescent background. (D) LOX cells stably expressing dominant-negative ARF6-T27N were plated in a mesenchymal invasion assay and allowed to degrade matrix overnight before being fixed, stained as indicated, and analyzed by confocal microscopy. (E) Confocal immunofluorescent analysis of fascin distribution and invasive capacity in cells subjected to dominant inhibition of Rab35. (F) LOX cells were transfected with dominant-negative Rab35-S22N and used in an invadopodium invasion assay. Scale bar, 25 µm. (G) LOX and LOX Rab35KO cells were plated in an in vitro mesenchymal invasion assay and allowed to degrade matrix overnight before being counterstained for actin and β 1 -integrin to define cell boundaries; they were then imaged by confocal microscopy. Depletion of Rab35 blocks invadopodium-mediated matrix degradation, which appears as dark spots in the control image. (H) Immunofluorescent staining of endogenous fascin at the invasive surface revealed that the intracellular distribution associated with invadopodium formation is lost with depletion of Rab35 and that fascin has a predominantly peripheral localization. (I) Expression of wild-type Rab35 rescues invadopodium-mediated invasive capacity in LOX Rab35KO cells. Unless otherwise indicated, scale bars indicate 20 µm.

    Journal: Molecular and Cellular Biology

    Article Title: Coordinated Regulation of Intracellular Fascin Distribution Governs Tumor Microvesicle Release and Invasive Cell Capacity

    doi: 10.1128/MCB.00264-18

    Figure Lengend Snippet: Loss of Rab35 alters intracellular fascin localization. (A) Parental LOX cells plated on unlabeled gelatin were fixed, stained, and analyzed by confocal microscopy to examine the localization of endogenous fascin at the invasive, ventral surfaces of the cells. (B) Fascin localization and cortactin localization were examined together in cells transiently expressing mEmerald-fascin on unlabeled gelatin. Colocalization of both markers is indicative of localization of both components to invadopodia. (C) Invadopodium-mediated degradation, together with the intracellular distribution of endogenous fascin or cortactin, was examined in mesenchymal LOX cells transfected with myc–Rab35-Q67L. Matrix degradation appears as dark spots on the fluorescent background. (D) LOX cells stably expressing dominant-negative ARF6-T27N were plated in a mesenchymal invasion assay and allowed to degrade matrix overnight before being fixed, stained as indicated, and analyzed by confocal microscopy. (E) Confocal immunofluorescent analysis of fascin distribution and invasive capacity in cells subjected to dominant inhibition of Rab35. (F) LOX cells were transfected with dominant-negative Rab35-S22N and used in an invadopodium invasion assay. Scale bar, 25 µm. (G) LOX and LOX Rab35KO cells were plated in an in vitro mesenchymal invasion assay and allowed to degrade matrix overnight before being counterstained for actin and β 1 -integrin to define cell boundaries; they were then imaged by confocal microscopy. Depletion of Rab35 blocks invadopodium-mediated matrix degradation, which appears as dark spots in the control image. (H) Immunofluorescent staining of endogenous fascin at the invasive surface revealed that the intracellular distribution associated with invadopodium formation is lost with depletion of Rab35 and that fascin has a predominantly peripheral localization. (I) Expression of wild-type Rab35 rescues invadopodium-mediated invasive capacity in LOX Rab35KO cells. Unless otherwise indicated, scale bars indicate 20 µm.

    Article Snippet: Fascin, β1 -integrin, and tubulin antibodies were from Millipore Sigma.

    Techniques: Staining, Confocal Microscopy, Expressing, Transfection, Stable Transfection, Dominant Negative Mutation, Invasion Assay, Inhibition, In Vitro

    Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: β-Catenin/CBP–Dependent Signaling Regulates TGF-β–Induced Epithelial to Mesenchymal Transition of Lens Epithelial Cells

    doi: 10.1167/iovs.16-20162

    Figure Lengend Snippet: Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.

    Article Snippet: As to primary antibodies, fascin was from Millipore (Temecula, CA, USA), E-cadherin from BD Transduction Laboratories (Lexington, KY, USA), active β-catenin (clone 8E7) from Upstate (Lake Placid, NY, USA), MMP9 and GAPDH from Abcam (Cambridge, MA, USA), α-SMA fluorescein isothiocyanate (FITC) conjugated and unconjugated from Sigma-Aldrich Corp., Pan actin from Abcam.

    Techniques: Expressing, Inhibition

    Identification of fascin as a macroketone target. a, Diagram of the structures of migrastatin, one of its analogue (the macroketone core), and the biotin-conjugated macroketone core. b, Coomassie blue stain of the SDS/PAGE gel after protein affinity purification. The arrow indicated the band identified as mouse fascin 1. c, Direct interaction of fascin with macroketone. Agarose beads with biotin-conjugated macroketone (10 μM) or biotin (10 μM) were mixed with GST-fascin or GST. Data are representative of three experiments with similar results. d, Assay of the actin-bundling activity by the low-speed co-sedimentation assay. Polymerized F-actin (1 μM) was incubated with 0.125 μM or 0.25 μM purified fascin in the presence or absence of macroketone (10 μM). Supernatants (S) or pellets (P) were analyzed by SDS-PAGE followed by Coomassie blue staining. A representative of five experiments with similar outcomes was shown. e, Quantification of F-actin bundling assays from d . Results are mean ± SD (n=5, *, p

    Journal: Nature

    Article Title: Migrastatin Analogues Target Fascin to Block Tumor Metastasis

    doi: 10.1038/nature08978

    Figure Lengend Snippet: Identification of fascin as a macroketone target. a, Diagram of the structures of migrastatin, one of its analogue (the macroketone core), and the biotin-conjugated macroketone core. b, Coomassie blue stain of the SDS/PAGE gel after protein affinity purification. The arrow indicated the band identified as mouse fascin 1. c, Direct interaction of fascin with macroketone. Agarose beads with biotin-conjugated macroketone (10 μM) or biotin (10 μM) were mixed with GST-fascin or GST. Data are representative of three experiments with similar results. d, Assay of the actin-bundling activity by the low-speed co-sedimentation assay. Polymerized F-actin (1 μM) was incubated with 0.125 μM or 0.25 μM purified fascin in the presence or absence of macroketone (10 μM). Supernatants (S) or pellets (P) were analyzed by SDS-PAGE followed by Coomassie blue staining. A representative of five experiments with similar outcomes was shown. e, Quantification of F-actin bundling assays from d . Results are mean ± SD (n=5, *, p

    Article Snippet: After extensive washing, GST-fascin was eluted and concentrated with a Centricon Plus-20 (Millipore).

    Techniques: Staining, SDS Page, Affinity Purification, Activity Assay, Sedimentation, Incubation, Purification

    Functional analysis of T‐and B‐cells in stem cells products. Proliferation of T‐and B‐cells in donor stem cell products was analysed using the FASCIA method. B‐cell proliferation was only measured upon stimulation with PWM and EBV , depicted PMW (b) and EBV (b) in 1 a. Cells were unstimulated or stimulated with PWM , SEA / SEB , CMV , VZV , HSV , EBV , tetanus toxoid, candida, influenza antigen or adenovirus antigen. Proliferation was expressed as stimulation indices ( SI ) with an SI > 4 considered positive. A: Proliferation against antigens, horizontal line represents mean SI and the dotted line represents cut‐off. B: Stem cell products were divided into two groups, ‘infection’ (I, n = 12) and ‘no infection’ ( NI , n = 9) based on patients’ clinical outcome. A composite analysis was performed where a positive response against any of HSV , EBV , CMV , VZV , candida or adenovirus rendered 1 point with a maximum of 6 points. ** P ‐value

    Journal: Vox Sanguinis

    Article Title: Functionality testing of stem cell grafts to predict infectious complications after allogeneic hematopoietic stem cell transplantation

    doi: 10.1111/vox.12521

    Figure Lengend Snippet: Functional analysis of T‐and B‐cells in stem cells products. Proliferation of T‐and B‐cells in donor stem cell products was analysed using the FASCIA method. B‐cell proliferation was only measured upon stimulation with PWM and EBV , depicted PMW (b) and EBV (b) in 1 a. Cells were unstimulated or stimulated with PWM , SEA / SEB , CMV , VZV , HSV , EBV , tetanus toxoid, candida, influenza antigen or adenovirus antigen. Proliferation was expressed as stimulation indices ( SI ) with an SI > 4 considered positive. A: Proliferation against antigens, horizontal line represents mean SI and the dotted line represents cut‐off. B: Stem cell products were divided into two groups, ‘infection’ (I, n = 12) and ‘no infection’ ( NI , n = 9) based on patients’ clinical outcome. A composite analysis was performed where a positive response against any of HSV , EBV , CMV , VZV , candida or adenovirus rendered 1 point with a maximum of 6 points. ** P ‐value

    Article Snippet: Cytokine detection Cytokines and chemokines in culture supernatants from unstimulated FASCIA tubes and tubes stimulated with PWM, CMV, EBV and HSV from all patients were measured with a 5‐plex Milliplex human cytokine⁄chemokine kit, containing monoclonal antibodies to detect IFNγ, IL‐1b, IL‐4, IL‐10 and IL‐17A according to the manufacturer's instructions (EMD Millipore corporation, MA, USA).

    Techniques: Functional Assay, Infection

    Cytokine secretion in FASCIA cultures stimulated with EBV , CMV , HCV or PWM . Cytokines were analysed at day 7 in FASCIA culture supernatants. Results were divided based on presence of infection (I, n = 12) or no infection ( NI , n = 9) in patients at the 1‐year follow‐up. (a) Box and whiskers plot showing PWM stimulated concentration of IFN γ and IL ‐1β (in ng/ ml ) as well as IL ‐10 and IL ‐17 (in pg/ ml ) for stem cell products in the non‐infection group ( NI , checked boxes) and infection group (I, white boxes). Concentration of IL ‐10 and IL ‐17 (b) as well as IFN γ and IL ‐1β (c) in supernatants from cultures stimulated with HSV (black bars), CMV (grey bars) or EBV (white bars) divided based on absence of infectious complications ( NI ) or infectious complications (I). * P ‐value

    Journal: Vox Sanguinis

    Article Title: Functionality testing of stem cell grafts to predict infectious complications after allogeneic hematopoietic stem cell transplantation

    doi: 10.1111/vox.12521

    Figure Lengend Snippet: Cytokine secretion in FASCIA cultures stimulated with EBV , CMV , HCV or PWM . Cytokines were analysed at day 7 in FASCIA culture supernatants. Results were divided based on presence of infection (I, n = 12) or no infection ( NI , n = 9) in patients at the 1‐year follow‐up. (a) Box and whiskers plot showing PWM stimulated concentration of IFN γ and IL ‐1β (in ng/ ml ) as well as IL ‐10 and IL ‐17 (in pg/ ml ) for stem cell products in the non‐infection group ( NI , checked boxes) and infection group (I, white boxes). Concentration of IL ‐10 and IL ‐17 (b) as well as IFN γ and IL ‐1β (c) in supernatants from cultures stimulated with HSV (black bars), CMV (grey bars) or EBV (white bars) divided based on absence of infectious complications ( NI ) or infectious complications (I). * P ‐value

    Article Snippet: Cytokine detection Cytokines and chemokines in culture supernatants from unstimulated FASCIA tubes and tubes stimulated with PWM, CMV, EBV and HSV from all patients were measured with a 5‐plex Milliplex human cytokine⁄chemokine kit, containing monoclonal antibodies to detect IFNγ, IL‐1b, IL‐4, IL‐10 and IL‐17A according to the manufacturer's instructions (EMD Millipore corporation, MA, USA).

    Techniques: Infection, Concentration Assay