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  • cd147  (Abcam)
    86
    Abcam cd147
    HCMV colocalizes with <t>CD147</t> in early endosomes. ARPE-19 epithelial cells on glass slides were transduced with a baculovirus expressing a fluorescent-tagged early endosome marker, EEA-1. The cells were then incubated with HCMV UL32-GFP virus particles for 1 h at 4°C and then shifted to 37°C for 1 h. The cells were fixed and processed for immunofluorescent staining with an anti-CD147 MAb (109403) followed by a 649-conjugated secondary antibody to detect CD147 and then analyzed by deconvolution microscopy. (A and B) Representative images with arrows depict HCMV particles (green) colocalizing with CD147 (red) in EEA-1-labeled endosomes (blue). (C to E) More highly magnified images of HCMV particles (green) colocalizing with CD147 (red) and EEA-1-labeled endosomes (blue). The scale bars on the bottom left of each panel represent 1 µm.
    Cd147, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Santa Cruz Biotechnology cd147
    Molecular association between CD29, CD98, CD187, and the actin cytoskeleton in U937 cell-cell adhesion. (A and C) U937 cells were incubated with pro-aggregative (activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), <t>CD147</t> (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) for 3 h. The localization patterns between CD29, CD98, CD147, and the actin cytoskeleton were evaluated by confocal microscopy. Results show one experiment out of three. (B) U937 cells (1×10 7 cells/ml) were treated with antibodies to CD147 (M6-1D4) and CD98 (AHN-18) for 6 h. After immunoprecipitation with antibodies to CD147 or CD98, the level of co-immunoprecipitated CD147 was determined by immunoblotting analysis with anti-CD147 antibodies. Results represent one experiment out of three. Relative intensities were calculated with the DNR Bioimaging system (Gelquant software Ver. 2.7).
    Cd147, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cd147/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cd147 - by Bioz Stars, 2021-06
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    99
    Millipore cd147
    Infection of intestinal organoids by SARS-CoV-2 in vitro A . Baseline SARS-CoV-2 host gene expression in mock treated A . Representative immunofluorescence staining of intestinal organoids for SARS-CoV-2 nucleocapsid (N) (red), the epithelial marker EPCAM (green) and DAPI (blue), following mock or SARS-CoV-2 infection (MOI of 0.5 or 1, 48 hours). Scale bar: 100μm. B .intestinal organoids day 24 and d50. C . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected intestinal organoids infected (MOI of 0.05 or 0.5, 24 hours). D . Representative immunofluorescence staining of dissociated intestinal cells after SARS-CoV-2 infection on day 25 (MOI of 0.05, 48 hours), positive for SARS-CoV-2 N protein (red), EPCAM (green), DAPI (blue). Scale bar: 50μm. E . shRNA knock down of FURIN, ACE2 , and <t>CD147</t> host genes in dissociated intestinal cells, normalized to 18S levels and infected scrambled control. F . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2, CD147 and FURIN , as well as a scrambled control, error bars shown as SEM. G . Quantification of high-content imaging for SARS-CoV-2 nucleocapsid (N) protein in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2 and FURIN , as well as a scrambled control. (SARS-CoV-2 infected at MOI of 0.05 and 0.5 for 48 hours.) Each data point represents one 96-well. 2-way ANOVA; *p
    Cd147, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech cd147
    Analysis of tissue microarray cores for immunohistochemistry. A: Representative images from immunohistochemical staining of p-STAT3 nuclear expression (upper), Cyclin D1 nuclear expression (middle), <t>CD147</t> cytoplasmic expression (lower) in human normal
    Cd147, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cd147 - by Bioz Stars, 2021-06
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    N/A
    This is a recombinant monoclonal antibody This chimeric mouse antibody was made using the variable domain sequences of the original Rat IgG1 format for improved compatibility with existing reagents assays
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    N/A
    This antibody recognizes extracellular epitope 2 within the N terminal Ig domain of human CD147 It expressed more intensely on thymocytes than on mature peripheral blood T cells CD147 is
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    N/A
    Mouse monoclonal CD147 antibody
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    Image Search Results


    HCMV colocalizes with CD147 in early endosomes. ARPE-19 epithelial cells on glass slides were transduced with a baculovirus expressing a fluorescent-tagged early endosome marker, EEA-1. The cells were then incubated with HCMV UL32-GFP virus particles for 1 h at 4°C and then shifted to 37°C for 1 h. The cells were fixed and processed for immunofluorescent staining with an anti-CD147 MAb (109403) followed by a 649-conjugated secondary antibody to detect CD147 and then analyzed by deconvolution microscopy. (A and B) Representative images with arrows depict HCMV particles (green) colocalizing with CD147 (red) in EEA-1-labeled endosomes (blue). (C to E) More highly magnified images of HCMV particles (green) colocalizing with CD147 (red) and EEA-1-labeled endosomes (blue). The scale bars on the bottom left of each panel represent 1 µm.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: HCMV colocalizes with CD147 in early endosomes. ARPE-19 epithelial cells on glass slides were transduced with a baculovirus expressing a fluorescent-tagged early endosome marker, EEA-1. The cells were then incubated with HCMV UL32-GFP virus particles for 1 h at 4°C and then shifted to 37°C for 1 h. The cells were fixed and processed for immunofluorescent staining with an anti-CD147 MAb (109403) followed by a 649-conjugated secondary antibody to detect CD147 and then analyzed by deconvolution microscopy. (A and B) Representative images with arrows depict HCMV particles (green) colocalizing with CD147 (red) in EEA-1-labeled endosomes (blue). (C to E) More highly magnified images of HCMV particles (green) colocalizing with CD147 (red) and EEA-1-labeled endosomes (blue). The scale bars on the bottom left of each panel represent 1 µm.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Transduction, Expressing, Marker, Incubation, Staining, Microscopy, Labeling

    CD147 induces cell-cell fusion of HeLa cells expressing HCMV fusion proteins. (A to C) HeLa cells were transduced with Ad vectors expressing HCMV gB and gH/gL (A), gB and gH/gL/gO (B), or Ad vectors expressing gB, gH/gL, UL128, UL130, and UL131 (C) and assayed for the presence of cell-cell fusion. (D to F) HeLa cells were transduced with a retrovirus to express CD147 and then transduced with Ad vectors expressing HCMV gB and gH/gL (D), gB and gH/gL/gO (E), or Ad vectors expressing gB, gH/gL, UL128, UL130, and UL131 (F) and assayed for the presence of cell-cell fusion. Fusion was quantified by comparing the number of nuclei involved in cell-cell fusion events (involving ≥5 cells per fusion event) with the total number of nuclei.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: CD147 induces cell-cell fusion of HeLa cells expressing HCMV fusion proteins. (A to C) HeLa cells were transduced with Ad vectors expressing HCMV gB and gH/gL (A), gB and gH/gL/gO (B), or Ad vectors expressing gB, gH/gL, UL128, UL130, and UL131 (C) and assayed for the presence of cell-cell fusion. (D to F) HeLa cells were transduced with a retrovirus to express CD147 and then transduced with Ad vectors expressing HCMV gB and gH/gL (D), gB and gH/gL/gO (E), or Ad vectors expressing gB, gH/gL, UL128, UL130, and UL131 (F) and assayed for the presence of cell-cell fusion. Fusion was quantified by comparing the number of nuclei involved in cell-cell fusion events (involving ≥5 cells per fusion event) with the total number of nuclei.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Expressing, Transduction

    Transduction of HeLa cells with CD147 enhances HCMV entry. (A and B) HeLa cells were transduced with an empty retrovirus (A) or a retrovirus expressing CD147 (HeLa-CD147) (B), propagated in puromycin to select for retrovirus transduction, and then challenged with HCMV BAD r UL131, which expresses the pentamer and GFP. (C) HeLa-CD147 cells were challenged with HCMV AD 169, which does not express the pentamer and expresses GFP (AD 169-GFP). (D) HeLa-CD147 cells were challenged with AD 169-GFP for 2 h, and then the cells were treated with a solution of buffered 43% PEG, which promotes entry of virus into cells. The level of HCMV entry is based on the percentage of GFP expression (indicated on the bottom right of each panel).

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: Transduction of HeLa cells with CD147 enhances HCMV entry. (A and B) HeLa cells were transduced with an empty retrovirus (A) or a retrovirus expressing CD147 (HeLa-CD147) (B), propagated in puromycin to select for retrovirus transduction, and then challenged with HCMV BAD r UL131, which expresses the pentamer and GFP. (C) HeLa-CD147 cells were challenged with HCMV AD 169, which does not express the pentamer and expresses GFP (AD 169-GFP). (D) HeLa-CD147 cells were challenged with AD 169-GFP for 2 h, and then the cells were treated with a solution of buffered 43% PEG, which promotes entry of virus into cells. The level of HCMV entry is based on the percentage of GFP expression (indicated on the bottom right of each panel).

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Transduction, Expressing

    Effects of soluble CD147 on HCMV entry and binding to soluble HCMV glycoproteins. (A) A soluble form of CD147 that was fused to a polyhistidine epitope tag and purified from the tissue culture supernatant of plasmid-transfected 293E cells via use of nickel-agarose was analyzed by electrophoresis, polyacrylamide gel staining, and Coomassie brilliant blue stain. (B) Soluble CD147 was bound to nickel-coated plates and then analyzed in an ELISA. Individual wells were incubated with either a control MAb to transferrin (TfR) or CD147-specific MAbs 109403, 12G10, or 2F5, followed by goat anti-mouse–HRP conjugate. Controls also included incubation with secondary antibodies only (secondary). The bound antibodies were detected by chemiluminescence by adding Turbo-TMB ELISA substrate (Thermo Fisher), and absorbance was read using a precision plate reader (Molecular Dynamics). (C) HCMV BAD r UL131 virus particles were incubated with soluble CD147 (sol. CD147 + ) at 100 µg ml −1 or no protein (sol. CD147 -) for 1 h at 37°C and then added to ARPE-19 epithelial cells or HUVECs for 2 h at 37°C. The virus inoclula were removed, and cells were incubated an additional 24 h before the numbers of GFP + cells were assessed. Relative infectivity was calculated by comparing the numbers of GFP + cells in soluble CD147 treated groups versus no-protein controls. (D) Soluble CD147 (black bars) or soluble PDGFRα (gray bars) were allowed to adsorb onto microtiter plates and then incubated with soluble gH/gL (dimer), trimer, or pentamer complexes. The plates were washed and then incubated with anti-gH MAb 14-4b, washed, and incubated with goat anti-mouse–HRP conjugate. Positive controls included anti-CD147 or anti-PDGFRα MAbs followed by secondary goat anti-mouse–HRP conjugate (CD147 pos. and PDGFRα pos.). Negative controls involved wells with adsorbed proteins incubated with secondary antibodies only (secondary). Chemiluminescence was detected as described for panel B.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: Effects of soluble CD147 on HCMV entry and binding to soluble HCMV glycoproteins. (A) A soluble form of CD147 that was fused to a polyhistidine epitope tag and purified from the tissue culture supernatant of plasmid-transfected 293E cells via use of nickel-agarose was analyzed by electrophoresis, polyacrylamide gel staining, and Coomassie brilliant blue stain. (B) Soluble CD147 was bound to nickel-coated plates and then analyzed in an ELISA. Individual wells were incubated with either a control MAb to transferrin (TfR) or CD147-specific MAbs 109403, 12G10, or 2F5, followed by goat anti-mouse–HRP conjugate. Controls also included incubation with secondary antibodies only (secondary). The bound antibodies were detected by chemiluminescence by adding Turbo-TMB ELISA substrate (Thermo Fisher), and absorbance was read using a precision plate reader (Molecular Dynamics). (C) HCMV BAD r UL131 virus particles were incubated with soluble CD147 (sol. CD147 + ) at 100 µg ml −1 or no protein (sol. CD147 -) for 1 h at 37°C and then added to ARPE-19 epithelial cells or HUVECs for 2 h at 37°C. The virus inoclula were removed, and cells were incubated an additional 24 h before the numbers of GFP + cells were assessed. Relative infectivity was calculated by comparing the numbers of GFP + cells in soluble CD147 treated groups versus no-protein controls. (D) Soluble CD147 (black bars) or soluble PDGFRα (gray bars) were allowed to adsorb onto microtiter plates and then incubated with soluble gH/gL (dimer), trimer, or pentamer complexes. The plates were washed and then incubated with anti-gH MAb 14-4b, washed, and incubated with goat anti-mouse–HRP conjugate. Positive controls included anti-CD147 or anti-PDGFRα MAbs followed by secondary goat anti-mouse–HRP conjugate (CD147 pos. and PDGFRα pos.). Negative controls involved wells with adsorbed proteins incubated with secondary antibodies only (secondary). Chemiluminescence was detected as described for panel B.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Binding Assay, Purification, Plasmid Preparation, Transfection, Electrophoresis, Staining, Enzyme-linked Immunosorbent Assay, Incubation, Infection

    Inhibition of HCMV entry via anti-CD147 antibodies. (A) Human ARPE-19 epithelial cells were left untreated (No Ab) or were pretreated with MAbs specific for the transferrin receptor (TfR) or CD147 (MAbs 9B10, M61, 109403, 2F5, and 12G10) for 1 h at 37°C and then HCMV BAD r UL131 was added to these cells in the presence of the MAbs for an additional 2 h at 37°C. The virus inoculum was removed, and the culture medium was replenished with fresh growth medium that contained the MAbs for 24 h, after which HCMV entry was assessed. (B) Human retinal epithelial cells were either left untreated or treated with antibodies as described above and then incubated with HSV-1 F-BAC VP26GFP, an HSV recombinant that express a GFP-tagged tegument protein. (C and D) Antibody inhibition assays were performed as described for panel A with HUVECs or fibroblast cells, respectively, and then challenged with HCMV BAD r UL131. Under all experimental conditions, virus entry was quantified by counting GFP-positive from at least three independent wells, and these values compared to the numbers of GFP-positive cells among those not treated with antibodies. (E) Lysates from epithelial, endothelial, or fibroblast cells were analyzed by Western blotting to detect endogenous CD147 by probing membranes with anti-CD147 MAb 109403 or with polyclonal antibodies against beta-actin as a loading control.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: Inhibition of HCMV entry via anti-CD147 antibodies. (A) Human ARPE-19 epithelial cells were left untreated (No Ab) or were pretreated with MAbs specific for the transferrin receptor (TfR) or CD147 (MAbs 9B10, M61, 109403, 2F5, and 12G10) for 1 h at 37°C and then HCMV BAD r UL131 was added to these cells in the presence of the MAbs for an additional 2 h at 37°C. The virus inoculum was removed, and the culture medium was replenished with fresh growth medium that contained the MAbs for 24 h, after which HCMV entry was assessed. (B) Human retinal epithelial cells were either left untreated or treated with antibodies as described above and then incubated with HSV-1 F-BAC VP26GFP, an HSV recombinant that express a GFP-tagged tegument protein. (C and D) Antibody inhibition assays were performed as described for panel A with HUVECs or fibroblast cells, respectively, and then challenged with HCMV BAD r UL131. Under all experimental conditions, virus entry was quantified by counting GFP-positive from at least three independent wells, and these values compared to the numbers of GFP-positive cells among those not treated with antibodies. (E) Lysates from epithelial, endothelial, or fibroblast cells were analyzed by Western blotting to detect endogenous CD147 by probing membranes with anti-CD147 MAb 109403 or with polyclonal antibodies against beta-actin as a loading control.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Inhibition, Incubation, BAC Assay, Recombinant, Western Blot

    HCMV colocalizes with CD147 patches on the surface of ARPE-19 cells. (A) ARPE-19 cells on glass slides were incubated with anti-CD147 MAb 109403 and HCMV UL32-GFP virus particles at 4° for 1 h, then shifted to 37° for 15 min, and then fixed. The fixed cells were then incubated with goat anti-mouse–594 fluorescent secondary antibody to detect surface CD147 and then the cells were analyzed by deconvolution microscopy. Arrows indicate green fluorescent HCMV virus particles that overlapped with red fluorescent channel signal from CD147 surface patches. (B and C) Magnified images of the squared areas from panel A. (D) ARPE-19 cells were incubated with anti-EGFR MAb (LA1) and HCMV UL32-GFP virus particles at 4°C for 1 h, then shifted to 37°C for 15 min, fixed, and then processed to detect surface EGFR as described for panel A. The scale bars on the bottom right of each panel represent 1 µm.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: HCMV colocalizes with CD147 patches on the surface of ARPE-19 cells. (A) ARPE-19 cells on glass slides were incubated with anti-CD147 MAb 109403 and HCMV UL32-GFP virus particles at 4° for 1 h, then shifted to 37° for 15 min, and then fixed. The fixed cells were then incubated with goat anti-mouse–594 fluorescent secondary antibody to detect surface CD147 and then the cells were analyzed by deconvolution microscopy. Arrows indicate green fluorescent HCMV virus particles that overlapped with red fluorescent channel signal from CD147 surface patches. (B and C) Magnified images of the squared areas from panel A. (D) ARPE-19 cells were incubated with anti-EGFR MAb (LA1) and HCMV UL32-GFP virus particles at 4°C for 1 h, then shifted to 37°C for 15 min, fixed, and then processed to detect surface EGFR as described for panel A. The scale bars on the bottom right of each panel represent 1 µm.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Incubation, Microscopy

    Silencing CD147 inhibits HCMV entry into endothelial cells. (A) Lysates from a control endothelial cell line (tAECs) transduced with an empty lentivirus vector (Ctl) or an endothelial cell line (tAECs) transduced with a lentivirus expressing a CD147-specific shRNA (CD147 shRNA; clone ID V3LHS_412785; Dharmacon) were analyzed in Western blot assays to determine the level of CD147 silencing. Membranes were probed with either anti-CD147 MAb 109403 or a rabbit polyclonal antibody against beta-actin (a loading control). (B) Human endothelial cells (tAECs) were transduced with an empty lentivirus vector (Ctl, lacking any shRNA) or a lentivirus vector expressing an shRNA to CD147 (CD147 shRNA) and then selected by puromycin. The cells lines were then infected with HCMV strain BAD r UL131, and the level of entry was assessed by monitoring GFP expression from at least three independent wells. (C) The lentivirus-transduced cell lines in panel B were infected with HSV-1 VP26-GFP and analyzed for GFP expression after 24 h. (D) Lysates from control fibroblasts transduced with an empty lentivirus vectors (Ctl) or CD147 shRNA-expressing fibroblasts (CD147 shRNA) were analyzed by Western blotting to characterize CD147 silencing as described for panel A. (E) Fibroblast cell lines that had been transduced with an empty lentivirus vector (Ctl) or a lentivirus vector expressing an shRNA to CD147 (CD147 shRNA) were established using puromycin and then infected with HCMV BAD r UL131, after which the number of GFP-positive cells was analyzed.

    Journal: mBio

    Article Title: CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into Epithelial and Endothelial Cells

    doi: 10.1128/mBio.00781-18

    Figure Lengend Snippet: Silencing CD147 inhibits HCMV entry into endothelial cells. (A) Lysates from a control endothelial cell line (tAECs) transduced with an empty lentivirus vector (Ctl) or an endothelial cell line (tAECs) transduced with a lentivirus expressing a CD147-specific shRNA (CD147 shRNA; clone ID V3LHS_412785; Dharmacon) were analyzed in Western blot assays to determine the level of CD147 silencing. Membranes were probed with either anti-CD147 MAb 109403 or a rabbit polyclonal antibody against beta-actin (a loading control). (B) Human endothelial cells (tAECs) were transduced with an empty lentivirus vector (Ctl, lacking any shRNA) or a lentivirus vector expressing an shRNA to CD147 (CD147 shRNA) and then selected by puromycin. The cells lines were then infected with HCMV strain BAD r UL131, and the level of entry was assessed by monitoring GFP expression from at least three independent wells. (C) The lentivirus-transduced cell lines in panel B were infected with HSV-1 VP26-GFP and analyzed for GFP expression after 24 h. (D) Lysates from control fibroblasts transduced with an empty lentivirus vectors (Ctl) or CD147 shRNA-expressing fibroblasts (CD147 shRNA) were analyzed by Western blotting to characterize CD147 silencing as described for panel A. (E) Fibroblast cell lines that had been transduced with an empty lentivirus vector (Ctl) or a lentivirus vector expressing an shRNA to CD147 (CD147 shRNA) were established using puromycin and then infected with HCMV BAD r UL131, after which the number of GFP-positive cells was analyzed.

    Article Snippet: Initially, these experiments involved three commercial monoclonal antibodies (MAbs) specific for CD147, MAbs 9B10 and M6/1 from Abcam, Inc., and MAb 109403 from R & D Systems.

    Techniques: Transduction, Plasmid Preparation, CTL Assay, Expressing, shRNA, Western Blot, Infection

    Molecular association between CD29, CD98, CD187, and the actin cytoskeleton in U937 cell-cell adhesion. (A and C) U937 cells were incubated with pro-aggregative (activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) for 3 h. The localization patterns between CD29, CD98, CD147, and the actin cytoskeleton were evaluated by confocal microscopy. Results show one experiment out of three. (B) U937 cells (1×10 7 cells/ml) were treated with antibodies to CD147 (M6-1D4) and CD98 (AHN-18) for 6 h. After immunoprecipitation with antibodies to CD147 or CD98, the level of co-immunoprecipitated CD147 was determined by immunoblotting analysis with anti-CD147 antibodies. Results represent one experiment out of three. Relative intensities were calculated with the DNR Bioimaging system (Gelquant software Ver. 2.7).

    Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

    Article Title: Molecular association of CD98, CD29, and CD147 critically mediates monocytic U937 cell adhesion

    doi: 10.4196/kjpp.2016.20.5.515

    Figure Lengend Snippet: Molecular association between CD29, CD98, CD187, and the actin cytoskeleton in U937 cell-cell adhesion. (A and C) U937 cells were incubated with pro-aggregative (activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) for 3 h. The localization patterns between CD29, CD98, CD147, and the actin cytoskeleton were evaluated by confocal microscopy. Results show one experiment out of three. (B) U937 cells (1×10 7 cells/ml) were treated with antibodies to CD147 (M6-1D4) and CD98 (AHN-18) for 6 h. After immunoprecipitation with antibodies to CD147 or CD98, the level of co-immunoprecipitated CD147 was determined by immunoblotting analysis with anti-CD147 antibodies. Results represent one experiment out of three. Relative intensities were calculated with the DNR Bioimaging system (Gelquant software Ver. 2.7).

    Article Snippet: Antibodies to CD98 (mouse, 4F2) and CD147 (rabbit, EMMPRIN) for immunoprecipitation and immunoblotting were from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and Sino Biological Inc. (Beijing, China), respectively.

    Techniques: Incubation, Confocal Microscopy, Immunoprecipitation, Software

    Cell-cell adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies. (A) U937 cells were incubated with pro-aggregative (aggregation-activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) for 6 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (B) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. Results (aggregation relative to control culture in the presence of stimuli) are expressed as mean±SEM from three independent experiments performed in triplicate. ** p

    Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

    Article Title: Molecular association of CD98, CD29, and CD147 critically mediates monocytic U937 cell adhesion

    doi: 10.4196/kjpp.2016.20.5.515

    Figure Lengend Snippet: Cell-cell adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies. (A) U937 cells were incubated with pro-aggregative (aggregation-activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) for 6 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (B) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. Results (aggregation relative to control culture in the presence of stimuli) are expressed as mean±SEM from three independent experiments performed in triplicate. ** p

    Article Snippet: Antibodies to CD98 (mouse, 4F2) and CD147 (rabbit, EMMPRIN) for immunoprecipitation and immunoblotting were from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and Sino Biological Inc. (Beijing, China), respectively.

    Techniques: Ligation, Incubation, Microscopy, Software

    Flow cytometric analysis of surface adhesion molecule expression in U937 cells. Surface adhesion molecules [CD29 (β1-integrins), CD43, CD98, and CD147] in U937 cells (1×10 5 ) were analyzed by flow cytometry. All staining antibodies were used at 1~5 µg/ml. Mean fluorescence intensity ( MFI , percent of control) was calculated using WIN-MDI software from a minimum of 7,500 cells. The results (mean±SD, n =4) show one representative experiment out of three.

    Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

    Article Title: Molecular association of CD98, CD29, and CD147 critically mediates monocytic U937 cell adhesion

    doi: 10.4196/kjpp.2016.20.5.515

    Figure Lengend Snippet: Flow cytometric analysis of surface adhesion molecule expression in U937 cells. Surface adhesion molecules [CD29 (β1-integrins), CD43, CD98, and CD147] in U937 cells (1×10 5 ) were analyzed by flow cytometry. All staining antibodies were used at 1~5 µg/ml. Mean fluorescence intensity ( MFI , percent of control) was calculated using WIN-MDI software from a minimum of 7,500 cells. The results (mean±SD, n =4) show one representative experiment out of three.

    Article Snippet: Antibodies to CD98 (mouse, 4F2) and CD147 (rabbit, EMMPRIN) for immunoprecipitation and immunoblotting were from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and Sino Biological Inc. (Beijing, China), respectively.

    Techniques: Flow Cytometry, Expressing, Cytometry, Staining, Fluorescence, Software

    Effect of blocking antibodies on cell-cell adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies. (A) U937 cells were incubated with pro-aggregative (aggregation-activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) in the presence of aggregation-blocking antibodies to CD29 (P5D2, 1 µg/ml), CD98 (MEM 108, 1 µg/ml), and CD147 (MEM M6/1, 1 µg/ml) for 6 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (B) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. Results (aggregation relative to control culture in the presence of stimuli) are expressed as mean±SEM from three independent experiments performed in triplicate. * p

    Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

    Article Title: Molecular association of CD98, CD29, and CD147 critically mediates monocytic U937 cell adhesion

    doi: 10.4196/kjpp.2016.20.5.515

    Figure Lengend Snippet: Effect of blocking antibodies on cell-cell adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies. (A) U937 cells were incubated with pro-aggregative (aggregation-activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) in the presence of aggregation-blocking antibodies to CD29 (P5D2, 1 µg/ml), CD98 (MEM 108, 1 µg/ml), and CD147 (MEM M6/1, 1 µg/ml) for 6 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (B) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. Results (aggregation relative to control culture in the presence of stimuli) are expressed as mean±SEM from three independent experiments performed in triplicate. * p

    Article Snippet: Antibodies to CD98 (mouse, 4F2) and CD147 (rabbit, EMMPRIN) for immunoprecipitation and immunoblotting were from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and Sino Biological Inc. (Beijing, China), respectively.

    Techniques: Blocking Assay, Ligation, Incubation, Microscopy, Software

    Effect of pharmacological inhibitors of ERK, PKCδ, and actin polymerization on cell-cell aggregation or cell-fibronectin adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies or immobilized fibronectin. (A left panel) U937 cells were incubated with pro-aggregative (activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) in the presence of chemical inhibitors to ERK (U0126, 25 µM), PKCδ (rottlerin, 10 µM), and actin polymerization (Cyto B: cytochalasin B, 10 µM) for 3 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (A right panel) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. (B) U937 cells pretreated with 10 µg/ml of function blocking antibody to CD29 (P5D2) or inhibitors [U0126 (20 µM) and cytochalasin B (10 µM)] were seeded on fibronectin (50 µg/ml)-immobilized plates and further incubated for 3 h. Attached cells were determined by crystal violet assay, as described in Materials and Methods. (C) Cytotoxic activity of U0126, rottlerin, and CytoB was confirmed by a conventional MTT assay. Results (aggregation relative to control culture in the presence of stimuli or % of cytotoxicity) are expressed as mean±SEM from three independent experiments performed in triplicate. ** p

    Journal: The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology

    Article Title: Molecular association of CD98, CD29, and CD147 critically mediates monocytic U937 cell adhesion

    doi: 10.4196/kjpp.2016.20.5.515

    Figure Lengend Snippet: Effect of pharmacological inhibitors of ERK, PKCδ, and actin polymerization on cell-cell aggregation or cell-fibronectin adhesion induced by ligation of surface adhesion molecules with aggregation-activating antibodies or immobilized fibronectin. (A left panel) U937 cells were incubated with pro-aggregative (activating) antibodies (1 µg/ml each as IgG1) to CD98 (AHN-18, 1 µg/ml), CD29 (MEM101A, 1 µg/ml), CD147 (M6-1D4, 10 µg/ml), and CD43 (161-46, 1 µg/ml) in the presence of chemical inhibitors to ERK (U0126, 25 µM), PKCδ (rottlerin, 10 µM), and actin polymerization (Cyto B: cytochalasin B, 10 µM) for 3 h. Aggregation of cells in the absence of stimuli (normal conditions) was less than 4%. Percentage of aggregation was quantitatively determined by cell-cell adhesion assays. (A right panel) Images of the aggregated cells in culture were obtained using an inverted phase-contrast microscope attached to a video camera, and captured using NIH image software. (B) U937 cells pretreated with 10 µg/ml of function blocking antibody to CD29 (P5D2) or inhibitors [U0126 (20 µM) and cytochalasin B (10 µM)] were seeded on fibronectin (50 µg/ml)-immobilized plates and further incubated for 3 h. Attached cells were determined by crystal violet assay, as described in Materials and Methods. (C) Cytotoxic activity of U0126, rottlerin, and CytoB was confirmed by a conventional MTT assay. Results (aggregation relative to control culture in the presence of stimuli or % of cytotoxicity) are expressed as mean±SEM from three independent experiments performed in triplicate. ** p

    Article Snippet: Antibodies to CD98 (mouse, 4F2) and CD147 (rabbit, EMMPRIN) for immunoprecipitation and immunoblotting were from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and Sino Biological Inc. (Beijing, China), respectively.

    Techniques: Ligation, Incubation, Microscopy, Software, Blocking Assay, Crystal Violet Assay, Activity Assay, MTT Assay

    Infection of intestinal organoids by SARS-CoV-2 in vitro A . Baseline SARS-CoV-2 host gene expression in mock treated A . Representative immunofluorescence staining of intestinal organoids for SARS-CoV-2 nucleocapsid (N) (red), the epithelial marker EPCAM (green) and DAPI (blue), following mock or SARS-CoV-2 infection (MOI of 0.5 or 1, 48 hours). Scale bar: 100μm. B .intestinal organoids day 24 and d50. C . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected intestinal organoids infected (MOI of 0.05 or 0.5, 24 hours). D . Representative immunofluorescence staining of dissociated intestinal cells after SARS-CoV-2 infection on day 25 (MOI of 0.05, 48 hours), positive for SARS-CoV-2 N protein (red), EPCAM (green), DAPI (blue). Scale bar: 50μm. E . shRNA knock down of FURIN, ACE2 , and CD147 host genes in dissociated intestinal cells, normalized to 18S levels and infected scrambled control. F . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2, CD147 and FURIN , as well as a scrambled control, error bars shown as SEM. G . Quantification of high-content imaging for SARS-CoV-2 nucleocapsid (N) protein in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2 and FURIN , as well as a scrambled control. (SARS-CoV-2 infected at MOI of 0.05 and 0.5 for 48 hours.) Each data point represents one 96-well. 2-way ANOVA; *p

    Journal: bioRxiv

    Article Title: Common genetic variation in humans impacts in vitro susceptibility to SARS-CoV-2 infection

    doi: 10.1101/2020.09.20.300574

    Figure Lengend Snippet: Infection of intestinal organoids by SARS-CoV-2 in vitro A . Baseline SARS-CoV-2 host gene expression in mock treated A . Representative immunofluorescence staining of intestinal organoids for SARS-CoV-2 nucleocapsid (N) (red), the epithelial marker EPCAM (green) and DAPI (blue), following mock or SARS-CoV-2 infection (MOI of 0.5 or 1, 48 hours). Scale bar: 100μm. B .intestinal organoids day 24 and d50. C . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected intestinal organoids infected (MOI of 0.05 or 0.5, 24 hours). D . Representative immunofluorescence staining of dissociated intestinal cells after SARS-CoV-2 infection on day 25 (MOI of 0.05, 48 hours), positive for SARS-CoV-2 N protein (red), EPCAM (green), DAPI (blue). Scale bar: 50μm. E . shRNA knock down of FURIN, ACE2 , and CD147 host genes in dissociated intestinal cells, normalized to 18S levels and infected scrambled control. F . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2, CD147 and FURIN , as well as a scrambled control, error bars shown as SEM. G . Quantification of high-content imaging for SARS-CoV-2 nucleocapsid (N) protein in mock and SARS-CoV-2 infected dissociated intestinal cells expressing shRNAs against ACE2 and FURIN , as well as a scrambled control. (SARS-CoV-2 infected at MOI of 0.05 and 0.5 for 48 hours.) Each data point represents one 96-well. 2-way ANOVA; *p

    Article Snippet: Used shRNA against ACE2 (SHCLNG-NM_021804), CD147 (SHCLNG-NM_001728), TMPRSS2 (SHCLNG-NM_005656) were obtained from Sigma.

    Techniques: Infection, In Vitro, Expressing, Immunofluorescence, Staining, Marker, Real-time Polymerase Chain Reaction, shRNA, Imaging

    Infection of lung alveolospheres by SARS-CoV-2 in vitro A . Representative brightfield image of alveolosphere cultures on d30. 100μm. B . Baseline SARS-CoV-2 host gene expression in alveolospheres. Scale bar: 100μm. C . Representative immunofluorescence staining against SARS-CoV-2 nucleocapsid (N) (red), epithelial marker EPCAM (green), Nkx2.1 (blue, left) and DAPI (blue, right) in alveolospheres with mock or SARS-CoV-2 infection (MOI 0.5, 24 hours). Scale bar: 100μm. D . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected d34 alveolospheres from two donors (MOI of 0.1 or 0.5, 24 hours). E . Dissociated alveolar cells after SARS-CoV-2 infection on day 34 are positive for SARS-CoV-2 N protein (red). Scale bar: 100μm. F . shRNA knock down of FURIN, ACE2, CD147 , and TMPRSS2 host genes, normalized to 18S levels and C1 alveolosphere (MOI 0.1, 24 hours). T-test, **p

    Journal: bioRxiv

    Article Title: Common genetic variation in humans impacts in vitro susceptibility to SARS-CoV-2 infection

    doi: 10.1101/2020.09.20.300574

    Figure Lengend Snippet: Infection of lung alveolospheres by SARS-CoV-2 in vitro A . Representative brightfield image of alveolosphere cultures on d30. 100μm. B . Baseline SARS-CoV-2 host gene expression in alveolospheres. Scale bar: 100μm. C . Representative immunofluorescence staining against SARS-CoV-2 nucleocapsid (N) (red), epithelial marker EPCAM (green), Nkx2.1 (blue, left) and DAPI (blue, right) in alveolospheres with mock or SARS-CoV-2 infection (MOI 0.5, 24 hours). Scale bar: 100μm. D . qPCR analysis of relative change in subgenomic vRNA N transcript in mock and SARS-CoV-2 infected d34 alveolospheres from two donors (MOI of 0.1 or 0.5, 24 hours). E . Dissociated alveolar cells after SARS-CoV-2 infection on day 34 are positive for SARS-CoV-2 N protein (red). Scale bar: 100μm. F . shRNA knock down of FURIN, ACE2, CD147 , and TMPRSS2 host genes, normalized to 18S levels and C1 alveolosphere (MOI 0.1, 24 hours). T-test, **p

    Article Snippet: Used shRNA against ACE2 (SHCLNG-NM_021804), CD147 (SHCLNG-NM_001728), TMPRSS2 (SHCLNG-NM_005656) were obtained from Sigma.

    Techniques: Infection, In Vitro, Expressing, Immunofluorescence, Staining, Marker, Real-time Polymerase Chain Reaction, shRNA

    Infection of neurons by SARS-CoV-2 in vitro . A . Expression of host genes associated with SARS-CoV-2 infection ( Gordon et al., 2020 ; Ou et al., 2020 ; Wruck and Adjaye, 2020 ) examined by RNA-sequencing (Log 2 RNA-seq, CPM medians) of post-mortem human prefrontal cortex (PFC), human induced pluripotent stem cells (hiPSCs), neural progenitor cells (NPCs) and four hiPSC-derived neuronal cell types: induced glutamatergic (GLUT), differentiated forebrain (FB) populations (comprised of glutamatergic neurons, GABAergic neurons and astrocytes), induced GABAergic (GABA) and induced dopaminergic (DOPA). B . Immunoblot showing ACE2, FURIN and CD147 protein in post-mortem human adult substantia nigra (SN) and PFC. C . Baseline host gene expression in d21 NGN2 -induced glutamatergic neurons, uninfected or infected with SARS-CoV-2 (MOI 0.5), normalized relative to alveolospheres, to ensure comparability across cell types. D . qPCR analysis of relative change in subgenomic vRNA N transcript and Interferon β (IFNβ) in mock and SARS-CoV-2 infected d21 NGN2 -induced glutamatergic neurons (MOI of 0.05, 24 hours). E . Representative immunostaining for SARS-CoV-2 nucleocapsid (N) protein (red), neuronal marker β-III-tubulin (green) and DAPI (blue) in d7 NGN2 -induced glutamatergic neurons infected with a SARS-CoV-2 (MOI of 0.05, 48 hours). Scale bar: 50μm F . Immunoblot against SARS-CoV-2 nucleocapsid (N) protein shows replication in NGN2 -induced glutamatergic neurons at a MOI of 1 after 24 hours. G . shRNA knock down of FURIN, ACE2, CD147 , and TMPRSS2 host genes, normalized to 18S levels and scrambled, in d7 NGN2 -induced glutamatergic neurons. T-test, **p

    Journal: bioRxiv

    Article Title: Common genetic variation in humans impacts in vitro susceptibility to SARS-CoV-2 infection

    doi: 10.1101/2020.09.20.300574

    Figure Lengend Snippet: Infection of neurons by SARS-CoV-2 in vitro . A . Expression of host genes associated with SARS-CoV-2 infection ( Gordon et al., 2020 ; Ou et al., 2020 ; Wruck and Adjaye, 2020 ) examined by RNA-sequencing (Log 2 RNA-seq, CPM medians) of post-mortem human prefrontal cortex (PFC), human induced pluripotent stem cells (hiPSCs), neural progenitor cells (NPCs) and four hiPSC-derived neuronal cell types: induced glutamatergic (GLUT), differentiated forebrain (FB) populations (comprised of glutamatergic neurons, GABAergic neurons and astrocytes), induced GABAergic (GABA) and induced dopaminergic (DOPA). B . Immunoblot showing ACE2, FURIN and CD147 protein in post-mortem human adult substantia nigra (SN) and PFC. C . Baseline host gene expression in d21 NGN2 -induced glutamatergic neurons, uninfected or infected with SARS-CoV-2 (MOI 0.5), normalized relative to alveolospheres, to ensure comparability across cell types. D . qPCR analysis of relative change in subgenomic vRNA N transcript and Interferon β (IFNβ) in mock and SARS-CoV-2 infected d21 NGN2 -induced glutamatergic neurons (MOI of 0.05, 24 hours). E . Representative immunostaining for SARS-CoV-2 nucleocapsid (N) protein (red), neuronal marker β-III-tubulin (green) and DAPI (blue) in d7 NGN2 -induced glutamatergic neurons infected with a SARS-CoV-2 (MOI of 0.05, 48 hours). Scale bar: 50μm F . Immunoblot against SARS-CoV-2 nucleocapsid (N) protein shows replication in NGN2 -induced glutamatergic neurons at a MOI of 1 after 24 hours. G . shRNA knock down of FURIN, ACE2, CD147 , and TMPRSS2 host genes, normalized to 18S levels and scrambled, in d7 NGN2 -induced glutamatergic neurons. T-test, **p

    Article Snippet: Used shRNA against ACE2 (SHCLNG-NM_021804), CD147 (SHCLNG-NM_001728), TMPRSS2 (SHCLNG-NM_005656) were obtained from Sigma.

    Techniques: Infection, In Vitro, Expressing, RNA Sequencing Assay, Derivative Assay, Real-time Polymerase Chain Reaction, Immunostaining, Marker, shRNA

    Analysis of tissue microarray cores for immunohistochemistry. A: Representative images from immunohistochemical staining of p-STAT3 nuclear expression (upper), Cyclin D1 nuclear expression (middle), CD147 cytoplasmic expression (lower) in human normal

    Journal: American Journal of Cancer Research

    Article Title: Inhibition of STAT3 reduces proliferation and invasion in salivary gland adenoid cystic carcinoma

    doi:

    Figure Lengend Snippet: Analysis of tissue microarray cores for immunohistochemistry. A: Representative images from immunohistochemical staining of p-STAT3 nuclear expression (upper), Cyclin D1 nuclear expression (middle), CD147 cytoplasmic expression (lower) in human normal

    Article Snippet: The following antibodies were used in this study: p-STAT3 (1:100), Cyclin D1 (1:100), Survivin (1:100), Slug (1:200) from Cell Signaling Technology, Inc., (Danvers, MA, USA), CD147 (1:100) from Proteintech Group, Inc. (Chicago, USA).

    Techniques: Microarray, Immunohistochemistry, Staining, Expressing

    Correlation and regression of p-STAT3 with CD147, Cyclin D1, Slug and Survivin in human AdCC. A: The expression of p-STAT3 had significant correlation with CD147 (p

    Journal: American Journal of Cancer Research

    Article Title: Inhibition of STAT3 reduces proliferation and invasion in salivary gland adenoid cystic carcinoma

    doi:

    Figure Lengend Snippet: Correlation and regression of p-STAT3 with CD147, Cyclin D1, Slug and Survivin in human AdCC. A: The expression of p-STAT3 had significant correlation with CD147 (p

    Article Snippet: The following antibodies were used in this study: p-STAT3 (1:100), Cyclin D1 (1:100), Survivin (1:100), Slug (1:200) from Cell Signaling Technology, Inc., (Danvers, MA, USA), CD147 (1:100) from Proteintech Group, Inc. (Chicago, USA).

    Techniques: Expressing