goat polyclonal antibody  (R&D Systems)

 
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    Name:
    Human EPCR Antibody
    Description:
    The Human EPCR Antibody from R D Systems is a goat polyclonal antibody to EPCR This antibody reacts with human The Human EPCR Antibody has been validated for the following applications Western Blot Flow Cytometry Immunohistochemistry CyTOF ready
    Catalog Number:
    af2245
    Price:
    369
    Applications:
    Western Blot, Flow Cytometry, Immunohistochemistry, CyTOF-ready
    Host:
    Goat
    Purity:
    Antigen Affinity-purified
    Conjugate:
    Unconjugated
    Immunogen:
    Mouse myeloma cell line NS0-derived recombinant human EPCR, Ser18-Ser210, Accession # Q9UNN8
    Size:
    100 ug
    Category:
    Primary Antibodies
    Isotype:
    IgG
    Buy from Supplier


    Structured Review

    R&D Systems goat polyclonal antibody
    Human EPCR Antibody
    The Human EPCR Antibody from R D Systems is a goat polyclonal antibody to EPCR This antibody reacts with human The Human EPCR Antibody has been validated for the following applications Western Blot Flow Cytometry Immunohistochemistry CyTOF ready
    https://www.bioz.com/result/goat polyclonal antibody/product/R&D Systems
    Average 94 stars, based on 49 article reviews
    Price from $9.99 to $1999.99
    goat polyclonal antibody - by Bioz Stars, 2021-01
    94/100 stars

    Images

    1) Product Images from "Infected erythrocytes expressing DC13 PfEMP1 differ from recombinant proteins in EPCR-binding function"

    Article Title: Infected erythrocytes expressing DC13 PfEMP1 differ from recombinant proteins in EPCR-binding function

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

    doi: 10.1073/pnas.1712879115

    DC8 IT4var19, but not DC13 HB3var03 and IT4var07, IE binding to the HBEC line HBEC-5i is reduced by EPCR siRNA knockdown. ( A ) Expression of EPCR on HBEC-5i by immunostaining and flow cytometry. HBEC-5i was transfected with EPCR siRNA (orange) or a negative control siRNA (blue). Forty-eight hours after transfection, HBEC-5i was stained with 1 μg/mL goat polyclonal antibody to EPCR (orange/blue) or goat IgG-negative control (red), followed by Alexa Fluor 488 donkey anti-goat IgG at a 1:1,500 dilution. Data shown are representative of four similar experiments. ( B – D ) Binding of IEs to HBEC-5i transfected with control siRNA or EPCR siRNA under static conditions. The data shown are the mean and SEM from four independent experiments. The difference in mean values compared with the siRNA control was analyzed by a two-tailed paired t test. * P
    Figure Legend Snippet: DC8 IT4var19, but not DC13 HB3var03 and IT4var07, IE binding to the HBEC line HBEC-5i is reduced by EPCR siRNA knockdown. ( A ) Expression of EPCR on HBEC-5i by immunostaining and flow cytometry. HBEC-5i was transfected with EPCR siRNA (orange) or a negative control siRNA (blue). Forty-eight hours after transfection, HBEC-5i was stained with 1 μg/mL goat polyclonal antibody to EPCR (orange/blue) or goat IgG-negative control (red), followed by Alexa Fluor 488 donkey anti-goat IgG at a 1:1,500 dilution. Data shown are representative of four similar experiments. ( B – D ) Binding of IEs to HBEC-5i transfected with control siRNA or EPCR siRNA under static conditions. The data shown are the mean and SEM from four independent experiments. The difference in mean values compared with the siRNA control was analyzed by a two-tailed paired t test. * P

    Techniques Used: Binding Assay, Expressing, Immunostaining, Flow Cytometry, Cytometry, Transfection, Negative Control, Staining, Two Tailed Test

    2) Product Images from "Primary Human Placental Trophoblasts are Permissive for Zika Virus (ZIKV) Replication"

    Article Title: Primary Human Placental Trophoblasts are Permissive for Zika Virus (ZIKV) Replication

    Journal: Scientific Reports

    doi: 10.1038/srep41389

    Putative ZIKV cell entry receptors are expressed in syncytialized primary human trophoblasts. ( A ) Select viral receptor targets were measured on day 5 post isolation. Cultured primary trophoblasts exhibit AXL, DC-SIGN, TYRO3 and TIM-1 , but not L-SIGN transcription as assessed by RT-PCR detection of human transcript message. Isolated reverse transcribed mRNA was amplified using intron/exon junction spanning primers with a GAPDH as a loading control. For DC SIGN and L- SIGN, primers were designed to capture the multiple transcript variants. Discovered major bands are shown comprising RefSeq transcript variant 1 for DC-SIGN, and transcript variants 1, 8, 9 and 10 (larger band), and variants 7 and 11 (smaller band) for L-SIGN. Isolated buffy coat, A549 cells, isolated primary human hepatocytes and whole human liver were used as controls. ( B ) Immunofluorescence labeling for the expression and cellular localization of the Axl presumptive ZIKV entry receptor. Representative images of day 5 uninfected trophoblasts were imaged following antibody probing with goat polyclonal antibody and Alexa Fluor ® 647 labeled anti-goat secondary antibody for detection (i). Z-stacks of 20X immunofluorescence images were deconvolved and maximum projected. Areas were abstracted (ii-iii) to visualize cellular localization at the cell membrane. Panel iii is indicated by the boxed area.
    Figure Legend Snippet: Putative ZIKV cell entry receptors are expressed in syncytialized primary human trophoblasts. ( A ) Select viral receptor targets were measured on day 5 post isolation. Cultured primary trophoblasts exhibit AXL, DC-SIGN, TYRO3 and TIM-1 , but not L-SIGN transcription as assessed by RT-PCR detection of human transcript message. Isolated reverse transcribed mRNA was amplified using intron/exon junction spanning primers with a GAPDH as a loading control. For DC SIGN and L- SIGN, primers were designed to capture the multiple transcript variants. Discovered major bands are shown comprising RefSeq transcript variant 1 for DC-SIGN, and transcript variants 1, 8, 9 and 10 (larger band), and variants 7 and 11 (smaller band) for L-SIGN. Isolated buffy coat, A549 cells, isolated primary human hepatocytes and whole human liver were used as controls. ( B ) Immunofluorescence labeling for the expression and cellular localization of the Axl presumptive ZIKV entry receptor. Representative images of day 5 uninfected trophoblasts were imaged following antibody probing with goat polyclonal antibody and Alexa Fluor ® 647 labeled anti-goat secondary antibody for detection (i). Z-stacks of 20X immunofluorescence images were deconvolved and maximum projected. Areas were abstracted (ii-iii) to visualize cellular localization at the cell membrane. Panel iii is indicated by the boxed area.

    Techniques Used: Isolation, Cell Culture, Reverse Transcription Polymerase Chain Reaction, Amplification, Variant Assay, Immunofluorescence, Labeling, Expressing

    3) Product Images from "The NKG2D-Activating Receptor Mediates Pulmonary Clearance of Pseudomonas aeruginosa"

    Article Title: The NKG2D-Activating Receptor Mediates Pulmonary Clearance of Pseudomonas aeruginosa

    Journal: Infection and Immunity

    doi: 10.1128/IAI.74.5.2578-2586.2006

    NKG2D ligands are induced in the lungs of mice infected with P. aeruginosa . (A) Western blot analysis of RAE-1 in whole lungs of mice exposed to ∼1 × 10 6 CFU of P. aeruginosa for 0, 8, and 24 h. The blot is representative of results obtained with four to six mice per group. (B to E) NKG2D ligand expression in lung epithelial cells and alveolar macrophages of mice exposed to ∼1 × 10 6 CFU of P. aeruginosa for 24 h. The accumulation of NKG2D ligands in the lungs of CF1 mice was assessed by immunohistochemistry analysis using paraffin-embedded sections and a goat polyclonal antibody against RAE-1γ. (B) Large airway of PBS-treated mouse. (C) Large airway of P. aeruginosa -infected mouse. (D) Lung parenchyma of PBS-treated mouse. (E) Lung parenchyma of P. aeruginosa -infected mouse. The photomicrographs are representative of five mice per group. Original magnification, ×400.
    Figure Legend Snippet: NKG2D ligands are induced in the lungs of mice infected with P. aeruginosa . (A) Western blot analysis of RAE-1 in whole lungs of mice exposed to ∼1 × 10 6 CFU of P. aeruginosa for 0, 8, and 24 h. The blot is representative of results obtained with four to six mice per group. (B to E) NKG2D ligand expression in lung epithelial cells and alveolar macrophages of mice exposed to ∼1 × 10 6 CFU of P. aeruginosa for 24 h. The accumulation of NKG2D ligands in the lungs of CF1 mice was assessed by immunohistochemistry analysis using paraffin-embedded sections and a goat polyclonal antibody against RAE-1γ. (B) Large airway of PBS-treated mouse. (C) Large airway of P. aeruginosa -infected mouse. (D) Lung parenchyma of PBS-treated mouse. (E) Lung parenchyma of P. aeruginosa -infected mouse. The photomicrographs are representative of five mice per group. Original magnification, ×400.

    Techniques Used: Mouse Assay, Infection, Western Blot, Expressing, Immunohistochemistry

    4) Product Images from "Kinetics of Innate Immune Response to Yersinia pestis after Intradermal Infection in a Mouse Model"

    Article Title: Kinetics of Innate Immune Response to Yersinia pestis after Intradermal Infection in a Mouse Model

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00606-12

    Immunohistochemical staining of superficial parotid lymph node sections. Sections were stained with antimyeloperoxidase antibody (brown color) to label neutrophils and a polyclonal anti- Yersinia pestis antibody (red color). Panels show the range in neutrophil response in animals infected with the attenuated pYV − strain at 24 (A and B) and 48 h (C and D) postinjection (A and C given a severity score [SS] of 2; B and D, SS of 3) compared with the PBS treatment (SS of 1) (E) and WT Y. pestis 195/P (SS of 2) (F) at 24 h p.i. The bottom two panels are examples at 48 h p.i. with wild-type Y. pestis in mice before the appearance of clinical disease (SS of 1) (G) and in moribund individuals (SS of 4) (H). Scale bar = 50 μm.
    Figure Legend Snippet: Immunohistochemical staining of superficial parotid lymph node sections. Sections were stained with antimyeloperoxidase antibody (brown color) to label neutrophils and a polyclonal anti- Yersinia pestis antibody (red color). Panels show the range in neutrophil response in animals infected with the attenuated pYV − strain at 24 (A and B) and 48 h (C and D) postinjection (A and C given a severity score [SS] of 2; B and D, SS of 3) compared with the PBS treatment (SS of 1) (E) and WT Y. pestis 195/P (SS of 2) (F) at 24 h p.i. The bottom two panels are examples at 48 h p.i. with wild-type Y. pestis in mice before the appearance of clinical disease (SS of 1) (G) and in moribund individuals (SS of 4) (H). Scale bar = 50 μm.

    Techniques Used: Immunohistochemistry, Staining, Infection, Mouse Assay

    Immunohistochemical staining of ear sections. Sections were stained with antimyeloperoxidase antibody (brown color) to label neutrophils and a polyclonal anti- Yersinia pestis antibody (red color). Panels show representative samples at 24 h after injection with PBS (severity score [SS] of 1) (A), E. coli LPS (SS of 2) (B), pYV − Y. pestis (SS of 2) (C), or WT Y. pestis 195/P (SS of 2) (D) and at 48 h postinjection with pYV − (SS of 3) (E), LPS (SS of 3) (F), or WT Y. pestis 195/P (G, H, and I). The bottom three panels show the variation in neutrophil response in mice infected with wild-type Y. pestis 195/P at 48 h, ranging from normal to mild (SS of 1) (G), moderate (SS of 2) (H), or severe (SS of 4) (I), with white arrows indicating examples of extensive bacterial growth. Scale bar = 50 μm.
    Figure Legend Snippet: Immunohistochemical staining of ear sections. Sections were stained with antimyeloperoxidase antibody (brown color) to label neutrophils and a polyclonal anti- Yersinia pestis antibody (red color). Panels show representative samples at 24 h after injection with PBS (severity score [SS] of 1) (A), E. coli LPS (SS of 2) (B), pYV − Y. pestis (SS of 2) (C), or WT Y. pestis 195/P (SS of 2) (D) and at 48 h postinjection with pYV − (SS of 3) (E), LPS (SS of 3) (F), or WT Y. pestis 195/P (G, H, and I). The bottom three panels show the variation in neutrophil response in mice infected with wild-type Y. pestis 195/P at 48 h, ranging from normal to mild (SS of 1) (G), moderate (SS of 2) (H), or severe (SS of 4) (I), with white arrows indicating examples of extensive bacterial growth. Scale bar = 50 μm.

    Techniques Used: Immunohistochemistry, Staining, Injection, Mouse Assay, Infection

    5) Product Images from "Infected erythrocytes expressing DC13 PfEMP1 differ from recombinant proteins in EPCR-binding function"

    Article Title: Infected erythrocytes expressing DC13 PfEMP1 differ from recombinant proteins in EPCR-binding function

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

    doi: 10.1073/pnas.1712879115

    DC8 IT4var19, but not DC13 HB3var03 and IT4var07, IE binding to the HBEC line HBEC-5i is reduced by EPCR siRNA knockdown. ( A ) Expression of EPCR on HBEC-5i by immunostaining and flow cytometry. HBEC-5i was transfected with EPCR siRNA (orange) or a negative control siRNA (blue). Forty-eight hours after transfection, HBEC-5i was stained with 1 μg/mL goat polyclonal antibody to EPCR (orange/blue) or goat IgG-negative control (red), followed by Alexa Fluor 488 donkey anti-goat IgG at a 1:1,500 dilution. Data shown are representative of four similar experiments. ( B – D ) Binding of IEs to HBEC-5i transfected with control siRNA or EPCR siRNA under static conditions. The data shown are the mean and SEM from four independent experiments. The difference in mean values compared with the siRNA control was analyzed by a two-tailed paired t test. * P
    Figure Legend Snippet: DC8 IT4var19, but not DC13 HB3var03 and IT4var07, IE binding to the HBEC line HBEC-5i is reduced by EPCR siRNA knockdown. ( A ) Expression of EPCR on HBEC-5i by immunostaining and flow cytometry. HBEC-5i was transfected with EPCR siRNA (orange) or a negative control siRNA (blue). Forty-eight hours after transfection, HBEC-5i was stained with 1 μg/mL goat polyclonal antibody to EPCR (orange/blue) or goat IgG-negative control (red), followed by Alexa Fluor 488 donkey anti-goat IgG at a 1:1,500 dilution. Data shown are representative of four similar experiments. ( B – D ) Binding of IEs to HBEC-5i transfected with control siRNA or EPCR siRNA under static conditions. The data shown are the mean and SEM from four independent experiments. The difference in mean values compared with the siRNA control was analyzed by a two-tailed paired t test. * P

    Techniques Used: Binding Assay, Expressing, Immunostaining, Flow Cytometry, Cytometry, Transfection, Negative Control, Staining, Two Tailed Test

    6) Product Images from "Preliminary Evidence on the Diagnostic and Molecular Role of Circulating Soluble EGFR in Non-Small Cell Lung Cancer"

    Article Title: Preliminary Evidence on the Diagnostic and Molecular Role of Circulating Soluble EGFR in Non-Small Cell Lung Cancer

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms160819612

    EGFR holoreceptor localization in lung tumor cells treated with sEGFR/EGF proteins. A549 and H1299 cell lines were untreated (NT) or treated with sEGFR (1 µg/mL) and EGF (100 ng/mL), alone and in combination (EGF + sEGFR), and EGFR holoreceptor localization was detected by using an immunofluorescent (IF) assay 24 h after treatment. Cells were treated with a polyclonal antibody against EGFR-ECD (Ab1_EGFR) and stained with FITC-conjugated anti-mouse secondary antibody (green). Cell nuclei were stained with DAPI (blue). Magnification: 40×. Scale bar: 20 µm.
    Figure Legend Snippet: EGFR holoreceptor localization in lung tumor cells treated with sEGFR/EGF proteins. A549 and H1299 cell lines were untreated (NT) or treated with sEGFR (1 µg/mL) and EGF (100 ng/mL), alone and in combination (EGF + sEGFR), and EGFR holoreceptor localization was detected by using an immunofluorescent (IF) assay 24 h after treatment. Cells were treated with a polyclonal antibody against EGFR-ECD (Ab1_EGFR) and stained with FITC-conjugated anti-mouse secondary antibody (green). Cell nuclei were stained with DAPI (blue). Magnification: 40×. Scale bar: 20 µm.

    Techniques Used: Staining

    7) Product Images from "Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro"

    Article Title: Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro

    Journal: Vaccine

    doi: 10.1016/j.vaccine.2006.08.011

    Immunogenicity of triSpike. Sera collected at indicated time points from vaccinated mice or hamsters were analyzed for reactivity with triSpike. (A) Western Blot analysis of pooled sera from immunized mice with or without alum adjuvant. Sera were collected and used at 1/1000 dilution against S-FLAG that was separated under conditions that allowed simultaneous detection of mono-, di-, and trimers of S-protein. A SARS patient serum (SARS), a rabbit serum against S1 and M2 monoclonal antibody against the FLAG peptide was used as control. FLAG-tagged bacterial alkaline phosphatase (BAP-FLAG) was used to assess the presence of antibodies against the FLAG tag. Immune complexes were detected with HRP-conjugated goat anti-mouse, -human or -rabbit IgG polyclonal antibody. Sizes of molecular weight markers are indicated on the right. (B) Reactivity of immune sera from pooled immunized hamster with live BHK-21 cells expressing S-protein at the plasma membrane using FACS analysis. Values were expressed as mean ± standard deviations. (C) Effect of alum adjuvant on longevity of neutralizing response in mouse sera against SARS-CoV (determined on FRhK-4 cells). Values were expressed as mean ± standard deviations. (D) Dose effect of triSpike immunization with alum adjuvant on neutralizing response against SARS-CoV in hamsters (determined on FRhK-4 cells). Values were expressed as mean ± standard deviations. (E) Inhibition of S-protein binding to ACE2 by sera from immunized mice. S-protein coated beads were pre-incubated with sera prior to incubation with soluble ACE2 (sACE2) and detection of the receptor was performed with a polyclonal goat-anti human ACE2 antibody. BAP-FLAG coated beads were used as control.
    Figure Legend Snippet: Immunogenicity of triSpike. Sera collected at indicated time points from vaccinated mice or hamsters were analyzed for reactivity with triSpike. (A) Western Blot analysis of pooled sera from immunized mice with or without alum adjuvant. Sera were collected and used at 1/1000 dilution against S-FLAG that was separated under conditions that allowed simultaneous detection of mono-, di-, and trimers of S-protein. A SARS patient serum (SARS), a rabbit serum against S1 and M2 monoclonal antibody against the FLAG peptide was used as control. FLAG-tagged bacterial alkaline phosphatase (BAP-FLAG) was used to assess the presence of antibodies against the FLAG tag. Immune complexes were detected with HRP-conjugated goat anti-mouse, -human or -rabbit IgG polyclonal antibody. Sizes of molecular weight markers are indicated on the right. (B) Reactivity of immune sera from pooled immunized hamster with live BHK-21 cells expressing S-protein at the plasma membrane using FACS analysis. Values were expressed as mean ± standard deviations. (C) Effect of alum adjuvant on longevity of neutralizing response in mouse sera against SARS-CoV (determined on FRhK-4 cells). Values were expressed as mean ± standard deviations. (D) Dose effect of triSpike immunization with alum adjuvant on neutralizing response against SARS-CoV in hamsters (determined on FRhK-4 cells). Values were expressed as mean ± standard deviations. (E) Inhibition of S-protein binding to ACE2 by sera from immunized mice. S-protein coated beads were pre-incubated with sera prior to incubation with soluble ACE2 (sACE2) and detection of the receptor was performed with a polyclonal goat-anti human ACE2 antibody. BAP-FLAG coated beads were used as control.

    Techniques Used: Mouse Assay, Western Blot, FLAG-tag, Molecular Weight, Expressing, FACS, Inhibition, Protein Binding, Incubation

    Induction of mucosal immune response in triSpike plus alum vaccinated mice. (A) Antibodies prepared from fecal samples collected at day 44 post-immunization were reacted against S-protein as described in Fig. 2 A. Immune complexes were detected with HRP-conjugated goat anti-mouse IgG or IgA polyclonal antibody. (B) Similar as (A) except that Western Blot analysis was performed with pooled nasal lavage samples collected at day 65. (C). Antibodies prepared from fecal samples of vaccinated mice were analyzed for neutralizing activity against SARS-CoV infection on FRhK-4 cells. Weak neutralizing activity was detected after the third immunization only. Asterisk (**) indicates the value of p
    Figure Legend Snippet: Induction of mucosal immune response in triSpike plus alum vaccinated mice. (A) Antibodies prepared from fecal samples collected at day 44 post-immunization were reacted against S-protein as described in Fig. 2 A. Immune complexes were detected with HRP-conjugated goat anti-mouse IgG or IgA polyclonal antibody. (B) Similar as (A) except that Western Blot analysis was performed with pooled nasal lavage samples collected at day 65. (C). Antibodies prepared from fecal samples of vaccinated mice were analyzed for neutralizing activity against SARS-CoV infection on FRhK-4 cells. Weak neutralizing activity was detected after the third immunization only. Asterisk (**) indicates the value of p

    Techniques Used: Mouse Assay, Western Blot, Activity Assay, Infection

    8) Product Images from "Blockade of BAFF Receptor BR3 on T cells Enhances Their Activation and Cytotoxicity"

    Article Title: Blockade of BAFF Receptor BR3 on T cells Enhances Their Activation and Cytotoxicity

    Journal: Journal of immunotherapy (Hagerstown, Md. : 1997)

    doi: 10.1097/CJI.0000000000000209

    CD25 Expression Increases with Anti-BR3 Blockade (A) Flow cytometric analysis of CD25 expression. Purified CD4+ and CD8+ T cells were incubated with goat polyclonal BR3, TACI, or BCMA specific neutralization antibodies or the goat IgG control and activated with plate-bound CD3/CD28 specific stimulatory antibodies for 24 hours. Anti-CD25 APC was used to detect CD25 expression which is gauged by percent positive CD25 cells. Five separate T cell donors were analyzed. (B) Flow cytometric analysis as for (A) measured by mean channel fluorescence of CD25. (C) Relative gene expression of CD25 using semi-quantitative PCR. Purified T cells from three healthy donors were incubated with either the anti-BR3 neutralization antibody or the goat IgG control and activated for 24 hours.
    Figure Legend Snippet: CD25 Expression Increases with Anti-BR3 Blockade (A) Flow cytometric analysis of CD25 expression. Purified CD4+ and CD8+ T cells were incubated with goat polyclonal BR3, TACI, or BCMA specific neutralization antibodies or the goat IgG control and activated with plate-bound CD3/CD28 specific stimulatory antibodies for 24 hours. Anti-CD25 APC was used to detect CD25 expression which is gauged by percent positive CD25 cells. Five separate T cell donors were analyzed. (B) Flow cytometric analysis as for (A) measured by mean channel fluorescence of CD25. (C) Relative gene expression of CD25 using semi-quantitative PCR. Purified T cells from three healthy donors were incubated with either the anti-BR3 neutralization antibody or the goat IgG control and activated for 24 hours.

    Techniques Used: Expressing, Flow Cytometry, Purification, Incubation, Neutralization, Fluorescence, Real-time Polymerase Chain Reaction

    9) Product Images from "KSHV downregulation of galectin-3 in Kaposi's sarcoma"

    Article Title: KSHV downregulation of galectin-3 in Kaposi's sarcoma

    Journal: Glycobiology

    doi: 10.1093/glycob/cwp204

    Galectin-3 expression in KSHV and mock treated cells at 10 days. ( A ) Dual labeled immunofluorescent staining of KSHV-infected and mock infected DMVEC. DMVEC were mock infected or infected with BCBL-1 virus at a moi 0.01 and cultivated in EBM-2 complete media. Uninfected DMVEC in chamber slides seeded at 2×10 5 cells/well were stained by IFA using a polyclonal goat antibody to human galectin-3 (R D Systems, AF1154) at a 1:100 dilution. Infected cells were dual labeled with a monoclonal antibody to KSHV LANA (LANA/ORF73, Vector Laboratory VP-H913) and a goat polyclonal antibody to galectin-3, both at 1:50 dilution, then labeled with donkey anti-mouse rhodamine tagged secondary antibody together with a rabbit anti-goat FITC tagged antibody as a mixture. Photographs were taken with a NIKON TE 2000S microscope at a total magnification of ×600. Shown in ( A ) are galectin-3 positive cells (green) with cytoplasmic and some nuclear staining. DAPI was used to stain nuclei. In ( A ), LANA-positive cells that were rhodamine stained and have a nuclear punctate pattern; galectin-3 positive cells were stained green with FITC. ( B ) Western blot analysis of galectin-3 protein expression in KSHV-infected DMVEC. Mock and KSHV-infected DMVEC lysates (15 µg) were electrophoresed in 4–20% PAGE gels, transferred to nitrocellulose membranes and then screened for expression of galectin-3 using a goat anti-human galectin-3 antibody (R D Systems) at a 1:2000 dilution. Proteins bands of ∼30 kDa showed much reduced levels of galectin-3 in lysates from KSHV-infected DMVEC, compared to the mock infected controls. Densitometry analysis revealed a 10-fold decrease in the amount of galectin-3 protein in DMVEC lysates from KSHV-infected cells. ( C ) RT-PCR analysis of galectin-3 mRNA expression in KSHV-infected DMVEC. Ten nanograms of cDNA from mock and KSHV-infected DMVEC were amplified by PCR using galectin-3 gene-specific primers in Exon 3. PCR products were electrophoresed in 1.5% agarose, and PCR DNA fragments were sized using a 100-bp ladder. The expected fragment size for galectin-3 is 256 bp. GAPDH was amplified as a loading control with a fragment size of 240 bp. ( D ) Real-time qPCR analysis of galectin-3 showing a 3.1-fold decrease in mRNA in KSHV-infected DMVEC cells relative to mock infected controls
    Figure Legend Snippet: Galectin-3 expression in KSHV and mock treated cells at 10 days. ( A ) Dual labeled immunofluorescent staining of KSHV-infected and mock infected DMVEC. DMVEC were mock infected or infected with BCBL-1 virus at a moi 0.01 and cultivated in EBM-2 complete media. Uninfected DMVEC in chamber slides seeded at 2×10 5 cells/well were stained by IFA using a polyclonal goat antibody to human galectin-3 (R D Systems, AF1154) at a 1:100 dilution. Infected cells were dual labeled with a monoclonal antibody to KSHV LANA (LANA/ORF73, Vector Laboratory VP-H913) and a goat polyclonal antibody to galectin-3, both at 1:50 dilution, then labeled with donkey anti-mouse rhodamine tagged secondary antibody together with a rabbit anti-goat FITC tagged antibody as a mixture. Photographs were taken with a NIKON TE 2000S microscope at a total magnification of ×600. Shown in ( A ) are galectin-3 positive cells (green) with cytoplasmic and some nuclear staining. DAPI was used to stain nuclei. In ( A ), LANA-positive cells that were rhodamine stained and have a nuclear punctate pattern; galectin-3 positive cells were stained green with FITC. ( B ) Western blot analysis of galectin-3 protein expression in KSHV-infected DMVEC. Mock and KSHV-infected DMVEC lysates (15 µg) were electrophoresed in 4–20% PAGE gels, transferred to nitrocellulose membranes and then screened for expression of galectin-3 using a goat anti-human galectin-3 antibody (R D Systems) at a 1:2000 dilution. Proteins bands of ∼30 kDa showed much reduced levels of galectin-3 in lysates from KSHV-infected DMVEC, compared to the mock infected controls. Densitometry analysis revealed a 10-fold decrease in the amount of galectin-3 protein in DMVEC lysates from KSHV-infected cells. ( C ) RT-PCR analysis of galectin-3 mRNA expression in KSHV-infected DMVEC. Ten nanograms of cDNA from mock and KSHV-infected DMVEC were amplified by PCR using galectin-3 gene-specific primers in Exon 3. PCR products were electrophoresed in 1.5% agarose, and PCR DNA fragments were sized using a 100-bp ladder. The expected fragment size for galectin-3 is 256 bp. GAPDH was amplified as a loading control with a fragment size of 240 bp. ( D ) Real-time qPCR analysis of galectin-3 showing a 3.1-fold decrease in mRNA in KSHV-infected DMVEC cells relative to mock infected controls

    Techniques Used: Expressing, Labeling, Staining, Infection, Immunofluorescence, Plasmid Preparation, Microscopy, Western Blot, Polyacrylamide Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Amplification, Polymerase Chain Reaction, Real-time Polymerase Chain Reaction

    10) Product Images from "KSHV downregulation of galectin-3 in Kaposi's sarcoma"

    Article Title: KSHV downregulation of galectin-3 in Kaposi's sarcoma

    Journal: Glycobiology

    doi: 10.1093/glycob/cwp204

    Galectin-3 expression in KSHV and mock treated cells at 10 days. ( A ) Dual labeled immunofluorescent staining of KSHV-infected and mock infected DMVEC. DMVEC were mock infected or infected with BCBL-1 virus at a moi 0.01 and cultivated in EBM-2 complete media. Uninfected DMVEC in chamber slides seeded at 2×10 5 cells/well were stained by IFA using a polyclonal goat antibody to human galectin-3 (R D Systems, AF1154) at a 1:100 dilution. Infected cells were dual labeled with a monoclonal antibody to KSHV LANA (LANA/ORF73, Vector Laboratory VP-H913) and a goat polyclonal antibody to galectin-3, both at 1:50 dilution, then labeled with donkey anti-mouse rhodamine tagged secondary antibody together with a rabbit anti-goat FITC tagged antibody as a mixture. Photographs were taken with a NIKON TE 2000S microscope at a total magnification of ×600. Shown in ( A ) are galectin-3 positive cells (green) with cytoplasmic and some nuclear staining. DAPI was used to stain nuclei. In ( A ), LANA-positive cells that were rhodamine stained and have a nuclear punctate pattern; galectin-3 positive cells were stained green with FITC. ( B ) Western blot analysis of galectin-3 protein expression in KSHV-infected DMVEC. Mock and KSHV-infected DMVEC lysates (15 µg) were electrophoresed in 4–20% PAGE gels, transferred to nitrocellulose membranes and then screened for expression of galectin-3 using a goat anti-human galectin-3 antibody (R D Systems) at a 1:2000 dilution. Proteins bands of ∼30 kDa showed much reduced levels of galectin-3 in lysates from KSHV-infected DMVEC, compared to the mock infected controls. Densitometry analysis revealed a 10-fold decrease in the amount of galectin-3 protein in DMVEC lysates from KSHV-infected cells. ( C ) RT-PCR analysis of galectin-3 mRNA expression in KSHV-infected DMVEC. Ten nanograms of cDNA from mock and KSHV-infected DMVEC were amplified by PCR using galectin-3 gene-specific primers in Exon 3. PCR products were electrophoresed in 1.5% agarose, and PCR DNA fragments were sized using a 100-bp ladder. The expected fragment size for galectin-3 is 256 bp. GAPDH was amplified as a loading control with a fragment size of 240 bp. ( D ) Real-time qPCR analysis of galectin-3 showing a 3.1-fold decrease in mRNA in KSHV-infected DMVEC cells relative to mock infected controls
    Figure Legend Snippet: Galectin-3 expression in KSHV and mock treated cells at 10 days. ( A ) Dual labeled immunofluorescent staining of KSHV-infected and mock infected DMVEC. DMVEC were mock infected or infected with BCBL-1 virus at a moi 0.01 and cultivated in EBM-2 complete media. Uninfected DMVEC in chamber slides seeded at 2×10 5 cells/well were stained by IFA using a polyclonal goat antibody to human galectin-3 (R D Systems, AF1154) at a 1:100 dilution. Infected cells were dual labeled with a monoclonal antibody to KSHV LANA (LANA/ORF73, Vector Laboratory VP-H913) and a goat polyclonal antibody to galectin-3, both at 1:50 dilution, then labeled with donkey anti-mouse rhodamine tagged secondary antibody together with a rabbit anti-goat FITC tagged antibody as a mixture. Photographs were taken with a NIKON TE 2000S microscope at a total magnification of ×600. Shown in ( A ) are galectin-3 positive cells (green) with cytoplasmic and some nuclear staining. DAPI was used to stain nuclei. In ( A ), LANA-positive cells that were rhodamine stained and have a nuclear punctate pattern; galectin-3 positive cells were stained green with FITC. ( B ) Western blot analysis of galectin-3 protein expression in KSHV-infected DMVEC. Mock and KSHV-infected DMVEC lysates (15 µg) were electrophoresed in 4–20% PAGE gels, transferred to nitrocellulose membranes and then screened for expression of galectin-3 using a goat anti-human galectin-3 antibody (R D Systems) at a 1:2000 dilution. Proteins bands of ∼30 kDa showed much reduced levels of galectin-3 in lysates from KSHV-infected DMVEC, compared to the mock infected controls. Densitometry analysis revealed a 10-fold decrease in the amount of galectin-3 protein in DMVEC lysates from KSHV-infected cells. ( C ) RT-PCR analysis of galectin-3 mRNA expression in KSHV-infected DMVEC. Ten nanograms of cDNA from mock and KSHV-infected DMVEC were amplified by PCR using galectin-3 gene-specific primers in Exon 3. PCR products were electrophoresed in 1.5% agarose, and PCR DNA fragments were sized using a 100-bp ladder. The expected fragment size for galectin-3 is 256 bp. GAPDH was amplified as a loading control with a fragment size of 240 bp. ( D ) Real-time qPCR analysis of galectin-3 showing a 3.1-fold decrease in mRNA in KSHV-infected DMVEC cells relative to mock infected controls

    Techniques Used: Expressing, Labeling, Staining, Infection, Immunofluorescence, Plasmid Preparation, Microscopy, Western Blot, Polyacrylamide Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Amplification, Polymerase Chain Reaction, Real-time Polymerase Chain Reaction

    11) Product Images from "Requirement for Intercellular Adhesion Molecule 1 and Caveolae in Invasion of Human Oral Epithelial Cells by Porphyromonas gingivalis"

    Article Title: Requirement for Intercellular Adhesion Molecule 1 and Caveolae in Invasion of Human Oral Epithelial Cells by Porphyromonas gingivalis

    Journal:

    doi: 10.1128/IAI.73.10.6290-6298.2005

    P. gingivalis fimbriae bind to ICAM-1. Binding was detected using rabbit polyclonal anti- P. gingivalis fimbria antibody, peroxidase-conjugated secondary antibody, and 3,3′,5,5′-tetramethylbenzidine substrate with enzyme-linked immunosorbent
    Figure Legend Snippet: P. gingivalis fimbriae bind to ICAM-1. Binding was detected using rabbit polyclonal anti- P. gingivalis fimbria antibody, peroxidase-conjugated secondary antibody, and 3,3′,5,5′-tetramethylbenzidine substrate with enzyme-linked immunosorbent

    Techniques Used: Binding Assay

    Inhibition of P. gingivalis invasion into KB cells by anti-ICAM-1 antibody. The cells were preincubated with or without either goat polyclonal anti-ICAM-1 antibody, goat polyclonal anti-E-cadherin antibody, or goat IgG at 37°C for 30 min as indicated,
    Figure Legend Snippet: Inhibition of P. gingivalis invasion into KB cells by anti-ICAM-1 antibody. The cells were preincubated with or without either goat polyclonal anti-ICAM-1 antibody, goat polyclonal anti-E-cadherin antibody, or goat IgG at 37°C for 30 min as indicated,

    Techniques Used: Inhibition

    12) Product Images from "Amyloid Precursor-like Protein 2 and Sortilin Do Not Regulate the PCSK9 Convertase-mediated Low Density Lipoprotein Receptor Degradation but Interact with Each Other *"

    Article Title: Amyloid Precursor-like Protein 2 and Sortilin Do Not Regulate the PCSK9 Convertase-mediated Low Density Lipoprotein Receptor Degradation but Interact with Each Other *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M115.647180

    Co-expression of sortilin, APLP2, or both with PCSK9 has no major effect on LDLR degradation. Huh7 cells were transfected with a total of 3 μg using 1 μg of each vector encoding for either a control protein 7B2 (−), sortilin (+), APLP2 (+), or PCSK9 (+), as indicated. After 48 h, lysates were analyzed by Western blotting for expression of the LDLR, sortilin-Myc, APLP2-V5, intracellular pro- and mature-PCSK9-V5, and β-actin. Media were analyzed for secreted endogenous and overexpressed PCSK9-V5 using a rabbit polyclonal human PCSK9 antibody. Quantification of LDLR expression was normalized against that of β-actin. These data are representative of at least 3 different experiments showing similar results.
    Figure Legend Snippet: Co-expression of sortilin, APLP2, or both with PCSK9 has no major effect on LDLR degradation. Huh7 cells were transfected with a total of 3 μg using 1 μg of each vector encoding for either a control protein 7B2 (−), sortilin (+), APLP2 (+), or PCSK9 (+), as indicated. After 48 h, lysates were analyzed by Western blotting for expression of the LDLR, sortilin-Myc, APLP2-V5, intracellular pro- and mature-PCSK9-V5, and β-actin. Media were analyzed for secreted endogenous and overexpressed PCSK9-V5 using a rabbit polyclonal human PCSK9 antibody. Quantification of LDLR expression was normalized against that of β-actin. These data are representative of at least 3 different experiments showing similar results.

    Techniques Used: Expressing, Transfection, Plasmid Preparation, Western Blot

    Related Articles

    Recombinant:

    Article Title: Soluble endothelial protein C receptor (sEPCR) is likely a biomarker of cancer-associated hypercoagulability in human hematologic malignancies
    Article Snippet: .. Antibodies and primers Primary antibody AF2245 against the EPCR (R & D Systems, Lille, France); biotinylated anti-goat IgG, streptavidin-fluorescein conjugate (Amersham, UK); human recombinant APC (Lilly, France); sEPCR and D-Di asserachrom (Stago, France). .. The PCR primers were designed with Primer 3 program, BLAST verified, and synthesized by Eurobio (Les Ulis, France).

    other:

    Article Title: An optimized isolation of biotinylated cell surface proteins reveals novel players in cancer metastasis
    Article Snippet: We used the following primary antibodies: anti-PROCR (anti-EPCR, AF2245, R & D Systems Inc. Minneapolis, USA), anti-CD109 (AF4385, R & D Systems Inc., Minneapolis, USA), anti-integrin-α6 (ITGA6, CD49f, BD Pharmingen™, Franklin Lakes, NJ, USA), anti-integrin-β1/CD29 (ITGB1, BAF1778, R & D Systems Inc., Minneapolis, USA), anti-Ecto-ADP-ribosyltransferase 3 (ART3, D01P, Abnova, Taipei City, Taiwan), anti-PTGFRN (s0523, Epitomics, Inc., California, USA and HPA017074, Prestige Antibodies®, Atlas Antibodies, Sweden), anti-Erk1/2 (p44/42 MAPK, 3A7, Cell Signaling Technology Inc., Danvers, MA, USA), anti-β-tubulin (BD Pharmingen™, Franklin Lakes, NJ, USA), anti-BiP (Cell Signaling Technology Inc., Danvers, MA, USA), anti-cytochromec oxidase (Complex IV subunit IV, 20E8C12, Invitrogen, Molecular Probes, Carlsbad, CA, USA) and anti-golgin 97 (CDF4, Invitrogen, Molecular Probes, Carlsbad, CA, USA).

    Immunostaining:

    Article Title: Endothelial protein C receptor is overexpressed in rheumatoid arthritic (RA) synovium and mediates the anti-inflammatory effects of activated protein C in RA monocytes
    Article Snippet: .. Tissue sections (4 μm) were de‐paraffinised and processed for immunostaining using goat antihuman EPCR antibody (2 μg/ml, R & D systems). .. Negative control samples were incubated with the same concentration of goat IgG.

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    R&D Systems goat anti human sod3 ec sod
    Over-expression of <t>EC-SOD</t> in the lung preserves the ability to learn in adult female mice exposed to neonatal hyperoxia. Novel object recognition testing was evaluated separately in female (A,B) and male (C,D) adult wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice that were exposed to room air (RA) or 100% oxygen (O 2 ) between postnatal days (PND) 0–4. A recognition index (A,C) based on the proportion of total time spent in contact with the novel object, as well as a time per approach index (B,D) based on the proportion of total time spent approaching the non-novel object were measured to assess learning. Neonatal hyperoxia significantly decreased recognition of the familiar object in female WT mice ( A , * P
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    R&D Systems human podocalyxin antibody
    <t>Podocalyxin</t> is a glycoprotein ligand of rBC2LCN. ( A ) Hydrophilic fractions (labeled as “ cells ”, 0.4 μg) and EVs (0.4 μg) of 201B7 hiPSCs were separated by SDS PAGE and detected by silver staining. Separated proteins were transferred to PVDF membranes and blotted with HRP-labeled rBC2LCN. ( B ) Hydrophilic fractions (labeled as “ cells” , 4 μg) and EVs of 201B7 hiPSCs (4 μg) were captured with anti-podocalyxin (αPod) or rBC2LCN and blotted with HRP-labeled rBC2LCN or HRP-labeled anti-podocalyxin.
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    R&D Systems goat anti mouse ifn γ neutralizing
    : In vivo neutralization of <t>IFN-γ.</t> BALB/c mice were immunized twice with 20 μg of G2Na or PBS in alum and challenged after 3 weeks. These mice were treated with control IgGs or anti-IFN-γ neutralizing antibody administered i.p. and i.n. as indicated in Materials and Methods. Five days after challenge, the mice were sacrificed. The results are expressed as means ± standard deviations of RSV titers measured in lungs and NTL, calculated from two experiments with 9 or 10 mice per group. ∗, P
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    R&D Systems anti il 10 antibody
    TGF-β and interleukin-10 <t>(IL-10)</t> synergistically suppress toll-like receptor-mediated humoral immune responses. (A) Histogram plots and percentages of CFSE-labeled B220 + B cells stimulated by 10 µg/ml lipopolysaccharides (LPS) either with or without 2 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 3 days ( n = 3). (B) Total IgG antibody titers in the supernatants of 3 µg/ml LPS-stimulated B cells either with 10 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 7 days were quantified by ELISA ( n = 3). (C) B cells were cultured under 200 ng/ml R848 and anti-IgM stimulation either with or without TGF-β1 or TGF-β3 for 7 days and total IgG antibody production was assessed by ELISA ( n = 3). (D) Total IgG antibody titer in the supernatants of B cells cultured with LPS and 25 ng/ml IL-6 (left) or 1 ng/ml IL-17 (right) either with TGF-β1 or TGF-β3 for 7 days ( n = 3). Data are representative of more than two independent experiments in (A–D) . (E) Serum anti-NP-bovine serum albumin (BSA) antibody titers from NP-LPS-immunized B6 mice treated with 300 µg anti-IL-10 antibody and 300 µg anti-TGF-β antibody were quantified by ELISA ( n = 9–10). (F,G) Anti-NP-BSA antibody titers from NP-KLH/CFA-immunized ( n = 11–16) (F) or NP-LPS-immunized ( n = 9–10) (G) mice with indicated pCAGGS plasmid vectors were quantified. P
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    Over-expression of EC-SOD in the lung preserves the ability to learn in adult female mice exposed to neonatal hyperoxia. Novel object recognition testing was evaluated separately in female (A,B) and male (C,D) adult wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice that were exposed to room air (RA) or 100% oxygen (O 2 ) between postnatal days (PND) 0–4. A recognition index (A,C) based on the proportion of total time spent in contact with the novel object, as well as a time per approach index (B,D) based on the proportion of total time spent approaching the non-novel object were measured to assess learning. Neonatal hyperoxia significantly decreased recognition of the familiar object in female WT mice ( A , * P

    Journal: Frontiers in Medicine

    Article Title: Lung-Specific Extracellular Superoxide Dismutase Improves Cognition of Adult Mice Exposed to Neonatal Hyperoxia

    doi: 10.3389/fmed.2018.00334

    Figure Lengend Snippet: Over-expression of EC-SOD in the lung preserves the ability to learn in adult female mice exposed to neonatal hyperoxia. Novel object recognition testing was evaluated separately in female (A,B) and male (C,D) adult wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice that were exposed to room air (RA) or 100% oxygen (O 2 ) between postnatal days (PND) 0–4. A recognition index (A,C) based on the proportion of total time spent in contact with the novel object, as well as a time per approach index (B,D) based on the proportion of total time spent approaching the non-novel object were measured to assess learning. Neonatal hyperoxia significantly decreased recognition of the familiar object in female WT mice ( A , * P

    Article Snippet: After blocking the membranes with 5% non-fat dry milk, they were incubated overnight with goat anti-mouse SOD3/EC-SOD (1:500 dilution; R & D Systems, Minneapolis, MN, United States), goat anti-human SOD3/EC-SOD (1:500 dilution; R & D Systems), or rabbit anti-mouse β-actin (1:1,000 dilution; Sigma, St. Louis, MO, United States) antibodies.

    Techniques: Over Expression, Mouse Assay, Transgenic Assay

    Over-expression of EC-SOD in the lung protects against hyperoxia-induced changes in neuronal morphology in CA1 and DG of the hippocampus. (A) Over-expression of EC-SOD has no effect on CA1 nuclear size in the CA1 field. Distribution and Gaussian curve fit of neuronal nuclear size in the CA1 field performed in room air-treated mice (WT, 72.80 μm 2 ± 11.04 vs. EC-SOD, 73.83 μm 2 ± 9.97; p = 0.74 for comparison of Gaussian curves). (B) Over-expression of EC-SOD in the lung blocks hyperoxia-induced nuclear shrinkage in exposed CA1 neurons (WT, 59.38 μm 2 ± 12.09 vs. EC-SOD, 65.23 μm 2 ± 14.06; **** p

    Journal: Frontiers in Medicine

    Article Title: Lung-Specific Extracellular Superoxide Dismutase Improves Cognition of Adult Mice Exposed to Neonatal Hyperoxia

    doi: 10.3389/fmed.2018.00334

    Figure Lengend Snippet: Over-expression of EC-SOD in the lung protects against hyperoxia-induced changes in neuronal morphology in CA1 and DG of the hippocampus. (A) Over-expression of EC-SOD has no effect on CA1 nuclear size in the CA1 field. Distribution and Gaussian curve fit of neuronal nuclear size in the CA1 field performed in room air-treated mice (WT, 72.80 μm 2 ± 11.04 vs. EC-SOD, 73.83 μm 2 ± 9.97; p = 0.74 for comparison of Gaussian curves). (B) Over-expression of EC-SOD in the lung blocks hyperoxia-induced nuclear shrinkage in exposed CA1 neurons (WT, 59.38 μm 2 ± 12.09 vs. EC-SOD, 65.23 μm 2 ± 14.06; **** p

    Article Snippet: After blocking the membranes with 5% non-fat dry milk, they were incubated overnight with goat anti-mouse SOD3/EC-SOD (1:500 dilution; R & D Systems, Minneapolis, MN, United States), goat anti-human SOD3/EC-SOD (1:500 dilution; R & D Systems), or rabbit anti-mouse β-actin (1:1,000 dilution; Sigma, St. Louis, MO, United States) antibodies.

    Techniques: Over Expression, Mouse Assay

    Human EC-SOD protein is detected in the lungs, but not brains, of transgenic Sftpc EC − SOD mice. Lung and brain tissues were harvested on postnatal day 4 and at 8 weeks of age from wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice birthed into room air. Lung and brain homogenates were immunoblotted with antibodies to detect human (h) EC-SOD, mouse (m) EC-SOD, and β-actin (loading control). Each lane represents an individual mouse.

    Journal: Frontiers in Medicine

    Article Title: Lung-Specific Extracellular Superoxide Dismutase Improves Cognition of Adult Mice Exposed to Neonatal Hyperoxia

    doi: 10.3389/fmed.2018.00334

    Figure Lengend Snippet: Human EC-SOD protein is detected in the lungs, but not brains, of transgenic Sftpc EC − SOD mice. Lung and brain tissues were harvested on postnatal day 4 and at 8 weeks of age from wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice birthed into room air. Lung and brain homogenates were immunoblotted with antibodies to detect human (h) EC-SOD, mouse (m) EC-SOD, and β-actin (loading control). Each lane represents an individual mouse.

    Article Snippet: After blocking the membranes with 5% non-fat dry milk, they were incubated overnight with goat anti-mouse SOD3/EC-SOD (1:500 dilution; R & D Systems, Minneapolis, MN, United States), goat anti-human SOD3/EC-SOD (1:500 dilution; R & D Systems), or rabbit anti-mouse β-actin (1:1,000 dilution; Sigma, St. Louis, MO, United States) antibodies.

    Techniques: Transgenic Assay, Mouse Assay

    Exposure to neonatal hyperoxia does not affect locomotor activity in adult mice. Locomotor activity testing was evaluated in adult (A) female and (B) male wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice (8–10 weeks of age) exposed to room air (RA) or 100% oxygen (O 2 ) during postnatal days (PND) 0–4. Jumps, vertical counts, ambulatory episodes, stereotypic counts, and resting time were quantified in three 60-min sessions occurring once per day on three consecutive days ( n = 9–10 mice per group, * P

    Journal: Frontiers in Medicine

    Article Title: Lung-Specific Extracellular Superoxide Dismutase Improves Cognition of Adult Mice Exposed to Neonatal Hyperoxia

    doi: 10.3389/fmed.2018.00334

    Figure Lengend Snippet: Exposure to neonatal hyperoxia does not affect locomotor activity in adult mice. Locomotor activity testing was evaluated in adult (A) female and (B) male wild type (WT) and Sftpc EC − SOD transgenic (Tg) mice (8–10 weeks of age) exposed to room air (RA) or 100% oxygen (O 2 ) during postnatal days (PND) 0–4. Jumps, vertical counts, ambulatory episodes, stereotypic counts, and resting time were quantified in three 60-min sessions occurring once per day on three consecutive days ( n = 9–10 mice per group, * P

    Article Snippet: After blocking the membranes with 5% non-fat dry milk, they were incubated overnight with goat anti-mouse SOD3/EC-SOD (1:500 dilution; R & D Systems, Minneapolis, MN, United States), goat anti-human SOD3/EC-SOD (1:500 dilution; R & D Systems), or rabbit anti-mouse β-actin (1:1,000 dilution; Sigma, St. Louis, MO, United States) antibodies.

    Techniques: Activity Assay, Mouse Assay, Transgenic Assay

    Over-expression of EC-SOD in the lung does not block hyperoxia-induced microglial priming in CA1 of the adult hippocampus. (A) CA1 field of the hippocampus showing neuronal nuclei, Iba1 + microglia, and GFAP + astrocytes. Scale bar = 200 μm. (B) Neonatal hyperoxia stimulates Iba1 expression in both WT and EC-SOD mice; * P

    Journal: Frontiers in Medicine

    Article Title: Lung-Specific Extracellular Superoxide Dismutase Improves Cognition of Adult Mice Exposed to Neonatal Hyperoxia

    doi: 10.3389/fmed.2018.00334

    Figure Lengend Snippet: Over-expression of EC-SOD in the lung does not block hyperoxia-induced microglial priming in CA1 of the adult hippocampus. (A) CA1 field of the hippocampus showing neuronal nuclei, Iba1 + microglia, and GFAP + astrocytes. Scale bar = 200 μm. (B) Neonatal hyperoxia stimulates Iba1 expression in both WT and EC-SOD mice; * P

    Article Snippet: After blocking the membranes with 5% non-fat dry milk, they were incubated overnight with goat anti-mouse SOD3/EC-SOD (1:500 dilution; R & D Systems, Minneapolis, MN, United States), goat anti-human SOD3/EC-SOD (1:500 dilution; R & D Systems), or rabbit anti-mouse β-actin (1:1,000 dilution; Sigma, St. Louis, MO, United States) antibodies.

    Techniques: Over Expression, Blocking Assay, Expressing, Mouse Assay

    Podocalyxin is a glycoprotein ligand of rBC2LCN. ( A ) Hydrophilic fractions (labeled as “ cells ”, 0.4 μg) and EVs (0.4 μg) of 201B7 hiPSCs were separated by SDS PAGE and detected by silver staining. Separated proteins were transferred to PVDF membranes and blotted with HRP-labeled rBC2LCN. ( B ) Hydrophilic fractions (labeled as “ cells” , 4 μg) and EVs of 201B7 hiPSCs (4 μg) were captured with anti-podocalyxin (αPod) or rBC2LCN and blotted with HRP-labeled rBC2LCN or HRP-labeled anti-podocalyxin.

    Journal: Scientific Reports

    Article Title: Glycome analysis of extracellular vesicles derived from human induced pluripotent stem cells using lectin microarray

    doi: 10.1038/s41598-018-22450-2

    Figure Lengend Snippet: Podocalyxin is a glycoprotein ligand of rBC2LCN. ( A ) Hydrophilic fractions (labeled as “ cells ”, 0.4 μg) and EVs (0.4 μg) of 201B7 hiPSCs were separated by SDS PAGE and detected by silver staining. Separated proteins were transferred to PVDF membranes and blotted with HRP-labeled rBC2LCN. ( B ) Hydrophilic fractions (labeled as “ cells” , 4 μg) and EVs of 201B7 hiPSCs (4 μg) were captured with anti-podocalyxin (αPod) or rBC2LCN and blotted with HRP-labeled rBC2LCN or HRP-labeled anti-podocalyxin.

    Article Snippet: The beads were also incubated with a 100-fold dilution of anti-CD9 antibody (clone#: 12A12, SHI-EXO-M01, COSMO BIO Co. Ltd.), a 100-fold dilution of anti-CD63 (Clone#: 8A12, Cat#: SHI-EXO-M02, COSMO BIO Co. Ltd.), anti-podocalyxin goat pAb (Cat#: AF1658, R & D Systems, Inc., Minneapolis, MN), a 100-fold dilution of anti-SSEA4 (clone#: MC-813-70, Cat#: MAB4304, Merck KGaA), anti-TRA1-60 (clone#: TRA-1-60, Cat#: MAB4360, Merck KGaA), or R-10G (Clone#: R-10G, Cat#: 011-25811, Wako Pure Chemical Industries, Ltd.) followed by R-phycoerythrin (PE)-conjugated AffiniPure Donkey Anti-Goat IgG (H+L) (Cat#: 705-115-147, Jackson ImmunoResearch Inc.,) or PE-Goat Anti-Mouse IgG (Cat#: 550589, BD).

    Techniques: Labeling, SDS Page, Silver Staining

    Flow cytometry analysis. ( A ) Expression of exosome markers (CD9 and CD63) and hiPSC markers [rBC2LCN, TRA-1-60, SSEA4, R-10G, podocalyxin (Pod)] on EVs and cells. ( B ) Correlation between marker expression of cells (y-axis) and EVs (x-axis).

    Journal: Scientific Reports

    Article Title: Glycome analysis of extracellular vesicles derived from human induced pluripotent stem cells using lectin microarray

    doi: 10.1038/s41598-018-22450-2

    Figure Lengend Snippet: Flow cytometry analysis. ( A ) Expression of exosome markers (CD9 and CD63) and hiPSC markers [rBC2LCN, TRA-1-60, SSEA4, R-10G, podocalyxin (Pod)] on EVs and cells. ( B ) Correlation between marker expression of cells (y-axis) and EVs (x-axis).

    Article Snippet: The beads were also incubated with a 100-fold dilution of anti-CD9 antibody (clone#: 12A12, SHI-EXO-M01, COSMO BIO Co. Ltd.), a 100-fold dilution of anti-CD63 (Clone#: 8A12, Cat#: SHI-EXO-M02, COSMO BIO Co. Ltd.), anti-podocalyxin goat pAb (Cat#: AF1658, R & D Systems, Inc., Minneapolis, MN), a 100-fold dilution of anti-SSEA4 (clone#: MC-813-70, Cat#: MAB4304, Merck KGaA), anti-TRA1-60 (clone#: TRA-1-60, Cat#: MAB4360, Merck KGaA), or R-10G (Clone#: R-10G, Cat#: 011-25811, Wako Pure Chemical Industries, Ltd.) followed by R-phycoerythrin (PE)-conjugated AffiniPure Donkey Anti-Goat IgG (H+L) (Cat#: 705-115-147, Jackson ImmunoResearch Inc.,) or PE-Goat Anti-Mouse IgG (Cat#: 550589, BD).

    Techniques: Flow Cytometry, Cytometry, Expressing, Marker

    : In vivo neutralization of IFN-γ. BALB/c mice were immunized twice with 20 μg of G2Na or PBS in alum and challenged after 3 weeks. These mice were treated with control IgGs or anti-IFN-γ neutralizing antibody administered i.p. and i.n. as indicated in Materials and Methods. Five days after challenge, the mice were sacrificed. The results are expressed as means ± standard deviations of RSV titers measured in lungs and NTL, calculated from two experiments with 9 or 10 mice per group. ∗, P

    Journal: Journal of Virology

    Article Title: Gamma Interferon-Dependent Protection of the Mouse Upper Respiratory Tract following Parenteral Immunization with a Respiratory Syncytial Virus G Protein Fragment

    doi: 10.1128/JVI.76.20.10203-10210.2002

    Figure Lengend Snippet: : In vivo neutralization of IFN-γ. BALB/c mice were immunized twice with 20 μg of G2Na or PBS in alum and challenged after 3 weeks. These mice were treated with control IgGs or anti-IFN-γ neutralizing antibody administered i.p. and i.n. as indicated in Materials and Methods. Five days after challenge, the mice were sacrificed. The results are expressed as means ± standard deviations of RSV titers measured in lungs and NTL, calculated from two experiments with 9 or 10 mice per group. ∗, P

    Article Snippet: In vivo neutralization of IFN-γ was performed on the same day as the RSV challenge by one i.p. injection (per mouse) of 100 μg of goat anti-mouse IFN-γ-neutralizing or control IgG Abs (AF-485-NA and AB-108C, respectively; R & D Systems) diluted in 200 μl of PBS, followed for 2 days by daily i.n. administrations of 10 μg in 20 μl.

    Techniques: In Vivo, Neutralization, Mouse Assay

    TGF-β and interleukin-10 (IL-10) synergistically suppress toll-like receptor-mediated humoral immune responses. (A) Histogram plots and percentages of CFSE-labeled B220 + B cells stimulated by 10 µg/ml lipopolysaccharides (LPS) either with or without 2 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 3 days ( n = 3). (B) Total IgG antibody titers in the supernatants of 3 µg/ml LPS-stimulated B cells either with 10 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 7 days were quantified by ELISA ( n = 3). (C) B cells were cultured under 200 ng/ml R848 and anti-IgM stimulation either with or without TGF-β1 or TGF-β3 for 7 days and total IgG antibody production was assessed by ELISA ( n = 3). (D) Total IgG antibody titer in the supernatants of B cells cultured with LPS and 25 ng/ml IL-6 (left) or 1 ng/ml IL-17 (right) either with TGF-β1 or TGF-β3 for 7 days ( n = 3). Data are representative of more than two independent experiments in (A–D) . (E) Serum anti-NP-bovine serum albumin (BSA) antibody titers from NP-LPS-immunized B6 mice treated with 300 µg anti-IL-10 antibody and 300 µg anti-TGF-β antibody were quantified by ELISA ( n = 9–10). (F,G) Anti-NP-BSA antibody titers from NP-KLH/CFA-immunized ( n = 11–16) (F) or NP-LPS-immunized ( n = 9–10) (G) mice with indicated pCAGGS plasmid vectors were quantified. P

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β and Interleukin-10 Synergistically Regulate Humoral Immunity via Modulating Metabolic Signals

    doi: 10.3389/fimmu.2018.01364

    Figure Lengend Snippet: TGF-β and interleukin-10 (IL-10) synergistically suppress toll-like receptor-mediated humoral immune responses. (A) Histogram plots and percentages of CFSE-labeled B220 + B cells stimulated by 10 µg/ml lipopolysaccharides (LPS) either with or without 2 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 3 days ( n = 3). (B) Total IgG antibody titers in the supernatants of 3 µg/ml LPS-stimulated B cells either with 10 ng/ml TGF-β1, TGF-β3, and/or 50 ng/ml IL-10 for 7 days were quantified by ELISA ( n = 3). (C) B cells were cultured under 200 ng/ml R848 and anti-IgM stimulation either with or without TGF-β1 or TGF-β3 for 7 days and total IgG antibody production was assessed by ELISA ( n = 3). (D) Total IgG antibody titer in the supernatants of B cells cultured with LPS and 25 ng/ml IL-6 (left) or 1 ng/ml IL-17 (right) either with TGF-β1 or TGF-β3 for 7 days ( n = 3). Data are representative of more than two independent experiments in (A–D) . (E) Serum anti-NP-bovine serum albumin (BSA) antibody titers from NP-LPS-immunized B6 mice treated with 300 µg anti-IL-10 antibody and 300 µg anti-TGF-β antibody were quantified by ELISA ( n = 9–10). (F,G) Anti-NP-BSA antibody titers from NP-KLH/CFA-immunized ( n = 11–16) (F) or NP-LPS-immunized ( n = 9–10) (G) mice with indicated pCAGGS plasmid vectors were quantified. P

    Article Snippet: For example, elevated levels of serum IL-10 correlate with disease activity of SLE ( ) and anti-IL-10 antibody exhibits therapeutic effects in SLE ( ).

    Techniques: Labeling, Enzyme-linked Immunosorbent Assay, Cell Culture, Mouse Assay, Plasmid Preparation

    TGF-β3 exerts therapeutic effects in mouse models of lupus under the presence of interleukin-10 (IL-10). (A) Indicated pCAGGS vectors were i.v. administered every 2 weeks to BALB/c mice treated with 1.25 mg imiquimod epicutaneously three times weekly. Serum anti-dsDNA antibody titers were quantified by ELISA ( n = 12). (B) Serum IL-10 levels in 8- to 16-week-old MRL/+ and MRL/ lpr mice were analyzed by ELISA ( n = 3). (C–G) MRL/ lpr mice treated with indicated pCAGGS vectors every 4 weeks were analyzed at an age of 21 weeks. Serum anti-dsDNA antibody levels (C) , gross appearances and weights of spleens (D) ( n = 12–18), and chronological proteinuria progression (E) ( n = 12–25). Flow cytometric quantification of CXCR5 + PD-1 + T FH cells (F) and B220 + CD138 + plasmablasts (G) ( n = 12–18). P

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β and Interleukin-10 Synergistically Regulate Humoral Immunity via Modulating Metabolic Signals

    doi: 10.3389/fimmu.2018.01364

    Figure Lengend Snippet: TGF-β3 exerts therapeutic effects in mouse models of lupus under the presence of interleukin-10 (IL-10). (A) Indicated pCAGGS vectors were i.v. administered every 2 weeks to BALB/c mice treated with 1.25 mg imiquimod epicutaneously three times weekly. Serum anti-dsDNA antibody titers were quantified by ELISA ( n = 12). (B) Serum IL-10 levels in 8- to 16-week-old MRL/+ and MRL/ lpr mice were analyzed by ELISA ( n = 3). (C–G) MRL/ lpr mice treated with indicated pCAGGS vectors every 4 weeks were analyzed at an age of 21 weeks. Serum anti-dsDNA antibody levels (C) , gross appearances and weights of spleens (D) ( n = 12–18), and chronological proteinuria progression (E) ( n = 12–25). Flow cytometric quantification of CXCR5 + PD-1 + T FH cells (F) and B220 + CD138 + plasmablasts (G) ( n = 12–18). P

    Article Snippet: For example, elevated levels of serum IL-10 correlate with disease activity of SLE ( ) and anti-IL-10 antibody exhibits therapeutic effects in SLE ( ).

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay, Flow Cytometry

    Cytokine synergy of TGF-β3 and interleukin-10 (IL-10) modulate transcriptional programs in lipopolysaccharide (LPS)-stimulated B cells. (A) Heatmap visualization and hierarchical clustering analysis of differentially expressed genes of whole genome RNA-sequencing from B220 + 7-AAD − B cells stimulated by LPS with either TGF-β3 and/or IL-10 for 3 days. The clustered genes were subdivided into 16 categories labeled by different colors. (B,C) qRT-PCR analysis of genes downregulated (B) or upregulated (C) with TGF-β3 and IL-10 more than those in LPS-stimulated B cells ( n = 3). P

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β and Interleukin-10 Synergistically Regulate Humoral Immunity via Modulating Metabolic Signals

    doi: 10.3389/fimmu.2018.01364

    Figure Lengend Snippet: Cytokine synergy of TGF-β3 and interleukin-10 (IL-10) modulate transcriptional programs in lipopolysaccharide (LPS)-stimulated B cells. (A) Heatmap visualization and hierarchical clustering analysis of differentially expressed genes of whole genome RNA-sequencing from B220 + 7-AAD − B cells stimulated by LPS with either TGF-β3 and/or IL-10 for 3 days. The clustered genes were subdivided into 16 categories labeled by different colors. (B,C) qRT-PCR analysis of genes downregulated (B) or upregulated (C) with TGF-β3 and IL-10 more than those in LPS-stimulated B cells ( n = 3). P

    Article Snippet: For example, elevated levels of serum IL-10 correlate with disease activity of SLE ( ) and anti-IL-10 antibody exhibits therapeutic effects in SLE ( ).

    Techniques: RNA Sequencing Assay, Labeling, Quantitative RT-PCR

    TGF-β regulates T cell-dependent B cell activation. (A) Histogram plots of CFSE-labeled B220 + B cells stimulated by 10 µg/ml anti-CD40 and 10 µg/ml anti-IgM either with TGF-β1 or TGF-β3 for 3 days ( n = 3). Data are representative histograms with CFSE fluorescence gated on B220 + cells and the percentage of proliferating B220 + CFSE − cells. (B) Total IgG and IgA antibody titers in the supernatants of anti-CD40/IL-4 stimulated B cells with either TGF-β1 or TGF-β3 and 50 ng/ml interleukin-10 for 7 days quantified by ELISA ( n = 3). (C) Flow cytometry analyzing the expression of B220 and CD138 in B cells stimulated with anti-CD40/anti-IgM either with or without TGF-β1 or TGF-β3 for 3 days (left), and quantification of B220 + CD138 + plasmablasts (right) ( n = 3). Data are representative of three independent experiments in (A–C) . (D) C57BL/6 (B6) mice treated with indicated pCAGGS plasmid vectors were by i.p. injection of 100 µg NP-KLH in alum. Anti-NP-bovine serum albumin antibody titers in the sera ( n = 16) were quantified by ELISA 7 days after the immunization. (E) Flow cytometric (FCM) plots and quantification of GL-7 + Fas + germinal center B cells in B220 + cells from B6 mice administered the indicated pCAGGS vectors and immunized with 100 µg NP-KLH in alum ( n = 13–14). P

    Journal: Frontiers in Immunology

    Article Title: Transforming Growth Factor-β and Interleukin-10 Synergistically Regulate Humoral Immunity via Modulating Metabolic Signals

    doi: 10.3389/fimmu.2018.01364

    Figure Lengend Snippet: TGF-β regulates T cell-dependent B cell activation. (A) Histogram plots of CFSE-labeled B220 + B cells stimulated by 10 µg/ml anti-CD40 and 10 µg/ml anti-IgM either with TGF-β1 or TGF-β3 for 3 days ( n = 3). Data are representative histograms with CFSE fluorescence gated on B220 + cells and the percentage of proliferating B220 + CFSE − cells. (B) Total IgG and IgA antibody titers in the supernatants of anti-CD40/IL-4 stimulated B cells with either TGF-β1 or TGF-β3 and 50 ng/ml interleukin-10 for 7 days quantified by ELISA ( n = 3). (C) Flow cytometry analyzing the expression of B220 and CD138 in B cells stimulated with anti-CD40/anti-IgM either with or without TGF-β1 or TGF-β3 for 3 days (left), and quantification of B220 + CD138 + plasmablasts (right) ( n = 3). Data are representative of three independent experiments in (A–C) . (D) C57BL/6 (B6) mice treated with indicated pCAGGS plasmid vectors were by i.p. injection of 100 µg NP-KLH in alum. Anti-NP-bovine serum albumin antibody titers in the sera ( n = 16) were quantified by ELISA 7 days after the immunization. (E) Flow cytometric (FCM) plots and quantification of GL-7 + Fas + germinal center B cells in B220 + cells from B6 mice administered the indicated pCAGGS vectors and immunized with 100 µg NP-KLH in alum ( n = 13–14). P

    Article Snippet: For example, elevated levels of serum IL-10 correlate with disease activity of SLE ( ) and anti-IL-10 antibody exhibits therapeutic effects in SLE ( ).

    Techniques: Activation Assay, Labeling, Fluorescence, Enzyme-linked Immunosorbent Assay, Flow Cytometry, Cytometry, Expressing, Mouse Assay, Plasmid Preparation, Injection