Review

mouse mab anti cd55 (R&D Systems)

R&D Systems is a verified supplier

R&D Systems manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

R&D Systems mouse mab anti cd55
FIGURE 1 Expression of the novel construct MAP-2:CD551-4. (A) Graphical representation of MAP-2 and MAP-2:CD551-4. (B–D) Western immunoblotting of the purified protein MAP-2:CD551-4 probed with mAb anti-MASP-2/Map19 (B), mAb <t>anti-CD55</t> (C), and mAb anti-FLAG tag (D). rMAP-2 and rCD551-4 produced in-house were used as controls. (E) Direct protein stain of the same purified proteins.

FIGURE 1 Expression of the novel construct MAP-2:CD551-4. (A) Graphical representation of MAP-2 and MAP-2:CD551-4. (B–D) Western immunoblotting of the purified protein MAP-2:CD551-4 probed with mAb anti-MASP-2/Map19 (B), mAb <t>anti-CD55</t> (C), and mAb anti-FLAG tag (D). rMAP-2 and rCD551-4 produced in-house were used as controls. (E) Direct protein stain of the same purified proteins.

Mouse Mab Anti Cd55, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse mab anti cd55/product/R&D Systems
Average 92 stars, based on 6 article reviews

mouse mab anti cd55 - by Bioz Stars, 2026-06

92/100 stars

Images

1) Product Images from "MAP‐2:CD55 chimeric construct effectively modulates complement activation"

Article Title: MAP‐2:CD55 chimeric construct effectively modulates complement activation

Journal: The FASEB Journal

doi: 10.1096/fj.202300571r

Figure Legend Snippet: FIGURE 1 Expression of the novel construct MAP-2:CD551-4. (A) Graphical representation of MAP-2 and MAP-2:CD551-4. (B–D) Western immunoblotting of the purified protein MAP-2:CD551-4 probed with mAb anti-MASP-2/Map19 (B), mAb anti-CD55 (C), and mAb anti-FLAG tag (D). rMAP-2 and rCD551-4 produced in-house were used as controls. (E) Direct protein stain of the same purified proteins.

Techniques Used: Expressing, Construct, Western Blot, Purification, FLAG-tag, Produced, Staining

$FIGURE 2 Structural characterization of MAP-2:CD551-4. (A) MAP-2:CD551-4 elution profile from size exclusion chromatography exposed to 2 mM of calcium, 10 mM EDTA, or 10 mM EGTA. Vertical lines represent the molecular weight of the molecular marker, represented in kDa. (B–D) Western immunoblotting of the elution fractions 3–16 of MAP-2 from SEC exposed to 2.5 mM of calcium (B), 10 mM EDTA (C), or 10 mM EGTA (D). MAb anti MASP-2/Map19 clone 6G12 was used to detect MAP-2:CD551-4. Representative blots out of 3 independent replicates are shown. (E and F) Thermal stability of MAP-2, CD55, and MAP-2:CD551-4 exposed to 2 mM calcium or 10 mM EGTA shown as the ratio of the intrinsic fluorescence at 350 and 330 nm (E) and the right the first derivative of the ratio (F). Thermal stability was performed in triplicates.$
Figure Legend Snippet: FIGURE 2 Structural characterization of MAP-2:CD551-4. (A) MAP-2:CD551-4 elution profile from size exclusion chromatography exposed to 2 mM of calcium, 10 mM EDTA, or 10 mM EGTA. Vertical lines represent the molecular weight of the molecular marker, represented in kDa. (B–D) Western immunoblotting of the elution fractions 3–16 of MAP-2 from SEC exposed to 2.5 mM of calcium (B), 10 mM EDTA (C), or 10 mM EGTA (D). MAb anti MASP-2/Map19 clone 6G12 was used to detect MAP-2:CD551-4. Representative blots out of 3 independent replicates are shown. (E and F) Thermal stability of MAP-2, CD55, and MAP-2:CD551-4 exposed to 2 mM calcium or 10 mM EGTA shown as the ratio of the intrinsic fluorescence at 350 and 330 nm (E) and the right the first derivative of the ratio (F). Thermal stability was performed in triplicates.

Techniques Used: Size-exclusion Chromatography, Molecular Weight, Marker, Western Blot, Fluorescence

Image Search Results

Gene identity, NCBI accession number, and primer sequences of the primers used for the real time PCR.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Gene identity, NCBI accession number, and primer sequences of the primers used for the real time PCR.

Article Snippet: The rabbit and mouse monoclonal antibodies against CD55 and CD46 used in flow cytometry experiments, and the recombinant CD55 and CD46 were sourced from Sino Biological Inc. (Beijing, China).

Techniques: Amplification

Levels of complement-regulatory protein CD55 remain unaltered, but CD46 levels decline in HeLa cells infected with vesicular stomatitis virus. ( A – G ) Whole cell lysates collected from mock- and VSV-infected HeLa cells at the indicated time points were subjected to immunoblotting to determine the expression of CD46 and CD55. Samples at the time point 0–3 h ( A ), 4–7 h ( B ), 8–11 h ( C ), 12–15 h ( D ), 16–18 h ( E ), 19–21 h ( F ) and 22–24 h ( G ), respectively. Anti-CD55 and CD46 antibodies were used to detect the levels of the corresponding proteins in the lysate at different time points. Virus infectivity was detected using a VSV anti-M antibody while actin served as the loading control. The levels of CD55 were maintained at all of the time points tested compared to the mock; however, the levels of CD46 declined significantly, starting from 15 h onwards (note the decreasing levels of CD46 in D , E , and the complete absence in F , G ). The entire panel of blots is representative of three independent experiments. ( H ) The densitometry analysis of the CD55 and CD46 protein expression, normalized against the loading control. The data represents the mean + SEM of the three independent experiments.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Levels of complement-regulatory protein CD55 remain unaltered, but CD46 levels decline in HeLa cells infected with vesicular stomatitis virus. ( A – G ) Whole cell lysates collected from mock- and VSV-infected HeLa cells at the indicated time points were subjected to immunoblotting to determine the expression of CD46 and CD55. Samples at the time point 0–3 h ( A ), 4–7 h ( B ), 8–11 h ( C ), 12–15 h ( D ), 16–18 h ( E ), 19–21 h ( F ) and 22–24 h ( G ), respectively. Anti-CD55 and CD46 antibodies were used to detect the levels of the corresponding proteins in the lysate at different time points. Virus infectivity was detected using a VSV anti-M antibody while actin served as the loading control. The levels of CD55 were maintained at all of the time points tested compared to the mock; however, the levels of CD46 declined significantly, starting from 15 h onwards (note the decreasing levels of CD46 in D , E , and the complete absence in F , G ). The entire panel of blots is representative of three independent experiments. ( H ) The densitometry analysis of the CD55 and CD46 protein expression, normalized against the loading control. The data represents the mean + SEM of the three independent experiments.

Techniques: Infection, Western Blot, Expressing

VSV infection causes a decline in the surface expression of CD46 and not CD55. HeLa cells were infected with VSV (10 MOI) for the specified time points. The surface distribution of CD55 and CD46 was determined by staining the mock- and VSV-infected cells with anti-CD55 and CD46 primary antibodies, and by counter staining with AF488-labelled secondary antibody. The two panels, A and B , denote the histogram representing the fluorescence intensity on the x -axis and the cell count on the y -axis. The infection of the HeLa cells with VSV did not alter the surface level expression of CD55 ( A ) even until 24 h; however, a drastic reduction in the surface expression of CD46 ( B ) could be evidenced 6 h post infection.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: VSV infection causes a decline in the surface expression of CD46 and not CD55. HeLa cells were infected with VSV (10 MOI) for the specified time points. The surface distribution of CD55 and CD46 was determined by staining the mock- and VSV-infected cells with anti-CD55 and CD46 primary antibodies, and by counter staining with AF488-labelled secondary antibody. The two panels, A and B , denote the histogram representing the fluorescence intensity on the x -axis and the cell count on the y -axis. The infection of the HeLa cells with VSV did not alter the surface level expression of CD55 ( A ) even until 24 h; however, a drastic reduction in the surface expression of CD46 ( B ) could be evidenced 6 h post infection.

Techniques: Infection, Expressing, Staining, Fluorescence, Cell Counting

Vesicular stomatitis virus infection leads to down-regulation of CD55 and CD46 transcripts. A comparative analysis of the relative levels of CD55 ( A ) and CD46 ( B ) mRNA in VSV and mock-infected HeLa cells at 6, 12, 18 and 24 h was carried out by RT-qPCR. The total RNA isolated from the mock- and VSV-infected cells was converted to cDNA. Equal concentrations of cDNA from all of the samples were used to analyze the gene expression at various time points post VSV-infection using Taqman gene expression assays. The fold change was calculated by the comparative Ct method (2^- ddCt). The statistical significance was calculated using Students t -test, with * p ≤ 0.01; ** p ≤ 0.001; **** p ≤ 0.0001, and ns = non-significance.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Vesicular stomatitis virus infection leads to down-regulation of CD55 and CD46 transcripts. A comparative analysis of the relative levels of CD55 ( A ) and CD46 ( B ) mRNA in VSV and mock-infected HeLa cells at 6, 12, 18 and 24 h was carried out by RT-qPCR. The total RNA isolated from the mock- and VSV-infected cells was converted to cDNA. Equal concentrations of cDNA from all of the samples were used to analyze the gene expression at various time points post VSV-infection using Taqman gene expression assays. The fold change was calculated by the comparative Ct method (2^- ddCt). The statistical significance was calculated using Students t -test, with * p ≤ 0.01; ** p ≤ 0.001; **** p ≤ 0.0001, and ns = non-significance.

Techniques: Infection, Quantitative RT-PCR, Isolation, Expressing

Cycloheximide chase assay to measure protein stability. ( A ) The HeLa cells were treated with Cycloheximide for the indicated times, and the whole cell lysate was subjected to immunoblotting in order to determine the stability of CD55 and CD46. β-actin was used as the loading control, and P53 served as the positive control. ( B ) Quantification of the immunoblot results by Image J software. The result represented is the average + SEM of four independent experiments obtained by normalizing the band intensity of the RCA against b-actin. The statistical significance was calculated using Student’s t -test.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Cycloheximide chase assay to measure protein stability. ( A ) The HeLa cells were treated with Cycloheximide for the indicated times, and the whole cell lysate was subjected to immunoblotting in order to determine the stability of CD55 and CD46. β-actin was used as the loading control, and P53 served as the positive control. ( B ) Quantification of the immunoblot results by Image J software. The result represented is the average + SEM of four independent experiments obtained by normalizing the band intensity of the RCA against b-actin. The statistical significance was calculated using Student’s t -test.

Techniques: Western Blot, Positive Control, Software

Complement regulator CD55 is found in greater abundance than CD46 on VSV from HeLa cells. ( A ) Equal concentrations of protein in the purified virus (5 μg) were separated by SDS-PAGE and subjected to Western blotting. The proteins that have been probed are indicated in the right, and their corresponding molecular weights are in parentheses. ( B ) An ELISA specific to VSV was performed by coating wells with serially-diluted gradient-purified VSV. The adsorbed virus particles were detected using an anti-VSV-G antibody. Variability in the absorbance was observed even at similar concentration of viruses purified at varying time intervals. Across the samples, an absorbance of ~1.3 was found to be common; this is indicated by the lines drawn against the optical density. ( y -axis) to the corresponding concentrations ( x -axis).

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Complement regulator CD55 is found in greater abundance than CD46 on VSV from HeLa cells. ( A ) Equal concentrations of protein in the purified virus (5 μg) were separated by SDS-PAGE and subjected to Western blotting. The proteins that have been probed are indicated in the right, and their corresponding molecular weights are in parentheses. ( B ) An ELISA specific to VSV was performed by coating wells with serially-diluted gradient-purified VSV. The adsorbed virus particles were detected using an anti-VSV-G antibody. Variability in the absorbance was observed even at similar concentration of viruses purified at varying time intervals. Across the samples, an absorbance of ~1.3 was found to be common; this is indicated by the lines drawn against the optical density. ( y -axis) to the corresponding concentrations ( x -axis).

Techniques: Purification, SDS Page, Western Blot, Enzyme-linked Immunosorbent Assay, Concentration Assay

Levels of CD55 and CD46 associated with sucrose gradient-purified VSV from HeLa cells at various time intervals. a,b The concentration of the virion-associated CD55/CD46 was calculated from the pixel intensity of the known concentrations of rCD46 and rCD55 run in parallel ( <xref ref-type=

Figure 5 A). The concentration of CD55 and CD46 is depicted as ng/5μg of VSV. c,f Based on the densitometric analysis of VSV-G or M, further normalization was performed relative to the values obtained at 6–12 h (taken as 1). The values indicate the decline in the concentration of G or M relative to 6–12 h. d,g The ratio of CD55 to VSV-G or VSV-M was calculated by dividing the CD55 concentration at a specific time point by the normalized levels of G or M. The values in d were obtained by dividing a by c , and those in e by dividing b by c . Similarly, the ratios in g and h were obtained by dividing a by f and b by f , respectively." width="100%" height="100%">

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: Levels of CD55 and CD46 associated with sucrose gradient-purified VSV from HeLa cells at various time intervals. a,b The concentration of the virion-associated CD55/CD46 was calculated from the pixel intensity of the known concentrations of rCD46 and rCD55 run in parallel ( Figure 5 A). The concentration of CD55 and CD46 is depicted as ng/5μg of VSV. c,f Based on the densitometric analysis of VSV-G or M, further normalization was performed relative to the values obtained at 6–12 h (taken as 1). The values indicate the decline in the concentration of G or M relative to 6–12 h. d,g The ratio of CD55 to VSV-G or VSV-M was calculated by dividing the CD55 concentration at a specific time point by the normalized levels of G or M. The values in d were obtained by dividing a by c , and those in e by dividing b by c . Similarly, the ratios in g and h were obtained by dividing a by f and b by f , respectively.

Techniques: Concentration Assay

CD55 confers greater resistance to VSV against complement compared to CD46. ( A ) Western blot depicting the level of expression of CD55 and CD46 in HeLa and A549 cells; β-actin served as the equal loading control. ( B ) The effect of NHS in neutralizing VSV grown in HeLa and A549 cells was assessed by a plaque reduction assay. The virus harvested at the indicated time intervals was incubated either with NHS or PBS (black bars). At all of the time points tested, the HeLa-grown viruses showed marked resistance to complement-mediated neutralization. The degree of neutralization of A549-grown VSV known to harbor less CD55 was significantly higher than that of HeLa-grown VSV at 12–18 h ( p < 0.0001). The symbols in the graph represent * p < 0.05; ** p < 0.005; *** p < 0.0005). The additional symbols represent the comparison of significance between A549- and HeLa-grown VSV treated with NHS at the respective time ranges, where # p < 0.0005; $ p < 0.0005; ^ p < 0.0001; @ p < 0.005.

Journal: Viruses

Article Title: Functional Dissection of the Dominant Role of CD55 in Protecting Vesicular Stomatitis Virus against Complement-Mediated Neutralization

doi: 10.3390/v13030373

Figure Lengend Snippet: CD55 confers greater resistance to VSV against complement compared to CD46. ( A ) Western blot depicting the level of expression of CD55 and CD46 in HeLa and A549 cells; β-actin served as the equal loading control. ( B ) The effect of NHS in neutralizing VSV grown in HeLa and A549 cells was assessed by a plaque reduction assay. The virus harvested at the indicated time intervals was incubated either with NHS or PBS (black bars). At all of the time points tested, the HeLa-grown viruses showed marked resistance to complement-mediated neutralization. The degree of neutralization of A549-grown VSV known to harbor less CD55 was significantly higher than that of HeLa-grown VSV at 12–18 h ( p < 0.0001). The symbols in the graph represent * p < 0.05; ** p < 0.005; *** p < 0.0005). The additional symbols represent the comparison of significance between A549- and HeLa-grown VSV treated with NHS at the respective time ranges, where # p < 0.0005; $ p < 0.0005; ^ p < 0.0001; @ p < 0.005.

Techniques: Western Blot, Expressing, Incubation, Neutralization

Journal: The FASEB Journal

Article Title: MAP‐2:CD55 chimeric construct effectively modulates complement activation

doi: 10.1096/fj.202300571r

Figure Lengend Snippet: FIGURE 1 Expression of the novel construct MAP-2:CD551-4. (A) Graphical representation of MAP-2 and MAP-2:CD551-4. (B–D) Western immunoblotting of the purified protein MAP-2:CD551-4 probed with mAb anti-MASP-2/Map19 (B), mAb anti-CD55 (C), and mAb anti-FLAG tag (D). rMAP-2 and rCD551-4 produced in-house were used as controls. (E) Direct protein stain of the same purified proteins.

Article Snippet: Membranes were blocked with 5% (w/v) skim milk (Sigma- Aldrich) for 30 min and then incubated with 0.5 μg/mL rat monoclonal antibody (mAb) anti- MASP- 2/ Map19, clone 6G12 (Hycult, Uden, The Netherlands), 1 μg/mL mouse mAb anti- CD55, clone 278803 (MAB2009; R&D Systems, Minneapolis, MN, USA), or 2 μg/mL mouse mAb anti- FLAG- tag (clone 18, produced in- house).

Techniques: Expressing, Construct, Western Blot, Purification, FLAG-tag, Produced, Staining

Journal: The FASEB Journal

Article Title: MAP‐2:CD55 chimeric construct effectively modulates complement activation

doi: 10.1096/fj.202300571r

Figure Lengend Snippet: FIGURE 2 Structural characterization of MAP-2:CD551-4. (A) MAP-2:CD551-4 elution profile from size exclusion chromatography exposed to 2 mM of calcium, 10 mM EDTA, or 10 mM EGTA. Vertical lines represent the molecular weight of the molecular marker, represented in kDa. (B–D) Western immunoblotting of the elution fractions 3–16 of MAP-2 from SEC exposed to 2.5 mM of calcium (B), 10 mM EDTA (C), or 10 mM EGTA (D). MAb anti MASP-2/Map19 clone 6G12 was used to detect MAP-2:CD551-4. Representative blots out of 3 independent replicates are shown. (E and F) Thermal stability of MAP-2, CD55, and MAP-2:CD551-4 exposed to 2 mM calcium or 10 mM EGTA shown as the ratio of the intrinsic fluorescence at 350 and 330 nm (E) and the right the first derivative of the ratio (F). Thermal stability was performed in triplicates.

Techniques: Size-exclusion Chromatography, Molecular Weight, Marker, Western Blot, Fluorescence

Schematic representation of BDES constructs and the expression of functional proteins. a The pfcsp genes were cloned from P. falciparum (PfCSP 19–373 ; PfCSP1) or synthesized with codon-optimization (synthesized PfCSP 19–377 ; sPfCSP2). Both pfcsp genes were fused to the N-terminus of the gp64 gene (gp64 21–512 ) and the transmembrane region of the vsv - g gene (VSV-G 421–511 ; G). Expression of the PfCSP gene cassette was driven by a dual promoter (pCMV and pPolh). In the “Spider” type of BDES construct, but not in the “Spier” type construct, the human daf gene (hDAF) was displayed on virions under the control of the p10 promoter. b AcNPV-WT (non-recombinant control), BES-GL3-Spider (hDAF-displayed control), BDES-PfCSP1-gp64, BDES-sPfCSP2-Spier, and BDES-sPfCSP2-Spider (lanes 1–5, respectively) were lysed and subjected to the immunoblots with anti-PfCSP, anti-hDAF, or anti-VP39 Abs. ( c – j ) The morphologies of BDES-sPfCSP2-Spider ( c – f ) and BDES-sPfCSP2-Spier ( g – j ) are shown by transmission electron microscopy. The viral particles were reacted with a nonspecific mouse IgG ( c , g ), anti-FLAG mAb ( d , h ), anti-PfCSP mAb ( e , i ), or anti-DAF mouse mAb ( f , j ), and then incubated with a 5 nm colloidal gold-conjugated secondary Ab. Bars, 100 nm; Arrows, colloidal gold signals

Journal: Malaria Journal

Article Title: DAF-shielded baculovirus-vectored vaccine enhances protection against malaria sporozoite challenge in mice

doi: 10.1186/s12936-017-2039-x

Figure Lengend Snippet: Schematic representation of BDES constructs and the expression of functional proteins. a The pfcsp genes were cloned from P. falciparum (PfCSP 19–373 ; PfCSP1) or synthesized with codon-optimization (synthesized PfCSP 19–377 ; sPfCSP2). Both pfcsp genes were fused to the N-terminus of the gp64 gene (gp64 21–512 ) and the transmembrane region of the vsv - g gene (VSV-G 421–511 ; G). Expression of the PfCSP gene cassette was driven by a dual promoter (pCMV and pPolh). In the “Spider” type of BDES construct, but not in the “Spier” type construct, the human daf gene (hDAF) was displayed on virions under the control of the p10 promoter. b AcNPV-WT (non-recombinant control), BES-GL3-Spider (hDAF-displayed control), BDES-PfCSP1-gp64, BDES-sPfCSP2-Spier, and BDES-sPfCSP2-Spider (lanes 1–5, respectively) were lysed and subjected to the immunoblots with anti-PfCSP, anti-hDAF, or anti-VP39 Abs. ( c – j ) The morphologies of BDES-sPfCSP2-Spider ( c – f ) and BDES-sPfCSP2-Spier ( g – j ) are shown by transmission electron microscopy. The viral particles were reacted with a nonspecific mouse IgG ( c , g ), anti-FLAG mAb ( d , h ), anti-PfCSP mAb ( e , i ), or anti-DAF mouse mAb ( f , j ), and then incubated with a 5 nm colloidal gold-conjugated secondary Ab. Bars, 100 nm; Arrows, colloidal gold signals

Article Snippet: The lysates were separated by 8% SDS-PAGE and transferred to polyvinylidene fluoride membranes, and then probed with either of the following: an anti-PfCSP mouse mAb (2A10) or an anti-hDAF mouse mAb (anti-CD55, Merck Millipore, Temecula, CA), together with an anti-VP39 rabbit Ab [ ].

Techniques: Construct, Expressing, Functional Assay, Clone Assay, Synthesized, Control, Recombinant, Western Blot, Transmission Assay, Electron Microscopy, Incubation

Schematic representation of the luciferase-expressing vaccines and their complement resistance in vitro and in vivo. a BES-GL3-Spier and BES-GL3-Spider vectors express firefly luciferase GL3 under the pCMV single promoter, and the BES-GL3-Spider vector contains a gene cassette for hDAF display. PB, PiggyBac transposon sequence; S, gp64 signal sequence; F, FLAG epitope tag; M, myc epitope tag; and EGFP, enhanced green fluorescent protein. b BES-GL3-Spier (lane 1) and BES-GL3-Spider (lane 2) were lysed and subjected to immunoblotting with anti-DAF and anti-VP39 Abs. c BES-GL3-Spier and BES-GL3-Spider were treated with heat-inactivated or intact serum and then transduced into HepG2 cells. Cell lysates were subjected to luciferase assays. Each relative luciferase unit (RLU) was normalized against each of the values of the heat-inactivated samples (n = 3). Bars and error bars indicate the mean ± SD of the values, respectively. Representative data from three independent studies are shown. HI, heat-inactivated serum; Intact, non-heat-inactivated serum. d Luciferase expression in BES-GL3-Spier- and BES-GL3-Spider-immunized Balb/c mice at 1, 3, 5, 7, and 14 days post-immunization (n = 4). The heat map image visible in the mice represents the total flux of photons (p/sec/cm 2 ) in that area. e The mean total flux of photons is shown. Bars and error bars indicate the mean ± SD of the values, respectively. Comparison between groups was assessed by the Mann–Whitney U -test. * p < 0.05, compared with BES-GL3-Spier

Journal: Malaria Journal

Article Title: DAF-shielded baculovirus-vectored vaccine enhances protection against malaria sporozoite challenge in mice

doi: 10.1186/s12936-017-2039-x

Figure Lengend Snippet: Schematic representation of the luciferase-expressing vaccines and their complement resistance in vitro and in vivo. a BES-GL3-Spier and BES-GL3-Spider vectors express firefly luciferase GL3 under the pCMV single promoter, and the BES-GL3-Spider vector contains a gene cassette for hDAF display. PB, PiggyBac transposon sequence; S, gp64 signal sequence; F, FLAG epitope tag; M, myc epitope tag; and EGFP, enhanced green fluorescent protein. b BES-GL3-Spier (lane 1) and BES-GL3-Spider (lane 2) were lysed and subjected to immunoblotting with anti-DAF and anti-VP39 Abs. c BES-GL3-Spier and BES-GL3-Spider were treated with heat-inactivated or intact serum and then transduced into HepG2 cells. Cell lysates were subjected to luciferase assays. Each relative luciferase unit (RLU) was normalized against each of the values of the heat-inactivated samples (n = 3). Bars and error bars indicate the mean ± SD of the values, respectively. Representative data from three independent studies are shown. HI, heat-inactivated serum; Intact, non-heat-inactivated serum. d Luciferase expression in BES-GL3-Spier- and BES-GL3-Spider-immunized Balb/c mice at 1, 3, 5, 7, and 14 days post-immunization (n = 4). The heat map image visible in the mice represents the total flux of photons (p/sec/cm 2 ) in that area. e The mean total flux of photons is shown. Bars and error bars indicate the mean ± SD of the values, respectively. Comparison between groups was assessed by the Mann–Whitney U -test. * p < 0.05, compared with BES-GL3-Spier

Techniques: Luciferase, Expressing, Vaccines, In Vitro, In Vivo, Plasmid Preparation, Sequencing, FLAG-tag, Western Blot, Comparison, MANN-WHITNEY

Fig. 2. Intracellular distribution of CBV4, CAR, or CD55 and organelle marker for lysosomes at 30-min postinfection. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Lysosomes are labeled green with Lysotraker green DND-99. CAR molecules labeled with TRITC-C1079 and CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three (CBV4, CAR, lysosomes) is shown as well as a merged image of the three (CBV4, CD55, lysosomes). Although CBV4 and CD55 do not overlap with the labeling pattern of lysosomes, there is colocalization between CAR and lysosomes (seen as yellow). Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Journal: Virology

Article Title: Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi.

doi: 10.1016/j.virol.2004.04.051

Figure Lengend Snippet: Fig. 2. Intracellular distribution of CBV4, CAR, or CD55 and organelle marker for lysosomes at 30-min postinfection. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Lysosomes are labeled green with Lysotraker green DND-99. CAR molecules labeled with TRITC-C1079 and CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three (CBV4, CAR, lysosomes) is shown as well as a merged image of the three (CBV4, CD55, lysosomes). Although CBV4 and CD55 do not overlap with the labeling pattern of lysosomes, there is colocalization between CAR and lysosomes (seen as yellow). Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: CD55-specific mAb MCA914 was obtained from Serotec (U.K.).

Techniques: Marker, Labeling

Fig. 3. Intracellular distribution of CBV4, CD55, and FITC-conjugated anti-EEA1-specific serum (FITC anti EEA1) for the detection of early endosomes at 30-min postinfection is shown. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Endosomes are revealed as green with FITC-anti EEA1. CD55 molecules labeled with TRITC-MCA914 are seen as red. Intracellular distribution of CBV4, CD55, and FITC anti-EEA1 at 15-min postinfection in the presence of NH4Cl (50 nM) is also shown. A merged image of the three (CBV4, CD55, early endosomes) is also shown. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Journal: Virology

Article Title: Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi.

doi: 10.1016/j.virol.2004.04.051

Figure Lengend Snippet: Fig. 3. Intracellular distribution of CBV4, CD55, and FITC-conjugated anti-EEA1-specific serum (FITC anti EEA1) for the detection of early endosomes at 30-min postinfection is shown. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Endosomes are revealed as green with FITC-anti EEA1. CD55 molecules labeled with TRITC-MCA914 are seen as red. Intracellular distribution of CBV4, CD55, and FITC anti-EEA1 at 15-min postinfection in the presence of NH4Cl (50 nM) is also shown. A merged image of the three (CBV4, CD55, early endosomes) is also shown. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: CD55-specific mAb MCA914 was obtained from Serotec (U.K.).

Techniques: Labeling

Fig. 5. Intracellular distribution of CBV4, CAR, or CD55 and organelle marker for endosomes. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Endosomes are revealed as green with FITC–Dextran. CAR molecules labeled with TRITC-C1079 and CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three (CBV4, CAR, endosomes) and (CBV4, CD55, endosomes) is shown. Although CBV4 particles do not overlap with the labeling pattern of endosomes, there is a partial overlap between CAR and endosomes, which is seen as yellow. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Journal: Virology

Article Title: Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi.

doi: 10.1016/j.virol.2004.04.051

Figure Lengend Snippet: Fig. 5. Intracellular distribution of CBV4, CAR, or CD55 and organelle marker for endosomes. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Endosomes are revealed as green with FITC–Dextran. CAR molecules labeled with TRITC-C1079 and CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three (CBV4, CAR, endosomes) and (CBV4, CD55, endosomes) is shown. Although CBV4 particles do not overlap with the labeling pattern of endosomes, there is a partial overlap between CAR and endosomes, which is seen as yellow. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: CD55-specific mAb MCA914 was obtained from Serotec (U.K.).

Techniques: Marker, Labeling

Fig. 7. Intracellular distribution of CBV4, CD55, and FITC–anti-GM130 for cis-Golgi at 0, 15, 30, and 60 min postinfection is shown. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. cis-Golgi is seen as green. CD55 molecules labeled with TRITC-MCA914 are seen as red. Merged images of the three are also shown (CBV4, Golgi, CD55), which show that CD55 and CBV4 concentrate in the cis-Golgi (colocalization of all three; CBV4, Golgi, CD55 is seen as white) at 30 and 60 min. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Journal: Virology

Article Title: Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi.

doi: 10.1016/j.virol.2004.04.051

Figure Lengend Snippet: Fig. 7. Intracellular distribution of CBV4, CD55, and FITC–anti-GM130 for cis-Golgi at 0, 15, 30, and 60 min postinfection is shown. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. cis-Golgi is seen as green. CD55 molecules labeled with TRITC-MCA914 are seen as red. Merged images of the three are also shown (CBV4, Golgi, CD55), which show that CD55 and CBV4 concentrate in the cis-Golgi (colocalization of all three; CBV4, Golgi, CD55 is seen as white) at 30 and 60 min. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: CD55-specific mAb MCA914 was obtained from Serotec (U.K.).

Techniques: Labeling

Fig. 9. Intracellular distribution of CBV4, CD55, and FITC–anti-GM130 for cis-Golgi at 60-min postinfection in the presence of chloropromazine and nystatin. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Golgi is seen as green. CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three is also shown. Colocalization of all three: CBV4, Golgi, CD55 is seen as white. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Journal: Virology

Article Title: Lipid-raft-dependent Coxsackievirus B4 internalization and rapid targeting to the Golgi.

doi: 10.1016/j.virol.2004.04.051

Figure Lengend Snippet: Fig. 9. Intracellular distribution of CBV4, CD55, and FITC–anti-GM130 for cis-Golgi at 60-min postinfection in the presence of chloropromazine and nystatin. CBV4 particles labeled with Cy5-specific CBV4 Fab are seen as blue. Golgi is seen as green. CD55 molecules labeled with TRITC-MCA914 are seen as red. A merged image of the three is also shown. Colocalization of all three: CBV4, Golgi, CD55 is seen as white. Scale bar = 5 Am. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: CD55-specific mAb MCA914 was obtained from Serotec (U.K.).

Techniques: Labeling

Review

Structured Review

Images

1) Product Images from "MAP‐2:CD55 chimeric construct effectively modulates complement activation"

Similar Products

Image Search Results