goat anti mouse igg  (Thermo Fisher)


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    Name:
    Goat anti Mouse IgG
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    PA1-32125
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    Structured Review

    Thermo Fisher goat anti mouse igg
    Pre-labeling Ex- d STORM. a Simulated intensity profiles using a cylindrical distribution function to describe unexpanded or 3.2x expanded immunostained microtubules (labeled with <t>IgG</t> antibodies or DNA modified IgG antibodies pre-expansion) and resulting peak-to-peak distances of the cross-sectional profiles. b d STORM image of expanded and re-embedded α- and β-tubulin pre-labeled with secondary <t>Alexa</t> Fluor 532 IgG antibodies (Al532) using the MA-NHS/GA method 6 , i.e. antibodies are cross-linked with glutaraldehyde (GA) into the hydrogel (Antibody-Al532 (GA)). c Zoom in of white boxed region in ( b ). d Averaged cross-sectional profile of 8 microtubule segments with a length between 1.5–6.4 µm and 28.6 µm in total measured in 4 expanded cells. e Histogram of peak-to-peak distance distribution with normalized normal curve (red) of microtubule segments analyzed in ( d ) at n = 8 microtubule segments in 4 cells from 1 expansion experiment with a mean distance of 133.8 ± 13.2 nm (mean ± sd). f Unexpanded d STORM image of ssDNA-Cy5 secondary antibody hybridized with Cy5 bearing oligonucleotides pre-expansion (DNA-Cy5 protocol). g Magnified view of white boxed region in ( f ). h Average cross-sectional profile of 7 microtubule segments with a length between 1.0–1.8 µm and 8.7 µm in total. i Histogram of peak-to-peak distances with normalized normal distribution curve (red) of the data analyzed in ( h ) along n = 7 microtubule segments in 2 cells from 1 experiment with a mean distance of 43.9 ± 3.7 nm (mean ± sd). j Expanded d STORM image of microtubules labeled with α-tubulin and dsDNA (DNA-Al532) conjugated secondary antibodies exhibiting a methacryloyl group to crosslink the DNA with fluorophores pre-expansion into the hydrogel (original ExM trifunctional label concept) 1 . k Zoom-in of white boxed region in ( j ). l Average intensity profile of 26 microtubule segments with a length of 2.4–10.7 µm and 118.6 µm in total. m Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined from n = 26 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 226.7 ± 15.3 nm (mean ± sd). n d STORM image of α- and β-tubulin expanded according to the DNA-Cy5 protocol strategy with labels at Cy5-bearing oligonucleotides introduced post-re-embedding. o Zoom in of white boxed region in ( n ). p Average intensity profile of 15 microtubule segments with a length between 1.6–25.1 µm and a total length of 126.0 µm in 1 expanded sample. q Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by fitting the cross-sectional profiles analyzed in ( p ) along n = 22 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 201.0 ± 12.9 nm (mean ± sd). The small logos in the upper left corner symbolize the labeling method, e.g. pre- and post-immunolabeled with or without DNA-linker, respectively. Scale bars, 2 µm ( b , f , j , n ), 500 nm ( c , g , k , o ).

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    Images

    1) Product Images from "Molecular resolution imaging by post-labeling expansion single-molecule localization microscopy (Ex-SMLM)"

    Article Title: Molecular resolution imaging by post-labeling expansion single-molecule localization microscopy (Ex-SMLM)

    Journal: Nature Communications

    doi: 10.1038/s41467-020-17086-8

    Pre-labeling Ex- d STORM. a Simulated intensity profiles using a cylindrical distribution function to describe unexpanded or 3.2x expanded immunostained microtubules (labeled with IgG antibodies or DNA modified IgG antibodies pre-expansion) and resulting peak-to-peak distances of the cross-sectional profiles. b d STORM image of expanded and re-embedded α- and β-tubulin pre-labeled with secondary Alexa Fluor 532 IgG antibodies (Al532) using the MA-NHS/GA method 6 , i.e. antibodies are cross-linked with glutaraldehyde (GA) into the hydrogel (Antibody-Al532 (GA)). c Zoom in of white boxed region in ( b ). d Averaged cross-sectional profile of 8 microtubule segments with a length between 1.5–6.4 µm and 28.6 µm in total measured in 4 expanded cells. e Histogram of peak-to-peak distance distribution with normalized normal curve (red) of microtubule segments analyzed in ( d ) at n = 8 microtubule segments in 4 cells from 1 expansion experiment with a mean distance of 133.8 ± 13.2 nm (mean ± sd). f Unexpanded d STORM image of ssDNA-Cy5 secondary antibody hybridized with Cy5 bearing oligonucleotides pre-expansion (DNA-Cy5 protocol). g Magnified view of white boxed region in ( f ). h Average cross-sectional profile of 7 microtubule segments with a length between 1.0–1.8 µm and 8.7 µm in total. i Histogram of peak-to-peak distances with normalized normal distribution curve (red) of the data analyzed in ( h ) along n = 7 microtubule segments in 2 cells from 1 experiment with a mean distance of 43.9 ± 3.7 nm (mean ± sd). j Expanded d STORM image of microtubules labeled with α-tubulin and dsDNA (DNA-Al532) conjugated secondary antibodies exhibiting a methacryloyl group to crosslink the DNA with fluorophores pre-expansion into the hydrogel (original ExM trifunctional label concept) 1 . k Zoom-in of white boxed region in ( j ). l Average intensity profile of 26 microtubule segments with a length of 2.4–10.7 µm and 118.6 µm in total. m Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined from n = 26 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 226.7 ± 15.3 nm (mean ± sd). n d STORM image of α- and β-tubulin expanded according to the DNA-Cy5 protocol strategy with labels at Cy5-bearing oligonucleotides introduced post-re-embedding. o Zoom in of white boxed region in ( n ). p Average intensity profile of 15 microtubule segments with a length between 1.6–25.1 µm and a total length of 126.0 µm in 1 expanded sample. q Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by fitting the cross-sectional profiles analyzed in ( p ) along n = 22 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 201.0 ± 12.9 nm (mean ± sd). The small logos in the upper left corner symbolize the labeling method, e.g. pre- and post-immunolabeled with or without DNA-linker, respectively. Scale bars, 2 µm ( b , f , j , n ), 500 nm ( c , g , k , o ).
    Figure Legend Snippet: Pre-labeling Ex- d STORM. a Simulated intensity profiles using a cylindrical distribution function to describe unexpanded or 3.2x expanded immunostained microtubules (labeled with IgG antibodies or DNA modified IgG antibodies pre-expansion) and resulting peak-to-peak distances of the cross-sectional profiles. b d STORM image of expanded and re-embedded α- and β-tubulin pre-labeled with secondary Alexa Fluor 532 IgG antibodies (Al532) using the MA-NHS/GA method 6 , i.e. antibodies are cross-linked with glutaraldehyde (GA) into the hydrogel (Antibody-Al532 (GA)). c Zoom in of white boxed region in ( b ). d Averaged cross-sectional profile of 8 microtubule segments with a length between 1.5–6.4 µm and 28.6 µm in total measured in 4 expanded cells. e Histogram of peak-to-peak distance distribution with normalized normal curve (red) of microtubule segments analyzed in ( d ) at n = 8 microtubule segments in 4 cells from 1 expansion experiment with a mean distance of 133.8 ± 13.2 nm (mean ± sd). f Unexpanded d STORM image of ssDNA-Cy5 secondary antibody hybridized with Cy5 bearing oligonucleotides pre-expansion (DNA-Cy5 protocol). g Magnified view of white boxed region in ( f ). h Average cross-sectional profile of 7 microtubule segments with a length between 1.0–1.8 µm and 8.7 µm in total. i Histogram of peak-to-peak distances with normalized normal distribution curve (red) of the data analyzed in ( h ) along n = 7 microtubule segments in 2 cells from 1 experiment with a mean distance of 43.9 ± 3.7 nm (mean ± sd). j Expanded d STORM image of microtubules labeled with α-tubulin and dsDNA (DNA-Al532) conjugated secondary antibodies exhibiting a methacryloyl group to crosslink the DNA with fluorophores pre-expansion into the hydrogel (original ExM trifunctional label concept) 1 . k Zoom-in of white boxed region in ( j ). l Average intensity profile of 26 microtubule segments with a length of 2.4–10.7 µm and 118.6 µm in total. m Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined from n = 26 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 226.7 ± 15.3 nm (mean ± sd). n d STORM image of α- and β-tubulin expanded according to the DNA-Cy5 protocol strategy with labels at Cy5-bearing oligonucleotides introduced post-re-embedding. o Zoom in of white boxed region in ( n ). p Average intensity profile of 15 microtubule segments with a length between 1.6–25.1 µm and a total length of 126.0 µm in 1 expanded sample. q Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by fitting the cross-sectional profiles analyzed in ( p ) along n = 22 microtubule segments in 4 cells from 1 expanded sample showing a mean distance of 201.0 ± 12.9 nm (mean ± sd). The small logos in the upper left corner symbolize the labeling method, e.g. pre- and post-immunolabeled with or without DNA-linker, respectively. Scale bars, 2 µm ( b , f , j , n ), 500 nm ( c , g , k , o ).

    Techniques Used: Labeling, Modification, Immunolabeling

    Re-embedding enables Ex- d STORM. a Model of microtubules with an outer diameter of 25 nm stained with conventional primary (pab) and fluorescently labeled secondary IgG antibodies (sab) results in a total diameter of 60 nm with a linkage error (defined by the size of the primary and secondary antibody) of 17.5 nm 22 . b d STORM image of pre-labeled proExM expanded and re-embedded Cos-7 cells stained with primary antibodies against α-tubulin and secondary Alexa Fluor 532 conjugated antibodies (Al532). The small logo in the upper left corner symbolizes that microtubules have been immunolabeled before expansion (pre-labeled). c Zoom in on highlighted region in ( b ). d Averaged cross-sectional profile of nine microtubule segments with a total length of 29.1 µm (segment lengths range from 2.1-4.5 µm) measured in two cells from 1 expanded sample. e Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by bi-Gaussian fitting of the data analyzed in ( c ) with an average distance of 137.1 ± 10.1 nm (mean ± sd). The data were obtained from n = 9 microtubule segments in 2 cells from 1 expanded sample. f Unexpanded Cos-7 cells labeled with an anti α-tubulin primary antibody and Alexa Fluor 532 (Al532) conjugated IgG secondary antibodies. The small logo in the upper left corner symbolizes that microtubules have been immunolabeled and not expanded. g Zoom in of the white boxed region in ( f ). h Average intensity profile of 35 microtubule segments with a length between 1.1 and 5.8 µm (mean = 2.0 µm) and a total length of 69.6 µm analyzed in 12 d STORM images. i Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by bi-Gaussian fitting of cross-sectional profiles of the analyzed microtubule segments in ( h ) with a mean peak-to-peak distance of 36.2 ± 5.4 nm (mean ± sd). The data were obtained from n =35 microtubule segments in 12 cells and 3 independent experiments. Scale bars, 2 µm ( b , f ), 500 nm ( c , g ).
    Figure Legend Snippet: Re-embedding enables Ex- d STORM. a Model of microtubules with an outer diameter of 25 nm stained with conventional primary (pab) and fluorescently labeled secondary IgG antibodies (sab) results in a total diameter of 60 nm with a linkage error (defined by the size of the primary and secondary antibody) of 17.5 nm 22 . b d STORM image of pre-labeled proExM expanded and re-embedded Cos-7 cells stained with primary antibodies against α-tubulin and secondary Alexa Fluor 532 conjugated antibodies (Al532). The small logo in the upper left corner symbolizes that microtubules have been immunolabeled before expansion (pre-labeled). c Zoom in on highlighted region in ( b ). d Averaged cross-sectional profile of nine microtubule segments with a total length of 29.1 µm (segment lengths range from 2.1-4.5 µm) measured in two cells from 1 expanded sample. e Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by bi-Gaussian fitting of the data analyzed in ( c ) with an average distance of 137.1 ± 10.1 nm (mean ± sd). The data were obtained from n = 9 microtubule segments in 2 cells from 1 expanded sample. f Unexpanded Cos-7 cells labeled with an anti α-tubulin primary antibody and Alexa Fluor 532 (Al532) conjugated IgG secondary antibodies. The small logo in the upper left corner symbolizes that microtubules have been immunolabeled and not expanded. g Zoom in of the white boxed region in ( f ). h Average intensity profile of 35 microtubule segments with a length between 1.1 and 5.8 µm (mean = 2.0 µm) and a total length of 69.6 µm analyzed in 12 d STORM images. i Histogram of peak-to-peak distances with normalized normal distribution curve (red) determined by bi-Gaussian fitting of cross-sectional profiles of the analyzed microtubule segments in ( h ) with a mean peak-to-peak distance of 36.2 ± 5.4 nm (mean ± sd). The data were obtained from n =35 microtubule segments in 12 cells and 3 independent experiments. Scale bars, 2 µm ( b , f ), 500 nm ( c , g ).

    Techniques Used: Staining, Labeling, Immunolabeling

    2) Product Images from "CD1c molecules broadly survey the endocytic system"

    Article Title: CD1c molecules broadly survey the endocytic system

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

    doi:

    Colocalization of CD1c with ARF6-T27N. HeLa cell transfectants expressing CD1c were grown on coverslips and transiently supertransfected with ARF6-T27N cDNA. The cells were then fixed and permeabilized, and double-labeling with mouse anti-CD1c antibody (detected with Texas Red-conjugated donkey anti-mouse IgG) and rabbit anti-ARF6 antibody (detected with FITC-conjugated donkey anti-rabbit IgG) was performed. Fluorescent confocal images were obtained for CD1c ( A ) and ARF6 ( B ). The two images then were superimposed to detect vesicles expressing both CD1c and ARF6 ( C , yellow vesicles shown with arrowheads). (Scale bars = 5 μm.)
    Figure Legend Snippet: Colocalization of CD1c with ARF6-T27N. HeLa cell transfectants expressing CD1c were grown on coverslips and transiently supertransfected with ARF6-T27N cDNA. The cells were then fixed and permeabilized, and double-labeling with mouse anti-CD1c antibody (detected with Texas Red-conjugated donkey anti-mouse IgG) and rabbit anti-ARF6 antibody (detected with FITC-conjugated donkey anti-rabbit IgG) was performed. Fluorescent confocal images were obtained for CD1c ( A ) and ARF6 ( B ). The two images then were superimposed to detect vesicles expressing both CD1c and ARF6 ( C , yellow vesicles shown with arrowheads). (Scale bars = 5 μm.)

    Techniques Used: Expressing, Labeling

    Colocalization of CD1a, -b, and -c with LAMP-1. Monocyte-derived dendritic cells were fixed and permeablized after a cytospin procedure. The cells were then double-labeled with mouse mAbs to CD1a ( A ), CD1b ( D ), or CD1c ( G ) (detected with Texas Red-conjugated donkey anti-mouse IgG) and a rabbit antiserum against human LAMP-1 ( B , E , and H ) (detected with FITC-conjugated donkey anti-rabbit IgG) and analyzed by confocal microscopy. The corresponding red and green fluorescent confocal images then were superimposed to detect any cellular compartments expressing both CD1 and LAMP-1 ( C , F , and I , yellow vesicles). (Scale bars = 5 μm.)
    Figure Legend Snippet: Colocalization of CD1a, -b, and -c with LAMP-1. Monocyte-derived dendritic cells were fixed and permeablized after a cytospin procedure. The cells were then double-labeled with mouse mAbs to CD1a ( A ), CD1b ( D ), or CD1c ( G ) (detected with Texas Red-conjugated donkey anti-mouse IgG) and a rabbit antiserum against human LAMP-1 ( B , E , and H ) (detected with FITC-conjugated donkey anti-rabbit IgG) and analyzed by confocal microscopy. The corresponding red and green fluorescent confocal images then were superimposed to detect any cellular compartments expressing both CD1 and LAMP-1 ( C , F , and I , yellow vesicles). (Scale bars = 5 μm.)

    Techniques Used: Derivative Assay, Labeling, Confocal Microscopy, Expressing

    Related Articles

    Staining:

    Article Title: Anti-C1q autoantibodies deposit in glomeruli but are only pathogenic in combination with glomerular C1q-containing immune complexes
    Article Snippet: .. Sections were stained for the presence of mouse IgG, rabbit IgG, and mouse C1q using goat anti-mouse IgG Oregon Green (Invitrogen Corp.), goat anti-rabbit IgG conjugated to FITC (Nordic Immunological Laboratories), and rabbit anti–mouse C1q DIG, followed by sheep anti-DIG conjugated to HRP, where appropriate. .. For double staining, goat anti-mouse IgG Alexa 546 (Invitrogen Corp.) was used in combination with anti-C1q and anti-rabbit IgG stainings, as described above.

    Article Title: Identification of the Mycobacterium ulcerans Protein MUL_3720 as a Promising Target for the Development of a Diagnostic Test for Buruli Ulcer
    Article Snippet: Agarose blocks were embedded into paraffin, cut in 3 μm sections and transferred onto microscopy glass slides (Thermo Scientific). .. Bacteria were stained with mAb JD3.2 and Alexa fluor488 (Invitrogen) conjugated goat anti-mouse IgG and mounted in ProLong Gold anti-fade reagent containing 4′,6-Diamidino-2-phenylindole (DAPI; Invitrogen). .. Mycobacterial protein fragment complementation The system described for investigating protein interactions by the functional reconstitution of a murine dehydrofolate reductase domain in M. tuberculosis [ ] was modified here for use in M. ulcerans.

    Incubation:

    Article Title: CaGdt1 plays a compensatory role for the calcium pump CaPmr1 in the regulation of calcium signaling and cell wall integrity signaling in Candida albicans
    Article Snippet: BSA of 400 μg ml− 1 was added to the spheroplast mixture, and incubated for 20 min before mouse anti-HA antibodies was added at a dilution of 1:500. .. The mixture was incubated for 2 h, and washed twice with PBST before goat anti-mouse IgG conjugated to Alexa Fluor 555 (Invitrogen, USA) was added. .. The mixture was incubated in dark for 45 min before spheroplasts were collected, washed three times, and visualized under a Nikon 80i microscope equipped with DS-U2 CCD.

    Article Title: Design of novel small molecule base-pair recognizers of toxic CUG RNA transcripts characteristics of DM1
    Article Snippet: .. Then, samples were incubated with anti-MBNL1 3A4 antibody (Santa Cruz Biotechnology) solution in PBS at room temperature for 1 h. After that samples were washed 3 times with PBS and incubated using goat anti-mouse IgG-Alexa Fluor 488 (Invitrogen, Thermo Scientific, Carlsbad, CA). .. After that, samples were incubated with Hoechst 33,258 (Invitrogen) in PBS at room temperature for 10 min.

    Labeling:

    Article Title: RIM1/2-Mediated Facilitation of Cav1.4 Channel Opening Is Required for Ca2+-Stimulated Release in Mouse Rod Photoreceptors
    Article Snippet: Two primary antibodies were added simultaneously over the first night (one rabbit IgG, anti-Cav, and the other mouse IgG, anti-Cre) and then anti-CtBP2 was added for the second overnight incubation. .. In most instances, rabbit IgGs were labeled with chicken anti-rabbit IgG-Alexa Fluor 488 (Invitrogen, ) and mouse IgGs were labeled with goat anti-mouse IgG-Alexa Fluor 647 (Invitrogen, ). .. Confocal images of immunolabeled samples were collected as a stack of optical sections through the entire ∼10 μm cryosections and the images are presented here as maximal projections using ImageJ software.

    other:

    Article Title: A Soluble Fragment of the Tumor Antigen BCL2-associated Athanogene 6 (BAG-6) Is Essential and Sufficient for Inhibition of NKp30 Receptor-dependent Cytotoxicity of Natural Killer Cells *
    Article Snippet: The following antibodies were used: mouse monoclonal anti-polyhistidine tag HRP-conjugate and anti-human HRP-conjugate (both Sigma-Aldrich), anti-Strep-mAb classic HRP (IBA), anti-NKp30 clone p30-15 (kindly provided by Carsten Watzl), goat anti-mouse IgG1 APC conjugate (Life Technologies), and anti-CD4 APC conjugate (eBioscience).

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    • anti igm  (Thermo Fisher)
    99
    Thermo Fisher anti igm
    Phenotypic and functional characterization of the IL-33-induced Breg-like cells (Breg IL-33 ) in the blood. A–C. Surface phenotype of Breg IL-33 : The IL-33-induced IL-10 producing B cells expressed high surface <t>IgM</t> (A), CD1d and CD25 (B), but down-regulated CD23 (FceRII) (B, C). Data shown in the table under (B) were results showing the Mean MFI (±SD) values calculated from results of 5 repeated experiments, as ratio of the IL-10 − B, and IL-10 + B, cell subset over the total B cells gated. Statistical analysis: p values (Student t test). D–F. In vitro Breg suppression assays: Immunosuppressive effects of the IL-33-induced Breg-like cells on B effector (Beff) cell proliferation (D), division (E), and its IL-10 dependency (F). D. CD23 + B cells (Beff, 10 5 ) were cultured in the presence of <t>anti-CD40</t> (2.5 μg/ml), with titrating (as indicated) doses of CD23 − B cells (Breg IL-33 ) purified from the IL-33-injected mice. Cell proliferation was determined by thymidine incorporation at 48 h s. E. Breg IL-33 (CD23 - ) purified from hIL-33-injected WT mice (Wk-2) were primed with anti-CD40 (2.5 μg/ml) for 5 h before being added to CFSE-labelled CD23 + Beff cells. Cell division (CFSE dilution) was determined by flow cytometry at day 5 of culture in the presence or absence of LPS (0.5 μg/ml) or anti-IgM (5 μg/ml). F. IL-10 levels in the culture supernatants were quantified by ELISA (BD Biosciences).
    Anti Igm, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1 article reviews
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    anti igm - by Bioz Stars, 2021-04
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    alkaline phosphatase conjugated goat anti mouse igg  (Thermo Fisher)
    86
    Thermo Fisher alkaline phosphatase conjugated goat anti mouse igg
    Plasmodium falciparum EBA175RIII–V construct and expressed antigen. A schematic representation of the 1620 bp region of EBA175RIII–V cloned into the pLEA2 expression vector, which contains the nucleotide sequence of a hexahistidine tag inframe of the multiple cloning site ( a ). The culture supernatant (1) containing the secreted protein as well as the purified protein (2) was analysed by SDS-PAGE followed by coomassie staining ( b ) and a western blot probed with penta-His mouse monoclonal antibody <t>(IgG1)</t> ( c )
    Alkaline Phosphatase Conjugated Goat Anti Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alkaline phosphatase conjugated goat anti mouse igg/product/Thermo Fisher
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    alkaline phosphatase conjugated goat anti mouse igg - by Bioz Stars, 2021-04
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    alexa 488 conjugated goat anti mouse igg  (Thermo Fisher)
    99
    Thermo Fisher alexa 488 conjugated goat anti mouse igg
    Confocal microscopy of cells labeled with anti–LDL receptor Ab. ( a – f ) EBV-lymphocytes were incubated with rabbit anti–LDL receptor (red) at 4°C, washed at 4°C, and either directly permeabilized ( a – c ) or incubated for 10 minutes at 37°C before permeabilization to allow internalization of LDL receptor/Ab complexes ( d – f ). Permeabilized cells were then incubated with mouse anti–α-adaptin (AP2), washed, and incubated with Alexa 568–conjugated goat anti-rabbit <t>IgG</t> (LDL receptors, red) and Alexa 488–conjugated goat anti-mouse IgG (AP2, green). Nuclei were stained with DAPI. The plates shown are an overlay of red and green images. The bar represents 5.0 μm. ( a and d ) Control cells; ( b and e ) cells from proband 1.1; ( c and f ) cells from proband 1.1 expressing viral c-myc-ARH. ( g – l ) EBV-lymphocytes ( g – i ) or cultured skin fibroblasts ( j – l ) from three different control subjects were incubated with anti–LDL receptor Ab at 4°C, permeabilized, and then incubated with anti–α-adaptin Ab (AP2) as described for a – f above. The bars represent 5.0 μm (in g for g – i , and in j for j – l ).
    Alexa 488 Conjugated Goat Anti Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Phenotypic and functional characterization of the IL-33-induced Breg-like cells (Breg IL-33 ) in the blood. A–C. Surface phenotype of Breg IL-33 : The IL-33-induced IL-10 producing B cells expressed high surface IgM (A), CD1d and CD25 (B), but down-regulated CD23 (FceRII) (B, C). Data shown in the table under (B) were results showing the Mean MFI (±SD) values calculated from results of 5 repeated experiments, as ratio of the IL-10 − B, and IL-10 + B, cell subset over the total B cells gated. Statistical analysis: p values (Student t test). D–F. In vitro Breg suppression assays: Immunosuppressive effects of the IL-33-induced Breg-like cells on B effector (Beff) cell proliferation (D), division (E), and its IL-10 dependency (F). D. CD23 + B cells (Beff, 10 5 ) were cultured in the presence of anti-CD40 (2.5 μg/ml), with titrating (as indicated) doses of CD23 − B cells (Breg IL-33 ) purified from the IL-33-injected mice. Cell proliferation was determined by thymidine incorporation at 48 h s. E. Breg IL-33 (CD23 - ) purified from hIL-33-injected WT mice (Wk-2) were primed with anti-CD40 (2.5 μg/ml) for 5 h before being added to CFSE-labelled CD23 + Beff cells. Cell division (CFSE dilution) was determined by flow cytometry at day 5 of culture in the presence or absence of LPS (0.5 μg/ml) or anti-IgM (5 μg/ml). F. IL-10 levels in the culture supernatants were quantified by ELISA (BD Biosciences).

    Journal: Journal of Autoimmunity

    Article Title: IL-10-producing regulatory B cells induced by IL-33 (BregIL-33) effectively attenuate mucosal inflammatory responses in the gut

    doi: 10.1016/j.jaut.2014.01.032

    Figure Lengend Snippet: Phenotypic and functional characterization of the IL-33-induced Breg-like cells (Breg IL-33 ) in the blood. A–C. Surface phenotype of Breg IL-33 : The IL-33-induced IL-10 producing B cells expressed high surface IgM (A), CD1d and CD25 (B), but down-regulated CD23 (FceRII) (B, C). Data shown in the table under (B) were results showing the Mean MFI (±SD) values calculated from results of 5 repeated experiments, as ratio of the IL-10 − B, and IL-10 + B, cell subset over the total B cells gated. Statistical analysis: p values (Student t test). D–F. In vitro Breg suppression assays: Immunosuppressive effects of the IL-33-induced Breg-like cells on B effector (Beff) cell proliferation (D), division (E), and its IL-10 dependency (F). D. CD23 + B cells (Beff, 10 5 ) were cultured in the presence of anti-CD40 (2.5 μg/ml), with titrating (as indicated) doses of CD23 − B cells (Breg IL-33 ) purified from the IL-33-injected mice. Cell proliferation was determined by thymidine incorporation at 48 h s. E. Breg IL-33 (CD23 - ) purified from hIL-33-injected WT mice (Wk-2) were primed with anti-CD40 (2.5 μg/ml) for 5 h before being added to CFSE-labelled CD23 + Beff cells. Cell division (CFSE dilution) was determined by flow cytometry at day 5 of culture in the presence or absence of LPS (0.5 μg/ml) or anti-IgM (5 μg/ml). F. IL-10 levels in the culture supernatants were quantified by ELISA (BD Biosciences).

    Article Snippet: Respectively, fixed numbers (105 ) of B responder cells (CD19+ CD23+ ) were cultured, in the presence or absence of anti-CD40 (2.5 μg/ml, Enzo Life Sciences, UK), anti-IgM (5 μg/ml, Thermo Scientific, UK) or LPS (0.5 μg/ml, Sigma–Aldrich, UK), with titrated doses of BregIL-33 (CD19+ CD23− ) isolated from IL-33-treated WT or IL-10−/− mice as described above.

    Techniques: Functional Assay, In Vitro, Cell Culture, Purification, Injection, Mouse Assay, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay

    Plasmodium falciparum EBA175RIII–V construct and expressed antigen. A schematic representation of the 1620 bp region of EBA175RIII–V cloned into the pLEA2 expression vector, which contains the nucleotide sequence of a hexahistidine tag inframe of the multiple cloning site ( a ). The culture supernatant (1) containing the secreted protein as well as the purified protein (2) was analysed by SDS-PAGE followed by coomassie staining ( b ) and a western blot probed with penta-His mouse monoclonal antibody (IgG1) ( c )

    Journal: Malaria Journal

    Article Title: Assessment of the quality and quantity of naturally induced antibody responses to EBA175RIII–V in Ghanaian children living in two communities with varying malaria transmission patterns

    doi: 10.1186/s12936-017-2167-3

    Figure Lengend Snippet: Plasmodium falciparum EBA175RIII–V construct and expressed antigen. A schematic representation of the 1620 bp region of EBA175RIII–V cloned into the pLEA2 expression vector, which contains the nucleotide sequence of a hexahistidine tag inframe of the multiple cloning site ( a ). The culture supernatant (1) containing the secreted protein as well as the purified protein (2) was analysed by SDS-PAGE followed by coomassie staining ( b ) and a western blot probed with penta-His mouse monoclonal antibody (IgG1) ( c )

    Article Snippet: The western blot was probed with penta-His mouse IgG1 monoclonal antibodies (Thermo Scientific, USA) followed by alkaline phosphatase conjugated goat anti mouse IgG (H + L) secondary antibodies (Thermo Scientific, USA).

    Techniques: Construct, Clone Assay, Expressing, Plasmid Preparation, Sequencing, Purification, SDS Page, Staining, Western Blot

    Characterization of cytophilic antibody responses. IgG1 ( a ) and IgG3 ( b ) antibody concentrations to EBA175RIII–V Ll in asymptomatic children from Obom and Abura measured in the peak malaria season (July). Processes similar to that described in Fig. 3 were used to determine the concentrations and avidity of IgG1 and IgG3, the only difference was that goat anti-human IgG1 and goat anti-human IgG3 secondary antibodies were used in place of the goat anti-human IgG. The graphs represent the median antibody concentrations with interquartile range as error bars

    Journal: Malaria Journal

    Article Title: Assessment of the quality and quantity of naturally induced antibody responses to EBA175RIII–V in Ghanaian children living in two communities with varying malaria transmission patterns

    doi: 10.1186/s12936-017-2167-3

    Figure Lengend Snippet: Characterization of cytophilic antibody responses. IgG1 ( a ) and IgG3 ( b ) antibody concentrations to EBA175RIII–V Ll in asymptomatic children from Obom and Abura measured in the peak malaria season (July). Processes similar to that described in Fig. 3 were used to determine the concentrations and avidity of IgG1 and IgG3, the only difference was that goat anti-human IgG1 and goat anti-human IgG3 secondary antibodies were used in place of the goat anti-human IgG. The graphs represent the median antibody concentrations with interquartile range as error bars

    Article Snippet: The western blot was probed with penta-His mouse IgG1 monoclonal antibodies (Thermo Scientific, USA) followed by alkaline phosphatase conjugated goat anti mouse IgG (H + L) secondary antibodies (Thermo Scientific, USA).

    Techniques:

    Characterization of IgG responses against EBA175RIII–V Ll . Antibody concentrations (ng/ml) of plasma obtained from the enrolled children from Obom and Abura ( a ) diluted 1:200 was determined using indirect ELISA and a EBA175RIII–V Ll as the antigen coated onto the ELISA plate and goat anti-human IgG used as the secondary antibody. The relative avidities of these same plasma samples were determined using a modified indirect ELISA assay where an incubation of the bound plasma samples obtained from children Obom and Abura ( b ) were treated with sodium thiocyanide is incorporated into the protocol. Plasma samples were obtained from whole blood collected from the children during the months of July 2015, October 2015 and February 2016. Data in the graphs are represented as the median with the interquartile range

    Journal: Malaria Journal

    Article Title: Assessment of the quality and quantity of naturally induced antibody responses to EBA175RIII–V in Ghanaian children living in two communities with varying malaria transmission patterns

    doi: 10.1186/s12936-017-2167-3

    Figure Lengend Snippet: Characterization of IgG responses against EBA175RIII–V Ll . Antibody concentrations (ng/ml) of plasma obtained from the enrolled children from Obom and Abura ( a ) diluted 1:200 was determined using indirect ELISA and a EBA175RIII–V Ll as the antigen coated onto the ELISA plate and goat anti-human IgG used as the secondary antibody. The relative avidities of these same plasma samples were determined using a modified indirect ELISA assay where an incubation of the bound plasma samples obtained from children Obom and Abura ( b ) were treated with sodium thiocyanide is incorporated into the protocol. Plasma samples were obtained from whole blood collected from the children during the months of July 2015, October 2015 and February 2016. Data in the graphs are represented as the median with the interquartile range

    Article Snippet: The western blot was probed with penta-His mouse IgG1 monoclonal antibodies (Thermo Scientific, USA) followed by alkaline phosphatase conjugated goat anti mouse IgG (H + L) secondary antibodies (Thermo Scientific, USA).

    Techniques: Indirect ELISA, Enzyme-linked Immunosorbent Assay, Modification, Incubation

    Confocal microscopy of cells labeled with anti–LDL receptor Ab. ( a – f ) EBV-lymphocytes were incubated with rabbit anti–LDL receptor (red) at 4°C, washed at 4°C, and either directly permeabilized ( a – c ) or incubated for 10 minutes at 37°C before permeabilization to allow internalization of LDL receptor/Ab complexes ( d – f ). Permeabilized cells were then incubated with mouse anti–α-adaptin (AP2), washed, and incubated with Alexa 568–conjugated goat anti-rabbit IgG (LDL receptors, red) and Alexa 488–conjugated goat anti-mouse IgG (AP2, green). Nuclei were stained with DAPI. The plates shown are an overlay of red and green images. The bar represents 5.0 μm. ( a and d ) Control cells; ( b and e ) cells from proband 1.1; ( c and f ) cells from proband 1.1 expressing viral c-myc-ARH. ( g – l ) EBV-lymphocytes ( g – i ) or cultured skin fibroblasts ( j – l ) from three different control subjects were incubated with anti–LDL receptor Ab at 4°C, permeabilized, and then incubated with anti–α-adaptin Ab (AP2) as described for a – f above. The bars represent 5.0 μm (in g for g – i , and in j for j – l ).

    Journal: The Journal of Clinical Investigation

    Article Title: Restoration of LDL receptor function in cells from patients with autosomal recessive hypercholesterolemia by retroviral expression of ARH1

    doi: 10.1172/JCI16445

    Figure Lengend Snippet: Confocal microscopy of cells labeled with anti–LDL receptor Ab. ( a – f ) EBV-lymphocytes were incubated with rabbit anti–LDL receptor (red) at 4°C, washed at 4°C, and either directly permeabilized ( a – c ) or incubated for 10 minutes at 37°C before permeabilization to allow internalization of LDL receptor/Ab complexes ( d – f ). Permeabilized cells were then incubated with mouse anti–α-adaptin (AP2), washed, and incubated with Alexa 568–conjugated goat anti-rabbit IgG (LDL receptors, red) and Alexa 488–conjugated goat anti-mouse IgG (AP2, green). Nuclei were stained with DAPI. The plates shown are an overlay of red and green images. The bar represents 5.0 μm. ( a and d ) Control cells; ( b and e ) cells from proband 1.1; ( c and f ) cells from proband 1.1 expressing viral c-myc-ARH. ( g – l ) EBV-lymphocytes ( g – i ) or cultured skin fibroblasts ( j – l ) from three different control subjects were incubated with anti–LDL receptor Ab at 4°C, permeabilized, and then incubated with anti–α-adaptin Ab (AP2) as described for a – f above. The bars represent 5.0 μm (in g for g – i , and in j for j – l ).

    Article Snippet: Cells were fixed in 4% (wt/vol) paraformaldehyde, permeabilized in PBS containing 0.1% Triton X-100 and 10 mM glycine, incubated sequentially for 1 hour at ambient temperature with mouse monoclonal anti–α-adaptin Ab (Santa Cruz Biotechnology Inc.; diluted 1/100), Alexa 568–conjugated goat anti-rabbit IgG (highly cross-absorbed; Molecular Probes Europe BV, Leiden, The Netherlands; diluted 1/100), and Alexa 488–conjugated goat anti-mouse IgG (highly cross-absorbed; Molecular Probes, diluted 1/100), and then mounted on slides with VECTASHIELD plus 4′,6-diamidine-2′-phenylindole dihydrochloride (DAPI) (Vector Laboratories, Peterborough, United Kingdom).

    Techniques: Confocal Microscopy, Labeling, Incubation, Staining, Expressing, Cell Culture