goat anti rabbit igg Millipore Search Results


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  • 81
    Millipore goat anti rabbit igg1 cy3
    Goat Anti Rabbit Igg1 Cy3, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg1 cy3/product/Millipore
    Average 81 stars, based on 22 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg1 cy3 - by Bioz Stars, 2020-02
    81/100 stars
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    99
    Millipore goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2945 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg/product/Millipore
    Average 99 stars, based on 2945 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg - by Bioz Stars, 2020-02
    99/100 stars
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    99
    Merck KGaA goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Goat Anti Rabbit Igg, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 99/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 52 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg - by Bioz Stars, 2020-02
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    75
    Millipore hrpconjugated goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Hrpconjugated Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 75/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 75 stars, based on 2 article reviews
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    79
    Millipore goat anti rabbit igg rpe
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Goat Anti Rabbit Igg Rpe, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 5 article reviews
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    99
    Millipore alexa 488 goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Alexa 488 Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 42 article reviews
    Price from $9.99 to $1999.99
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    99/100 stars
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    81
    Millipore cy5 goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Cy5 Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 81/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 81 stars, based on 22 article reviews
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    79
    Millipore rhodamine goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Rhodamine Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 11 article reviews
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    80
    Millipore alexa fluor goat anti rabbit igg
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Alexa Fluor Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor goat anti rabbit igg/product/Millipore
    Average 80 stars, based on 1 article reviews
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    alexa fluor goat anti rabbit igg - by Bioz Stars, 2020-02
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    80
    Millipore goat anti rabbit igg atto 594
    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) <t>IgE-binding</t> epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) <t>IgG4-binding</t> epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Goat Anti Rabbit Igg Atto 594, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 80 stars, based on 5 article reviews
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    goat anti rabbit igg atto 594 - by Bioz Stars, 2020-02
    80/100 stars
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    99
    Millipore biotinylated goat anti rabbit igg
    DDI of capture antibodies from goat directed against human <t>IgG</t> (GAH). Immobilization efficiencies of three alternative techniques are compared: <t>biotinylated</t> GAH was immobilized by either direct physisorption (triangles), biotin–STV interaction (rectangles) or DDI (circles). Serial dilutions of the target antigen (human IgG, hIgG) were incubated in the wells containing the capture antibody. Signal detection was carried out by either regular ELISA ( A ), using an anti-hIgG–STV–alkaline phosphatase conjugate and fluorescence detection or IPCR ( B ) using an anti-human IgG-STV-DNA conjugate and real-time TaqMan detection. The standard deviation of duplicate measurements was
    Biotinylated Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 512 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 512 article reviews
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    99
    Millipore fitc goat anti rabbit igg
    Antibodies against recombinant proteins recognize A . phagocytophilum in infected tick cells and ticks by immunofluorescence. (A) Uninfected and A . phagocytophilum (NY18)-infected ISE6 tick cells were characterized by immunofluorescence in (a, c, e, g) uninfected and (b, d, f, h) infected cells. Representative immunofluorescence images are shown for tick cells stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, <t>FITC;</t> blue, DAPI). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 5 μm. (B) Sections were made from I . scapularis female ticks after feeding on an uninfected (a, c, e) or A . phagocytophilum (NY18)-infected (b, d, f) sheep. Representative immunofluorescence images are shown for salivary gland sections stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 10 μm. (C) IDE8 tick cells were collected in low and high percentage A . phagocytophilum (L610)-infected cells and representative immunofluorescence images are shown. (a, b) Bright-field images of Giemsa-stained (a) low percentage and (b) high percentage infected tick cells. Bacteria stain purple (arrows) and host nuclei stain pink. (c) Low percentage and (d) high percentage infected tick cells were stained with rabbit anti- A . phagocytophilum HSP70 protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bar, 5 μm. (D) Flow cytometry profile showing MFI values determined using a FITC-conjugated secondary antibody. A . phagocytophilum (NY18)-infected and uninfected control ISE6 tick cells were washed, fixed, permeabilized and incubated with primary unlabeled antibody (preimmune <t>IgG</t> isotype control, MSP4, SOD, HSP70 and GroEL), washed in PBS and incubated with FITC-goat anti-rabbit IgG. MFI was calculated as the MFI of the test-labeled sample minus the MFI of the isotype control, shown as Ave+SD and compared between infected and uninfected tick cells by Student's t-test (*P
    Fitc Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 111 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 111 article reviews
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    fitc goat anti rabbit igg - by Bioz Stars, 2020-02
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    77
    Millipore 200 goat anti rabbit igg cy3
    Antibodies against recombinant proteins recognize A . phagocytophilum in infected tick cells and ticks by immunofluorescence. (A) Uninfected and A . phagocytophilum (NY18)-infected ISE6 tick cells were characterized by immunofluorescence in (a, c, e, g) uninfected and (b, d, f, h) infected cells. Representative immunofluorescence images are shown for tick cells stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, <t>FITC;</t> blue, DAPI). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 5 μm. (B) Sections were made from I . scapularis female ticks after feeding on an uninfected (a, c, e) or A . phagocytophilum (NY18)-infected (b, d, f) sheep. Representative immunofluorescence images are shown for salivary gland sections stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 10 μm. (C) IDE8 tick cells were collected in low and high percentage A . phagocytophilum (L610)-infected cells and representative immunofluorescence images are shown. (a, b) Bright-field images of Giemsa-stained (a) low percentage and (b) high percentage infected tick cells. Bacteria stain purple (arrows) and host nuclei stain pink. (c) Low percentage and (d) high percentage infected tick cells were stained with rabbit anti- A . phagocytophilum HSP70 protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bar, 5 μm. (D) Flow cytometry profile showing MFI values determined using a FITC-conjugated secondary antibody. A . phagocytophilum (NY18)-infected and uninfected control ISE6 tick cells were washed, fixed, permeabilized and incubated with primary unlabeled antibody (preimmune <t>IgG</t> isotype control, MSP4, SOD, HSP70 and GroEL), washed in PBS and incubated with FITC-goat anti-rabbit IgG. MFI was calculated as the MFI of the test-labeled sample minus the MFI of the isotype control, shown as Ave+SD and compared between infected and uninfected tick cells by Student's t-test (*P
    200 Goat Anti Rabbit Igg Cy3, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/200 goat anti rabbit igg cy3/product/Millipore
    Average 77 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    200 goat anti rabbit igg cy3 - by Bioz Stars, 2020-02
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    89
    Millipore cy3 affinipure goat anti rabbit igg
    Antibodies against recombinant proteins recognize A . phagocytophilum in infected tick cells and ticks by immunofluorescence. (A) Uninfected and A . phagocytophilum (NY18)-infected ISE6 tick cells were characterized by immunofluorescence in (a, c, e, g) uninfected and (b, d, f, h) infected cells. Representative immunofluorescence images are shown for tick cells stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, <t>FITC;</t> blue, DAPI). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 5 μm. (B) Sections were made from I . scapularis female ticks after feeding on an uninfected (a, c, e) or A . phagocytophilum (NY18)-infected (b, d, f) sheep. Representative immunofluorescence images are shown for salivary gland sections stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 10 μm. (C) IDE8 tick cells were collected in low and high percentage A . phagocytophilum (L610)-infected cells and representative immunofluorescence images are shown. (a, b) Bright-field images of Giemsa-stained (a) low percentage and (b) high percentage infected tick cells. Bacteria stain purple (arrows) and host nuclei stain pink. (c) Low percentage and (d) high percentage infected tick cells were stained with rabbit anti- A . phagocytophilum HSP70 protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bar, 5 μm. (D) Flow cytometry profile showing MFI values determined using a FITC-conjugated secondary antibody. A . phagocytophilum (NY18)-infected and uninfected control ISE6 tick cells were washed, fixed, permeabilized and incubated with primary unlabeled antibody (preimmune <t>IgG</t> isotype control, MSP4, SOD, HSP70 and GroEL), washed in PBS and incubated with FITC-goat anti-rabbit IgG. MFI was calculated as the MFI of the test-labeled sample minus the MFI of the isotype control, shown as Ave+SD and compared between infected and uninfected tick cells by Student's t-test (*P
    Cy3 Affinipure Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 89 stars, based on 7 article reviews
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    cy3 affinipure goat anti rabbit igg - by Bioz Stars, 2020-02
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    80
    Millipore goat anti rabbit igg gold conjugate
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Goat Anti Rabbit Igg Gold Conjugate, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Merck KGaA goat anti rabbit igg cy3 conjugate
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Goat Anti Rabbit Igg Cy3 Conjugate, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Millipore alkaline phosphataseconjugated goat anti rabbit igg
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Alkaline Phosphataseconjugated Goat Anti Rabbit Igg, supplied by Millipore, used in various techniques. Bioz Stars score: 82/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 82 stars, based on 8 article reviews
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    80
    Millipore goat anti rabbit igg agarose
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Goat Anti Rabbit Igg Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Millipore goat anti rabbit igg tritc
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Goat Anti Rabbit Igg Tritc, supplied by Millipore, used in various techniques. Bioz Stars score: 82/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 82 stars, based on 18 article reviews
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    81
    Merck KGaA goat anti rabbit igg tritc
    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
    Goat Anti Rabbit Igg Tritc, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 81/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with <t>polyclonal</t> rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit <t>IgG</t> gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.
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    Purification of <t>(anti-rLipL21)</t> <t>IgG</t> antibody was purified from rabbit antiserum against rLipL21. Lane L: anti-rLipL21 serum; Lane FT: flow through of unbound proteins from column; Lane W: wash of nonspecific proteins from column; Lane 1: eluted fraction without protein; Lane 2: purified anti-rLipL21-IgG; Lane 3: concentrated anti-rLipL21-IgG. Molecular weight standards are indicated in kilodaltons.
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    Purification of <t>(anti-rLipL21)</t> <t>IgG</t> antibody was purified from rabbit antiserum against rLipL21. Lane L: anti-rLipL21 serum; Lane FT: flow through of unbound proteins from column; Lane W: wash of nonspecific proteins from column; Lane 1: eluted fraction without protein; Lane 2: purified anti-rLipL21-IgG; Lane 3: concentrated anti-rLipL21-IgG. Molecular weight standards are indicated in kilodaltons.
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    Purification of <t>(anti-rLipL21)</t> <t>IgG</t> antibody was purified from rabbit antiserum against rLipL21. Lane L: anti-rLipL21 serum; Lane FT: flow through of unbound proteins from column; Lane W: wash of nonspecific proteins from column; Lane 1: eluted fraction without protein; Lane 2: purified anti-rLipL21-IgG; Lane 3: concentrated anti-rLipL21-IgG. Molecular weight standards are indicated in kilodaltons.
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    Localization of maize PSY1 in maize B73 endosperm. Endosperm dissected at 17 DAP was probed with: A, anti-maize PSY1 antiserum and anti-rabbit <t>IgG</t> <t>FITC</t> conjugate; or B, anti-rabbit IgG FITC conjugate only. Bar = 50 μ m (A) and 100 μ m (B). Arrow points to amyloplast within an endosperm cell.
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    Image Search Results


    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.

    Journal: Scientific Reports

    Article Title: The amyloid fold of Gad m 1 epitopes governs IgE binding

    doi: 10.1038/srep32801

    Figure Lengend Snippet: Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.

    Article Snippet: After extensive washes with TBST, a 30 min incubation with either horseradish peroxidase-labeled anti-human IgE (Abcam ab99806, 1/2,000 dilution), anti-human IgG4 (Abcam ab99823, 1/4,000 dilution), goat anti-rabbit IgG (Sigma, 1/5,000 dilution) or anti-6X His tag® antibody (Abcam ab18184, dilution 1/1,000) was performed.

    Techniques: Sequencing, Binding Assay, Mutagenesis

    Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).

    Journal: Scientific Reports

    Article Title: The amyloid fold of Gad m 1 epitopes governs IgE binding

    doi: 10.1038/srep32801

    Figure Lengend Snippet: Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).

    Article Snippet: After extensive washes with TBST, a 30 min incubation with either horseradish peroxidase-labeled anti-human IgE (Abcam ab99806, 1/2,000 dilution), anti-human IgG4 (Abcam ab99823, 1/4,000 dilution), goat anti-rabbit IgG (Sigma, 1/5,000 dilution) or anti-6X His tag® antibody (Abcam ab18184, dilution 1/1,000) was performed.

    Techniques: Binding Assay, Fluorescence In Situ Hybridization, Sequencing

    Blockade of Sema4a but not IFNαR1 signaling increases bronchiolitis severity and predisposes to subsequent asthma. (a) Protocol of PVM inoculation and administration of αSema4a or isotype control (IgG2a) and αIFNαR or isotype control (IgG1) to neonatal WT mice. (b) IFN-α protein expression in BALF, expressed as % change of the respective isotype control. (c) Viral load in the airway epithelium. (d) Nrp-1 + T reg cells in the lung. (e) IL-10 protein expression in lung, expressed as % change of the respective isotype control. (f) CD39 expression by Nrp-1 + T reg cells. (g) Sloughing of the airway epithelium. (h) Eosinophil number in BAL. (i) IL-33 protein expression in lung, expressed as % change of the respective isotype control. (j) Type-2 ILCs in lung. (k) AHR. (l) ASM area. (m) Intraluminal mucus plugging. (n) Eosinophil number in BAL. (o) IL-13 protein expression in BAL. Data are representative of n = 2 experiments with four to six neonates in each group and are presented as the mean ± SEM (k) or box-and-whisker plots showing quartiles (boxes) and range (whiskers; b–o). Data were analyzed by one-way (b–j and l–o) or two-way (k) ANOVA with Tukey’s post hoc test; *, P

    Journal: The Journal of Experimental Medicine

    Article Title: Plasmacytoid dendritic cells protect from viral bronchiolitis and asthma through semaphorin 4a–mediated T reg expansion

    doi: 10.1084/jem.20170298

    Figure Lengend Snippet: Blockade of Sema4a but not IFNαR1 signaling increases bronchiolitis severity and predisposes to subsequent asthma. (a) Protocol of PVM inoculation and administration of αSema4a or isotype control (IgG2a) and αIFNαR or isotype control (IgG1) to neonatal WT mice. (b) IFN-α protein expression in BALF, expressed as % change of the respective isotype control. (c) Viral load in the airway epithelium. (d) Nrp-1 + T reg cells in the lung. (e) IL-10 protein expression in lung, expressed as % change of the respective isotype control. (f) CD39 expression by Nrp-1 + T reg cells. (g) Sloughing of the airway epithelium. (h) Eosinophil number in BAL. (i) IL-33 protein expression in lung, expressed as % change of the respective isotype control. (j) Type-2 ILCs in lung. (k) AHR. (l) ASM area. (m) Intraluminal mucus plugging. (n) Eosinophil number in BAL. (o) IL-13 protein expression in BAL. Data are representative of n = 2 experiments with four to six neonates in each group and are presented as the mean ± SEM (k) or box-and-whisker plots showing quartiles (boxes) and range (whiskers; b–o). Data were analyzed by one-way (b–j and l–o) or two-way (k) ANOVA with Tukey’s post hoc test; *, P

    Article Snippet: Sections were washed three times in PBS/0.05% Tween-20 before incubation with biotinylated anti-mouse polyclonal antibody (Invitrogen; for PVM detection), goat anti–rabbit IgG-AP (Sigma-Aldrich; periostin), or goat anti–mouse IgG-AP (Sigma-Aldrich; α-smooth muscle actin).

    Techniques: Mouse Assay, Expressing, Whisker Assay

    The required amount of recombinant enzyme for antibody saturation can be calculated using patients' purified total IgGs. (A) Determination of the individual antibody status before and after infusion. (B) Effect of infused ERT amounts (gray) on antibody titer (black) during infusion and agalsidase activity (green). The longitudinal measurement of ADA titers during infusions allows estimating the amount of enzyme required to saturate ADAs. (C) Titration of purified total IgG against ERT allows calculating the required amount of enzyme from one serum sample. The determination of the individual amount of recombinant GLA to saturate ADAs was performed using titration and subsequent calculation. First, a titration was performed to identify the required amount of enzyme to saturate 90% of 5 µ g total IgGs (see Methods). ERT inhibition was plotted against the amount of enzyme. The amount required can be identified on the y -axis (here 10 ng, dashed orange line), showing that 2 ng is sufficient to saturate 1 µ g total IgG. In the example shown, the patient’s measured IgG concentration was 9.5 mg/ml serum. Because each patient has approximately 3 L of serum, the total amount of patient’s IgGs per total volume of serum was calculated with 28.5 g. Therefore, the amount of enzyme required to saturate 90% of all IgGs was 57 mg (28.5 g×2/1000=57 mg). (D) Crosstitration of agalsidase- α and agalsidase- β demonstrates similar ADA saturation of either type of enzyme.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: Dose-Dependent Effect of Enzyme Replacement Therapy on Neutralizing Antidrug Antibody Titers and Clinical Outcome in Patients with Fabry Disease

    doi: 10.1681/ASN.2018070740

    Figure Lengend Snippet: The required amount of recombinant enzyme for antibody saturation can be calculated using patients' purified total IgGs. (A) Determination of the individual antibody status before and after infusion. (B) Effect of infused ERT amounts (gray) on antibody titer (black) during infusion and agalsidase activity (green). The longitudinal measurement of ADA titers during infusions allows estimating the amount of enzyme required to saturate ADAs. (C) Titration of purified total IgG against ERT allows calculating the required amount of enzyme from one serum sample. The determination of the individual amount of recombinant GLA to saturate ADAs was performed using titration and subsequent calculation. First, a titration was performed to identify the required amount of enzyme to saturate 90% of 5 µ g total IgGs (see Methods). ERT inhibition was plotted against the amount of enzyme. The amount required can be identified on the y -axis (here 10 ng, dashed orange line), showing that 2 ng is sufficient to saturate 1 µ g total IgG. In the example shown, the patient’s measured IgG concentration was 9.5 mg/ml serum. Because each patient has approximately 3 L of serum, the total amount of patient’s IgGs per total volume of serum was calculated with 28.5 g. Therefore, the amount of enzyme required to saturate 90% of all IgGs was 57 mg (28.5 g×2/1000=57 mg). (D) Crosstitration of agalsidase- α and agalsidase- β demonstrates similar ADA saturation of either type of enzyme.

    Article Snippet: Detection was performed using anti-GLA antibody (ab168341, dilution: 1:10,000; Abcam) and a horseradish-peroxidase–labeled goat anti-rabbit IgG antibody (dilution: 1:20,000; Sigma-Aldrich).

    Techniques: Recombinant, Purification, Activity Assay, Titration, Inhibition, Concentration Assay

    Immune responses following intranasal immunization with MBPS1S1CtxA2B. (A) Specific titers of IgA antibody in saliva. (B) Specific titers of IgG antibody in sera. (C) Specific titers of IgA antibody in BAL and VW. Symbols: ▪, anti-PT antibodies; □, anti-CtxB antibodies; , anti-PT antibodies in PTd-immunized samples. In panels A and B, for the PTd group, only samples from the last time point were assayed. Results are mean titers (± standard error; n = 5) for individual animal samples.

    Journal: Infection and Immunity

    Article Title: Mucosal Immunization with a Genetically Engineered Pertussis Toxin S1 Fragment-Cholera Toxin Subunit B Chimeric Protein

    doi: 10.1128/IAI.71.4.2272-2275.2003

    Figure Lengend Snippet: Immune responses following intranasal immunization with MBPS1S1CtxA2B. (A) Specific titers of IgA antibody in saliva. (B) Specific titers of IgG antibody in sera. (C) Specific titers of IgA antibody in BAL and VW. Symbols: ▪, anti-PT antibodies; □, anti-CtxB antibodies; , anti-PT antibodies in PTd-immunized samples. In panels A and B, for the PTd group, only samples from the last time point were assayed. Results are mean titers (± standard error; n = 5) for individual animal samples.

    Article Snippet: The chimeric protein bound to GM1 was detected with a rabbit anti-PT (1/300; [ ]) or a goat anti-CtxB antibody followed by the goat anti-rabbit immunoglobulin G (IgG) (1/30,000; Sigma) or rabbit anti-goat IgG (1/20,000; Sigma) alkaline phosphatase conjugates, respectively.

    Techniques:

    DDI of capture antibodies from goat directed against human IgG (GAH). Immobilization efficiencies of three alternative techniques are compared: biotinylated GAH was immobilized by either direct physisorption (triangles), biotin–STV interaction (rectangles) or DDI (circles). Serial dilutions of the target antigen (human IgG, hIgG) were incubated in the wells containing the capture antibody. Signal detection was carried out by either regular ELISA ( A ), using an anti-hIgG–STV–alkaline phosphatase conjugate and fluorescence detection or IPCR ( B ) using an anti-human IgG-STV-DNA conjugate and real-time TaqMan detection. The standard deviation of duplicate measurements was

    Journal: Nucleic Acids Research

    Article Title: Combination of DNA-directed immobilization and immuno-PCR: very sensitive antigen detection by means of self-assembled DNA-protein conjugates

    doi:

    Figure Lengend Snippet: DDI of capture antibodies from goat directed against human IgG (GAH). Immobilization efficiencies of three alternative techniques are compared: biotinylated GAH was immobilized by either direct physisorption (triangles), biotin–STV interaction (rectangles) or DDI (circles). Serial dilutions of the target antigen (human IgG, hIgG) were incubated in the wells containing the capture antibody. Signal detection was carried out by either regular ELISA ( A ), using an anti-hIgG–STV–alkaline phosphatase conjugate and fluorescence detection or IPCR ( B ) using an anti-human IgG-STV-DNA conjugate and real-time TaqMan detection. The standard deviation of duplicate measurements was

    Article Snippet: Preconjugates of HA24 and biotinylated antibodies were prepared by mixing 0.01 mM stock solutions of HA24 and equimolar amounts (0.01 mM stock solution) of biotinylated goat anti-rabbit IgG (Sigma), biotinylated goat anti-human IgG (Biotrend) or biotinylated rabbit anti-CEA (Dako) [biotinylated with NHS-Biotin (Pierce) according to the manufacturer’s instructions] in buffer A (10 mM Tris buffer, pH 7.5, containing 5 mM EDTA).

    Techniques: Incubation, Enzyme-linked Immunosorbent Assay, Fluorescence, Standard Deviation

    Antibodies against recombinant proteins recognize A . phagocytophilum in infected tick cells and ticks by immunofluorescence. (A) Uninfected and A . phagocytophilum (NY18)-infected ISE6 tick cells were characterized by immunofluorescence in (a, c, e, g) uninfected and (b, d, f, h) infected cells. Representative immunofluorescence images are shown for tick cells stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC; blue, DAPI). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 5 μm. (B) Sections were made from I . scapularis female ticks after feeding on an uninfected (a, c, e) or A . phagocytophilum (NY18)-infected (b, d, f) sheep. Representative immunofluorescence images are shown for salivary gland sections stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 10 μm. (C) IDE8 tick cells were collected in low and high percentage A . phagocytophilum (L610)-infected cells and representative immunofluorescence images are shown. (a, b) Bright-field images of Giemsa-stained (a) low percentage and (b) high percentage infected tick cells. Bacteria stain purple (arrows) and host nuclei stain pink. (c) Low percentage and (d) high percentage infected tick cells were stained with rabbit anti- A . phagocytophilum HSP70 protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bar, 5 μm. (D) Flow cytometry profile showing MFI values determined using a FITC-conjugated secondary antibody. A . phagocytophilum (NY18)-infected and uninfected control ISE6 tick cells were washed, fixed, permeabilized and incubated with primary unlabeled antibody (preimmune IgG isotype control, MSP4, SOD, HSP70 and GroEL), washed in PBS and incubated with FITC-goat anti-rabbit IgG. MFI was calculated as the MFI of the test-labeled sample minus the MFI of the isotype control, shown as Ave+SD and compared between infected and uninfected tick cells by Student's t-test (*P

    Journal: PLoS ONE

    Article Title: Identification and Characterization of Anaplasma phagocytophilum Proteins Involved in Infection of the Tick Vector, Ixodes scapularis

    doi: 10.1371/journal.pone.0137237

    Figure Lengend Snippet: Antibodies against recombinant proteins recognize A . phagocytophilum in infected tick cells and ticks by immunofluorescence. (A) Uninfected and A . phagocytophilum (NY18)-infected ISE6 tick cells were characterized by immunofluorescence in (a, c, e, g) uninfected and (b, d, f, h) infected cells. Representative immunofluorescence images are shown for tick cells stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC; blue, DAPI). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 5 μm. (B) Sections were made from I . scapularis female ticks after feeding on an uninfected (a, c, e) or A . phagocytophilum (NY18)-infected (b, d, f) sheep. Representative immunofluorescence images are shown for salivary gland sections stained with rabbit preimmune (control) or anti- A . phagocytophilum protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bars, 10 μm. (C) IDE8 tick cells were collected in low and high percentage A . phagocytophilum (L610)-infected cells and representative immunofluorescence images are shown. (a, b) Bright-field images of Giemsa-stained (a) low percentage and (b) high percentage infected tick cells. Bacteria stain purple (arrows) and host nuclei stain pink. (c) Low percentage and (d) high percentage infected tick cells were stained with rabbit anti- A . phagocytophilum HSP70 protein antibodies (green, FITC). Arrows show the localization of A . phagocytophilum proteins in infected cells. Bar, 5 μm. (D) Flow cytometry profile showing MFI values determined using a FITC-conjugated secondary antibody. A . phagocytophilum (NY18)-infected and uninfected control ISE6 tick cells were washed, fixed, permeabilized and incubated with primary unlabeled antibody (preimmune IgG isotype control, MSP4, SOD, HSP70 and GroEL), washed in PBS and incubated with FITC-goat anti-rabbit IgG. MFI was calculated as the MFI of the test-labeled sample minus the MFI of the isotype control, shown as Ave+SD and compared between infected and uninfected tick cells by Student's t-test (*P

    Article Snippet: After permeabilization, the cells were washed in PBS and incubated with primary unlabeled antibody (preimmune IgG isotype control, MSP4, SOD, HSP70 and GroEL; 50 μg ml-1 ), washed in PBS and incubated in 100 μl of PBS with FITC-goat anti-rabbit IgG (Sigma, Madrid, Spain) labeled antibody (diluted 1/500) for 15 min at 4°C.

    Techniques: Recombinant, Infection, Immunofluorescence, Staining, Flow Cytometry, Cytometry, Incubation, Labeling

    Co-localization of SARS-CoV NP and p42 in 2BS cells . ( A ) SARS-CoV NP was expressed in 2BS cells transfected with recombinant -pcDNA3.0+SNP22b (left panel), 2BS cells transfected with pcDNA3.0 (right panel; negative control). ( B ) Proteasome subunit p42 in 2BS cells localized with anti-p42 antibody and anti-rabbit IgG-FITC conjugate, excitation at 488 nm (lane 1). SARS-CoV NP expressed in 2BS cells, localized using an anti-SARS-CoV NP mAb and anti-mouse IgG-TRITC conjugate, excitation at 568 nm (lane 2). Co-localization was detected by merging lanes 1 and 2 (lane 3).

    Journal: Virology Journal

    Article Title: Interactions of SARS Coronavirus Nucleocapsid Protein with the host cell proteasome subunit p42

    doi: 10.1186/1743-422X-7-99

    Figure Lengend Snippet: Co-localization of SARS-CoV NP and p42 in 2BS cells . ( A ) SARS-CoV NP was expressed in 2BS cells transfected with recombinant -pcDNA3.0+SNP22b (left panel), 2BS cells transfected with pcDNA3.0 (right panel; negative control). ( B ) Proteasome subunit p42 in 2BS cells localized with anti-p42 antibody and anti-rabbit IgG-FITC conjugate, excitation at 488 nm (lane 1). SARS-CoV NP expressed in 2BS cells, localized using an anti-SARS-CoV NP mAb and anti-mouse IgG-TRITC conjugate, excitation at 568 nm (lane 2). Co-localization was detected by merging lanes 1 and 2 (lane 3).

    Article Snippet: After incubation with a 1:80 dilution of goat anti-rabbit IgG-FITC (Sigma) and a 1:200 dilution of goat anti-mouse IgG-TRITC (Sigma) conjugates at 37°C for 45 min, coverslips were again washed six times in distilled water and air-dried before being mounted on a slide with interspaces containing 50% (v/v) glycerol.

    Techniques: Transfection, Recombinant, Negative Control

    Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with polyclonal rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit IgG gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.

    Journal: Journal of Bacteriology

    Article Title: Genomic Diversity of Burkholderia pseudomallei Clinical Isolates: Subtractive Hybridization Reveals a Burkholderia mallei-Specific Prophage in B. pseudomallei 1026b

    doi: 10.1128/JB.186.12.3938-3950.2004

    Figure Lengend Snippet: Immunogold electron microscopy of bacteriophages φE125 and φ1026b. The bacteriophages were reacted with polyclonal rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit IgG gold conjugate (5 nm). Bacteriophage φ1026b was subsequently negatively stained with 1% PTA. Scale bar = 100 nm.

    Article Snippet: Briefly, φE125 and φ1026b were reacted with polyclonal rabbit antiserum directed against φE125, washed, and reacted with goat anti-rabbit IgG gold conjugate (Sigma).

    Techniques: Electron Microscopy, Staining

    Purification of (anti-rLipL21) IgG antibody was purified from rabbit antiserum against rLipL21. Lane L: anti-rLipL21 serum; Lane FT: flow through of unbound proteins from column; Lane W: wash of nonspecific proteins from column; Lane 1: eluted fraction without protein; Lane 2: purified anti-rLipL21-IgG; Lane 3: concentrated anti-rLipL21-IgG. Molecular weight standards are indicated in kilodaltons.

    Journal: BioMed Research International

    Article Title: Production and Characterization of a Polyclonal Antibody of Anti-rLipL21-IgG against Leptospira for Early Detection of Acute Leptospirosis

    doi: 10.1155/2014/592858

    Figure Lengend Snippet: Purification of (anti-rLipL21) IgG antibody was purified from rabbit antiserum against rLipL21. Lane L: anti-rLipL21 serum; Lane FT: flow through of unbound proteins from column; Lane W: wash of nonspecific proteins from column; Lane 1: eluted fraction without protein; Lane 2: purified anti-rLipL21-IgG; Lane 3: concentrated anti-rLipL21-IgG. Molecular weight standards are indicated in kilodaltons.

    Article Snippet: These membranes were then probed using purified anti-rLipL21-IgG at a 1 : 30,000 dilution of primary rabbit serum (anti-rLipL21) and goat anti-rabbit IgG-alkaline phosphatase (Calbiochem, Germany) at a 1 : 10,000 dilution as a secondary antibody, with BCIP and NBT substrates (Novagen, USA).

    Techniques: Purification, Flow Cytometry, Molecular Weight

    Immunoblot of panel of Leptospira spp. obtained by using rabbit anti-rLipL21-IgG antibody to detect single band in leptospiral LipL21 antigen in detergent phase. Lane 1: Canicola (strain Hond Utrecht IV); Lane 2: Hardjobovis (Sponselee); Lane 3: Autumnalis (strain Akiyami A); Lane 4: Icterohaemorrhagiae (strain RGA); Lane 5: Australis (strain Ballico); Lane 6: Pomona (strain Pomona); Lane 7: Grippotyphosa (strain Moskva V); Lane 8: L. kmetyi serovar Malaysia strain Bejo-iso 9 T ; Lane 9: Balum (strain Mus 127); Lane 10: Grippotyphosa (strain Moskva V); Lane 11: Hebdomadis (strain Hebdomadis); Lane 12: nonpathogenic species L. biflexa (strain Patoc 1). Molecular weight standards are indicated in kilodaltons.

    Journal: BioMed Research International

    Article Title: Production and Characterization of a Polyclonal Antibody of Anti-rLipL21-IgG against Leptospira for Early Detection of Acute Leptospirosis

    doi: 10.1155/2014/592858

    Figure Lengend Snippet: Immunoblot of panel of Leptospira spp. obtained by using rabbit anti-rLipL21-IgG antibody to detect single band in leptospiral LipL21 antigen in detergent phase. Lane 1: Canicola (strain Hond Utrecht IV); Lane 2: Hardjobovis (Sponselee); Lane 3: Autumnalis (strain Akiyami A); Lane 4: Icterohaemorrhagiae (strain RGA); Lane 5: Australis (strain Ballico); Lane 6: Pomona (strain Pomona); Lane 7: Grippotyphosa (strain Moskva V); Lane 8: L. kmetyi serovar Malaysia strain Bejo-iso 9 T ; Lane 9: Balum (strain Mus 127); Lane 10: Grippotyphosa (strain Moskva V); Lane 11: Hebdomadis (strain Hebdomadis); Lane 12: nonpathogenic species L. biflexa (strain Patoc 1). Molecular weight standards are indicated in kilodaltons.

    Article Snippet: These membranes were then probed using purified anti-rLipL21-IgG at a 1 : 30,000 dilution of primary rabbit serum (anti-rLipL21) and goat anti-rabbit IgG-alkaline phosphatase (Calbiochem, Germany) at a 1 : 10,000 dilution as a secondary antibody, with BCIP and NBT substrates (Novagen, USA).

    Techniques: Molecular Weight

    Localization of maize PSY1 in maize B73 endosperm. Endosperm dissected at 17 DAP was probed with: A, anti-maize PSY1 antiserum and anti-rabbit IgG FITC conjugate; or B, anti-rabbit IgG FITC conjugate only. Bar = 50 μ m (A) and 100 μ m (B). Arrow points to amyloplast within an endosperm cell.

    Journal: Plant Physiology

    Article Title: The Maize Phytoene Synthase Gene Family: Overlapping Roles for Carotenogenesis in Endosperm, Photomorphogenesis, and Thermal Stress Tolerance

    doi: 10.1104/pp.108.122119

    Figure Lengend Snippet: Localization of maize PSY1 in maize B73 endosperm. Endosperm dissected at 17 DAP was probed with: A, anti-maize PSY1 antiserum and anti-rabbit IgG FITC conjugate; or B, anti-rabbit IgG FITC conjugate only. Bar = 50 μ m (A) and 100 μ m (B). Arrow points to amyloplast within an endosperm cell.

    Article Snippet: Slides were rehydrated in phosphate-buffered saline (PBS; 137 m m NaCl, 2.7 m m KCl, 4.3 m m Na2 HPO4 , 1.4 m m KH2 PO4 ) for 15 min, blocked in 0.5% (w/v) bovine serum albumin (BSA) in PBS for 30 min, incubated with primary antiserum (anti-maize PSY1) diluted at 1:25 in BSA/PBS overnight in a moist chamber, washed with PBS three times (5 min each), labeled with the goat anti-rabbit IgG-FITC conjugate (Sigma Diagnostics) for 2 h, and washed with PBS three times at 5 min each.

    Techniques: