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    Santa Cruz Biotechnology horseradish peroxidase hrp linked goat antirabbit igg
    Horseradish Peroxidase Hrp Linked Goat Antirabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 81/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp linked goat anti mouse igg
    Horseradish Peroxidase Hrp Linked Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp linked donkey anti goat igg
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    Santa Cruz Biotechnology horseradish peroxidase linked anti goat igg
    Constitutive binding of <t>HuR</t> to the 5′UTR of Caspase-2 mRNA in DLD-1 cells. ( a ) An RNP-IP assay was performed in combination with RT-PCR from total cell lysates of DLD-1 cells to amplify mRNA species specifically bound by HuR. HuR-bound mRNA was precipitated by addition of a monoclonal HuR antibody (HuR) or, alternatively, the same amount of mouse <t>IgG</t> (IgG) as negative control. After elution from Sepharose beads, the isolated RNA samples were analyzed by RT-PCR using primer pairs, complementary and specific to the coding region of the indicated genes. The length of corresponding PCR products was determined by a DNA ladder. The specific immunoprecipitation (IP) of HuR is confirmed by western blot analysis (W.blot) shown in the right part of the panel. Data shown are representative of two independent experiments giving similar results. ( b , upper panel) Schematic representation of the different splice variants from human caspase-2 mRNA including caspase-2L (v1), caspase-2S (v2), and variant 3 (v3) encoding transcripts. The relative position of start (gray) and stop (dark) codons is depicted by triangles. Boxes show the relative position of exons and lacking exons are symbolized by a continuous line. The doubleheaded arrows indicate different regions (I, III and IV) encompassing variant-specific sequences (lines) or a region (II) commonly found in all three splice variants (dotted). ( b , lower panel) Crosslinking-RNP-IP analysis demonstrating that HuR specifically interacts with the 5′UTR of caspase-2L (v1) and splice variant 3, respectively. RNA-protein interactions were crosslinked with formaldehyde before HuR-bound mRNA was immunoprecipitated by addition of a HuR-specific antibody (HuR) or, alternatively, by the same amount of mouse IgG (IgG). The precipitated RNA samples were analyzed by RT-PCR by using primer pairs, spanning the indicated regions of caspase-2 mRNA (roman numerals). Input levels of different caspase-2 transcripts were isolated before the IP and were assessed by RT-PCR using the same primer pairs. ( c ) Biotin pull-down assay demonstrating a specific HuR binding to the 5′UTR of caspase-2. For pull-down assay, the biotinylated transcript encompassing 241 nucleotides of the 5′UTR of human caspase-2 (5′UTR Casp-2) was incubated with 300 μ g of total cell lysates from DLD-1 cells. The specific binding of HuR in the pull-down material was confirmed by western blotting. Biotinylated RNA from partial human reverse GAPDH (hrg) was used as a negative control, whereas 0.1 μ g of recombinant HuR (GST-HuR) instead of cell lysates was incubated with the same amount of biotinylated 5′UTR of caspase-2 and used as a positive control. Data shown are representative of two independent experiments giving similar results
    Horseradish Peroxidase Linked Anti Goat Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 82/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp linked goat anti rabbit igg antibodies
    Constitutive binding of <t>HuR</t> to the 5′UTR of Caspase-2 mRNA in DLD-1 cells. ( a ) An RNP-IP assay was performed in combination with RT-PCR from total cell lysates of DLD-1 cells to amplify mRNA species specifically bound by HuR. HuR-bound mRNA was precipitated by addition of a monoclonal HuR antibody (HuR) or, alternatively, the same amount of mouse <t>IgG</t> (IgG) as negative control. After elution from Sepharose beads, the isolated RNA samples were analyzed by RT-PCR using primer pairs, complementary and specific to the coding region of the indicated genes. The length of corresponding PCR products was determined by a DNA ladder. The specific immunoprecipitation (IP) of HuR is confirmed by western blot analysis (W.blot) shown in the right part of the panel. Data shown are representative of two independent experiments giving similar results. ( b , upper panel) Schematic representation of the different splice variants from human caspase-2 mRNA including caspase-2L (v1), caspase-2S (v2), and variant 3 (v3) encoding transcripts. The relative position of start (gray) and stop (dark) codons is depicted by triangles. Boxes show the relative position of exons and lacking exons are symbolized by a continuous line. The doubleheaded arrows indicate different regions (I, III and IV) encompassing variant-specific sequences (lines) or a region (II) commonly found in all three splice variants (dotted). ( b , lower panel) Crosslinking-RNP-IP analysis demonstrating that HuR specifically interacts with the 5′UTR of caspase-2L (v1) and splice variant 3, respectively. RNA-protein interactions were crosslinked with formaldehyde before HuR-bound mRNA was immunoprecipitated by addition of a HuR-specific antibody (HuR) or, alternatively, by the same amount of mouse IgG (IgG). The precipitated RNA samples were analyzed by RT-PCR by using primer pairs, spanning the indicated regions of caspase-2 mRNA (roman numerals). Input levels of different caspase-2 transcripts were isolated before the IP and were assessed by RT-PCR using the same primer pairs. ( c ) Biotin pull-down assay demonstrating a specific HuR binding to the 5′UTR of caspase-2. For pull-down assay, the biotinylated transcript encompassing 241 nucleotides of the 5′UTR of human caspase-2 (5′UTR Casp-2) was incubated with 300 μ g of total cell lysates from DLD-1 cells. The specific binding of HuR in the pull-down material was confirmed by western blotting. Biotinylated RNA from partial human reverse GAPDH (hrg) was used as a negative control, whereas 0.1 μ g of recombinant HuR (GST-HuR) instead of cell lysates was incubated with the same amount of biotinylated 5′UTR of caspase-2 and used as a positive control. Data shown are representative of two independent experiments giving similar results
    Horseradish Peroxidase Hrp Linked Goat Anti Rabbit Igg Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 77/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase linked bovine anti goat igg antibody
    Constitutive binding of <t>HuR</t> to the 5′UTR of Caspase-2 mRNA in DLD-1 cells. ( a ) An RNP-IP assay was performed in combination with RT-PCR from total cell lysates of DLD-1 cells to amplify mRNA species specifically bound by HuR. HuR-bound mRNA was precipitated by addition of a monoclonal HuR antibody (HuR) or, alternatively, the same amount of mouse <t>IgG</t> (IgG) as negative control. After elution from Sepharose beads, the isolated RNA samples were analyzed by RT-PCR using primer pairs, complementary and specific to the coding region of the indicated genes. The length of corresponding PCR products was determined by a DNA ladder. The specific immunoprecipitation (IP) of HuR is confirmed by western blot analysis (W.blot) shown in the right part of the panel. Data shown are representative of two independent experiments giving similar results. ( b , upper panel) Schematic representation of the different splice variants from human caspase-2 mRNA including caspase-2L (v1), caspase-2S (v2), and variant 3 (v3) encoding transcripts. The relative position of start (gray) and stop (dark) codons is depicted by triangles. Boxes show the relative position of exons and lacking exons are symbolized by a continuous line. The doubleheaded arrows indicate different regions (I, III and IV) encompassing variant-specific sequences (lines) or a region (II) commonly found in all three splice variants (dotted). ( b , lower panel) Crosslinking-RNP-IP analysis demonstrating that HuR specifically interacts with the 5′UTR of caspase-2L (v1) and splice variant 3, respectively. RNA-protein interactions were crosslinked with formaldehyde before HuR-bound mRNA was immunoprecipitated by addition of a HuR-specific antibody (HuR) or, alternatively, by the same amount of mouse IgG (IgG). The precipitated RNA samples were analyzed by RT-PCR by using primer pairs, spanning the indicated regions of caspase-2 mRNA (roman numerals). Input levels of different caspase-2 transcripts were isolated before the IP and were assessed by RT-PCR using the same primer pairs. ( c ) Biotin pull-down assay demonstrating a specific HuR binding to the 5′UTR of caspase-2. For pull-down assay, the biotinylated transcript encompassing 241 nucleotides of the 5′UTR of human caspase-2 (5′UTR Casp-2) was incubated with 300 μ g of total cell lysates from DLD-1 cells. The specific binding of HuR in the pull-down material was confirmed by western blotting. Biotinylated RNA from partial human reverse GAPDH (hrg) was used as a negative control, whereas 0.1 μ g of recombinant HuR (GST-HuR) instead of cell lysates was incubated with the same amount of biotinylated 5′UTR of caspase-2 and used as a positive control. Data shown are representative of two independent experiments giving similar results
    Horseradish Peroxidase Linked Bovine Anti Goat Igg Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase linked secondary goat anti mouse igg
    Identification of a potent small molecule inhibitor of Plk1 PBD A. The chemical structure of T521: 5-(ethylsulfonyl)-2-(4-fluorophenyl)-4-(phenylsulfonyl) oxazole. B, C, D. The inhibitory effect of T521, Poloxin and TQ on the binding of the PBDs of Plk1, 2 and 3 to the FITC-labeled phosphopeptide was analyzed by FP assay. Briefly, T521, Poloxin or TQ was incubated with Plk1-3 PBD for 1 hr at room temperature (RT) prior to addition of FITC-labeled phosphopeptide. The inhibitory effect was calculated as described in the Materials and Methods. Error bars represent SD. E. ELISA-based PBD binding inhibition assay to determine the inhibitory effect of T521 on the interaction between Plk1 PBD and its binding target Map205 PBM . His-tagged PBD of Plk1 and different concentrations of T521 were added into GST-Map205 PBM -coated plates. After incubation, the plate was washed and then probed with mouse anti-His primary antibody, followed by goat anti-mouse <t>IgG-HRP</t> secondary antibody. After washing, the plate was incubated with TMB solution and the OD 450 was measured. Detailed procedure was described in Methods and Materials. DMSO was used as control. F. T521 inhibits Bub1-Plk1 interaction in vivo using Co-immunoprecipitation (IP) assay. HeLa cells synchronized by double-thymidine block were released into medium containing DMSO or T521 at indicated concentrations for 10 hrs, and then lysed and subject to Bub1 IP. The proteins in the precipitates were separated by 10% SDS-PAGE and probed with the anti-hPlk1 and anti-Bub1 antibodies. Moreover, the Bub1 and Plk1 levels were also determined in the lysates of HeLa cells before IP. β-actin served as the loading control.
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    Santa Cruz Biotechnology horseradish peroxidase linked goat anti rabbit igg
    Identification of a potent small molecule inhibitor of Plk1 PBD A. The chemical structure of T521: 5-(ethylsulfonyl)-2-(4-fluorophenyl)-4-(phenylsulfonyl) oxazole. B, C, D. The inhibitory effect of T521, Poloxin and TQ on the binding of the PBDs of Plk1, 2 and 3 to the FITC-labeled phosphopeptide was analyzed by FP assay. Briefly, T521, Poloxin or TQ was incubated with Plk1-3 PBD for 1 hr at room temperature (RT) prior to addition of FITC-labeled phosphopeptide. The inhibitory effect was calculated as described in the Materials and Methods. Error bars represent SD. E. ELISA-based PBD binding inhibition assay to determine the inhibitory effect of T521 on the interaction between Plk1 PBD and its binding target Map205 PBM . His-tagged PBD of Plk1 and different concentrations of T521 were added into GST-Map205 PBM -coated plates. After incubation, the plate was washed and then probed with mouse anti-His primary antibody, followed by goat anti-mouse <t>IgG-HRP</t> secondary antibody. After washing, the plate was incubated with TMB solution and the OD 450 was measured. Detailed procedure was described in Methods and Materials. DMSO was used as control. F. T521 inhibits Bub1-Plk1 interaction in vivo using Co-immunoprecipitation (IP) assay. HeLa cells synchronized by double-thymidine block were released into medium containing DMSO or T521 at indicated concentrations for 10 hrs, and then lysed and subject to Bub1 IP. The proteins in the precipitates were separated by 10% SDS-PAGE and probed with the anti-hPlk1 and anti-Bub1 antibodies. Moreover, the Bub1 and Plk1 levels were also determined in the lysates of HeLa cells before IP. β-actin served as the loading control.
    Horseradish Peroxidase Linked Goat Anti Rabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 84/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology donkey anti goat hrp linked igg
    Quantification of assembled <t>hybrid-IgG/IgA</t> on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with <t>HRP-goat</t> anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.
    Donkey Anti Goat Hrp Linked Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 79/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp linked antibodies
    Quantification of assembled <t>hybrid-IgG/IgA</t> on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with <t>HRP-goat</t> anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.
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    Santa Cruz Biotechnology horseradish peroxidase linked goat anti rat immunoglobulin g igg
    Quantification of assembled <t>hybrid-IgG/IgA</t> on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with <t>HRP-goat</t> anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.
    Horseradish Peroxidase Linked Goat Anti Rat Immunoglobulin G Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology primary antibody horseradish peroxidase linked anti goat p gp igg secondary antibody
    Quantification of assembled <t>hybrid-IgG/IgA</t> on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with <t>HRP-goat</t> anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.
    Primary Antibody Horseradish Peroxidase Linked Anti Goat P Gp Igg Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology hrp linked goat anti rabbit igg
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology secondary horse anti goat igg linked hrp
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology peroxidase linked goat anti mouse igg
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology peroxidase linked secondary antibody goat anti mouse igg hrp
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology hrp conjugated rat anti goat igg
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology hrp horse radish peroxidase linked goat anti rabbit igg
    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV <t>IgG</t> or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse <t>IgG-HRP,</t> as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P
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    Santa Cruz Biotechnology horseradish peroxidase labelled goat anti hamster igg
    Anti- Leishmania <t>IgG</t> and <t>IgG2</t> serum levels in hamsters immunised with L. amazonensis antigens (LaAg) and infected with L. braziliensis . Golden hamsters (5–6 per group) were immunised with IN LaAg (•), IM LaAg (▴) or PBS (□). Two weeks after the last immunisation, hamsters were challenged with L. braziliensis . A) IgG and IgG2 serum levels were determined 114 days post-infection by ELISA. B) Correlation between lesion thickness and anti-leishmanial IgG (r = 0.78, p
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    Santa Cruz Biotechnology hrp conjugated bovine anti goat igg ab
    Expression of CD23 in mouse AECs Cell lysates (50 µg) derived from primary nasal ( A ), tracheal ( B ), and lung ( B ) epithelial cells were electrophoresed on a 12 % SDS-PAGE gel under reducing condition. The separated proteins were transferred onto a nitrocellulose membrane, blotted with rat anti-mouse CD23 mAb (B3B4) followed by <t>HRP-conjugated</t> rabbit anti-rat <t>IgG</t> Ab. Proteins were visualized using the ECL method. Lysates (50 µg) from mouse spleen or CHO cells were used as a positive or negative control, respectively. β-tubulin was used as an internal control. Arrows indicate mouse CD23 and β-tubulin. ( C ) Immunohistochemical staining of mouse lung. Normal mouse lung was prepared in OCT medium and cryosectioned at 5 µm. Frozen tissue sections were fixed and permeabilized with ice-cold acetone and blocked with 10% normal goat serum. A spleen section was used as a positive control. Sections were incubated with rabbit anti-CD23 Ab or normal rabbit IgG, followed by staining with Alexa Fluor 555-conjugated goat anti-rabbit Ab. Nuclei were stained with DAPI. Images were captured using a Zeiss LSM510 confocal microscope. Samples were visualized under consisten contrast and brightness settings.
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    Expression of CD23 in mouse AECs Cell lysates (50 µg) derived from primary nasal ( A ), tracheal ( B ), and lung ( B ) epithelial cells were electrophoresed on a 12 % SDS-PAGE gel under reducing condition. The separated proteins were transferred onto a nitrocellulose membrane, blotted with rat anti-mouse CD23 mAb (B3B4) followed by <t>HRP-conjugated</t> rabbit anti-rat <t>IgG</t> Ab. Proteins were visualized using the ECL method. Lysates (50 µg) from mouse spleen or CHO cells were used as a positive or negative control, respectively. β-tubulin was used as an internal control. Arrows indicate mouse CD23 and β-tubulin. ( C ) Immunohistochemical staining of mouse lung. Normal mouse lung was prepared in OCT medium and cryosectioned at 5 µm. Frozen tissue sections were fixed and permeabilized with ice-cold acetone and blocked with 10% normal goat serum. A spleen section was used as a positive control. Sections were incubated with rabbit anti-CD23 Ab or normal rabbit IgG, followed by staining with Alexa Fluor 555-conjugated goat anti-rabbit Ab. Nuclei were stained with DAPI. Images were captured using a Zeiss LSM510 confocal microscope. Samples were visualized under consisten contrast and brightness settings.
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    Expression of CD23 in mouse AECs Cell lysates (50 µg) derived from primary nasal ( A ), tracheal ( B ), and lung ( B ) epithelial cells were electrophoresed on a 12 % SDS-PAGE gel under reducing condition. The separated proteins were transferred onto a nitrocellulose membrane, blotted with rat anti-mouse CD23 mAb (B3B4) followed by <t>HRP-conjugated</t> rabbit anti-rat <t>IgG</t> Ab. Proteins were visualized using the ECL method. Lysates (50 µg) from mouse spleen or CHO cells were used as a positive or negative control, respectively. β-tubulin was used as an internal control. Arrows indicate mouse CD23 and β-tubulin. ( C ) Immunohistochemical staining of mouse lung. Normal mouse lung was prepared in OCT medium and cryosectioned at 5 µm. Frozen tissue sections were fixed and permeabilized with ice-cold acetone and blocked with 10% normal goat serum. A spleen section was used as a positive control. Sections were incubated with rabbit anti-CD23 Ab or normal rabbit IgG, followed by staining with Alexa Fluor 555-conjugated goat anti-rabbit Ab. Nuclei were stained with DAPI. Images were captured using a Zeiss LSM510 confocal microscope. Samples were visualized under consisten contrast and brightness settings.
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    Specific humoral responses elicited by immunization of mice with microneme proteins. The reactivity of immunoglobulins anti-STAg was determined by ELISA in serum samples collected from both immunized (TgMICs) and control (PBS) mice 15 days after the last antigen injection. Each point/bar represents the average absorbance ± SD of the serum samples from 4 animals. (A) Absorbance provided by the reaction of serum <t>IgG</t> with STAg. (B) Absorbance provided by the reaction of serum <t>IgG1</t> and IgG2a (diluted 1:25) with STAg. The average absorbance ± SD generated by the reaction of serum IgG1 or IgG2a from each group of immunized mice was significantly higher than the corresponding values provided by control mice, with the exception of the TgMIC6-immunized group, whose results were not significantly different of those of the control group. Three independent experiments were performed, and data from one representative experiment is shown. Asterisks represent statistical significant differences (*p
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    Santa Cruz Biotechnology goat anti mouse igg2a hrp secondary antibodies
    Specific humoral responses elicited by immunization of mice with microneme proteins. The reactivity of immunoglobulins anti-STAg was determined by ELISA in serum samples collected from both immunized (TgMICs) and control (PBS) mice 15 days after the last antigen injection. Each point/bar represents the average absorbance ± SD of the serum samples from 4 animals. (A) Absorbance provided by the reaction of serum <t>IgG</t> with STAg. (B) Absorbance provided by the reaction of serum <t>IgG1</t> and IgG2a (diluted 1:25) with STAg. The average absorbance ± SD generated by the reaction of serum IgG1 or IgG2a from each group of immunized mice was significantly higher than the corresponding values provided by control mice, with the exception of the TgMIC6-immunized group, whose results were not significantly different of those of the control group. Three independent experiments were performed, and data from one representative experiment is shown. Asterisks represent statistical significant differences (*p
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    Specific binding ELISA of hE16 to plant-derived DIII. Serial dilutions of hE16 purified from mammalian or plant cells were incubated in sample wells coated with plant-produced WNV DIII and detected with an <t>HRP-conjugated</t> anti-human gamma antibody. A commercial generic human <t>IgG</t> was used as a negative control. Mean ± SD of samples from three independent experiments is presented.
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    Specific binding ELISA of hE16 to plant-derived DIII. Serial dilutions of hE16 purified from mammalian or plant cells were incubated in sample wells coated with plant-produced WNV DIII and detected with an <t>HRP-conjugated</t> anti-human gamma antibody. A commercial generic human <t>IgG</t> was used as a negative control. Mean ± SD of samples from three independent experiments is presented.
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    Santa Cruz Biotechnology peroxidase linked donkey anti goat igg
    Specific binding ELISA of hE16 to plant-derived DIII. Serial dilutions of hE16 purified from mammalian or plant cells were incubated in sample wells coated with plant-produced WNV DIII and detected with an <t>HRP-conjugated</t> anti-human gamma antibody. A commercial generic human <t>IgG</t> was used as a negative control. Mean ± SD of samples from three independent experiments is presented.
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    In vivo immunogenicity of K. pneumoniae EVs. ( a ) K. pneumoniae EV-reactive <t>IgG</t> antibody in serum from mice immunized with 10, 100, 100 ng of K. pneumoniae EVs. This antibody was measured by ELISA ( n =5; * P
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    Santa Cruz Biotechnology horseradish peroxidase hrp conjugated goat against mouse igg
    In vivo immunogenicity of K. pneumoniae EVs. ( a ) K. pneumoniae EV-reactive <t>IgG</t> antibody in serum from mice immunized with 10, 100, 100 ng of K. pneumoniae EVs. This antibody was measured by ELISA ( n =5; * P
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    effect of drug treatment on Hsc70 and protein disulphide isomerase (PDI) expression in small intestinal villi isolated from ECwt-infected mice. A: flow cytometric analysis was performed on intestinal epithelial cells (IEC) isolated from villi from ECwt-infected mice (n = 2 mice for each experimental group) that had been treated with ibuprofen (IBF) (20 mg/kg/day), diclofenac (DCF) (1 mg/kg/day), pioglitazone (PGZ)(30 mg/kg/day), rosiglitazone (RGZ) (4 mg/kg/day), N-acetylcysteine (NAC) (18 mg/kg/day), ascorbic acid (AA) (20 mg/kg/day) or difenoxilate sodium (7.5 mg/kg/day) during three days post-inoculation (d.p.i.). Goat primary antibodies (Abs) against Hsc70 or PDI and fluorescein isothiocyanate (FITC)-conjugated mouse anti-goat <t>IgG</t> secondary Abs were used. Immunofluorescence analysis was performed on a Cyan (Dako) flow cytometer using a FlowJo software; B: radio immunoprecipitation assay lysates from villi isolated from ECwt-infected mice (n = 3 mice for each experimental group) that had been treated with NAC (18 mg/kg/day) during three days after 24 h post-inoculation. were added to ELISA plates coated with rabbit polyclonal Abs against Hsc70 or PDI. Goat Abs against Hsc70 or PDI were used as detection Abs and the reaction was revealed using horseradish peroxidase <t>(HRP)-conjugated</t> donkey anti-goat Abs and phenylenediamine dihydrochloride substrate before reading at optical density (OD) 492 nm . Lysates from uninfected villi were used as a control. Data are expressed as mean OD 492 nm Hsc70 or PDI antigen. Graph shows significant increase of Hsc70 and PDI expression (p
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    effect of drug treatment on Hsc70 and protein disulphide isomerase (PDI) expression in small intestinal villi isolated from ECwt-infected mice. A: flow cytometric analysis was performed on intestinal epithelial cells (IEC) isolated from villi from ECwt-infected mice (n = 2 mice for each experimental group) that had been treated with ibuprofen (IBF) (20 mg/kg/day), diclofenac (DCF) (1 mg/kg/day), pioglitazone (PGZ)(30 mg/kg/day), rosiglitazone (RGZ) (4 mg/kg/day), N-acetylcysteine (NAC) (18 mg/kg/day), ascorbic acid (AA) (20 mg/kg/day) or difenoxilate sodium (7.5 mg/kg/day) during three days post-inoculation (d.p.i.). Goat primary antibodies (Abs) against Hsc70 or PDI and fluorescein isothiocyanate (FITC)-conjugated mouse anti-goat <t>IgG</t> secondary Abs were used. Immunofluorescence analysis was performed on a Cyan (Dako) flow cytometer using a FlowJo software; B: radio immunoprecipitation assay lysates from villi isolated from ECwt-infected mice (n = 3 mice for each experimental group) that had been treated with NAC (18 mg/kg/day) during three days after 24 h post-inoculation. were added to ELISA plates coated with rabbit polyclonal Abs against Hsc70 or PDI. Goat Abs against Hsc70 or PDI were used as detection Abs and the reaction was revealed using horseradish peroxidase <t>(HRP)-conjugated</t> donkey anti-goat Abs and phenylenediamine dihydrochloride substrate before reading at optical density (OD) 492 nm . Lysates from uninfected villi were used as a control. Data are expressed as mean OD 492 nm Hsc70 or PDI antigen. Graph shows significant increase of Hsc70 and PDI expression (p
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    Santa Cruz Biotechnology chicken anti goat igg horseradish peroxidase
    effect of drug treatment on Hsc70 and protein disulphide isomerase (PDI) expression in small intestinal villi isolated from ECwt-infected mice. A: flow cytometric analysis was performed on intestinal epithelial cells (IEC) isolated from villi from ECwt-infected mice (n = 2 mice for each experimental group) that had been treated with ibuprofen (IBF) (20 mg/kg/day), diclofenac (DCF) (1 mg/kg/day), pioglitazone (PGZ)(30 mg/kg/day), rosiglitazone (RGZ) (4 mg/kg/day), N-acetylcysteine (NAC) (18 mg/kg/day), ascorbic acid (AA) (20 mg/kg/day) or difenoxilate sodium (7.5 mg/kg/day) during three days post-inoculation (d.p.i.). Goat primary antibodies (Abs) against Hsc70 or PDI and fluorescein isothiocyanate (FITC)-conjugated mouse anti-goat <t>IgG</t> secondary Abs were used. Immunofluorescence analysis was performed on a Cyan (Dako) flow cytometer using a FlowJo software; B: radio immunoprecipitation assay lysates from villi isolated from ECwt-infected mice (n = 3 mice for each experimental group) that had been treated with NAC (18 mg/kg/day) during three days after 24 h post-inoculation. were added to ELISA plates coated with rabbit polyclonal Abs against Hsc70 or PDI. Goat Abs against Hsc70 or PDI were used as detection Abs and the reaction was revealed using horseradish peroxidase <t>(HRP)-conjugated</t> donkey anti-goat Abs and phenylenediamine dihydrochloride substrate before reading at optical density (OD) 492 nm . Lysates from uninfected villi were used as a control. Data are expressed as mean OD 492 nm Hsc70 or PDI antigen. Graph shows significant increase of Hsc70 and PDI expression (p
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    Constitutive binding of HuR to the 5′UTR of Caspase-2 mRNA in DLD-1 cells. ( a ) An RNP-IP assay was performed in combination with RT-PCR from total cell lysates of DLD-1 cells to amplify mRNA species specifically bound by HuR. HuR-bound mRNA was precipitated by addition of a monoclonal HuR antibody (HuR) or, alternatively, the same amount of mouse IgG (IgG) as negative control. After elution from Sepharose beads, the isolated RNA samples were analyzed by RT-PCR using primer pairs, complementary and specific to the coding region of the indicated genes. The length of corresponding PCR products was determined by a DNA ladder. The specific immunoprecipitation (IP) of HuR is confirmed by western blot analysis (W.blot) shown in the right part of the panel. Data shown are representative of two independent experiments giving similar results. ( b , upper panel) Schematic representation of the different splice variants from human caspase-2 mRNA including caspase-2L (v1), caspase-2S (v2), and variant 3 (v3) encoding transcripts. The relative position of start (gray) and stop (dark) codons is depicted by triangles. Boxes show the relative position of exons and lacking exons are symbolized by a continuous line. The doubleheaded arrows indicate different regions (I, III and IV) encompassing variant-specific sequences (lines) or a region (II) commonly found in all three splice variants (dotted). ( b , lower panel) Crosslinking-RNP-IP analysis demonstrating that HuR specifically interacts with the 5′UTR of caspase-2L (v1) and splice variant 3, respectively. RNA-protein interactions were crosslinked with formaldehyde before HuR-bound mRNA was immunoprecipitated by addition of a HuR-specific antibody (HuR) or, alternatively, by the same amount of mouse IgG (IgG). The precipitated RNA samples were analyzed by RT-PCR by using primer pairs, spanning the indicated regions of caspase-2 mRNA (roman numerals). Input levels of different caspase-2 transcripts were isolated before the IP and were assessed by RT-PCR using the same primer pairs. ( c ) Biotin pull-down assay demonstrating a specific HuR binding to the 5′UTR of caspase-2. For pull-down assay, the biotinylated transcript encompassing 241 nucleotides of the 5′UTR of human caspase-2 (5′UTR Casp-2) was incubated with 300 μ g of total cell lysates from DLD-1 cells. The specific binding of HuR in the pull-down material was confirmed by western blotting. Biotinylated RNA from partial human reverse GAPDH (hrg) was used as a negative control, whereas 0.1 μ g of recombinant HuR (GST-HuR) instead of cell lysates was incubated with the same amount of biotinylated 5′UTR of caspase-2 and used as a positive control. Data shown are representative of two independent experiments giving similar results

    Journal: Cell Death & Disease

    Article Title: Attenuation of the ELAV1-like protein HuR sensitizes adenocarcinoma cells to the intrinsic apoptotic pathway by increasing the translation of caspase-2L

    doi: 10.1038/cddis.2014.279

    Figure Lengend Snippet: Constitutive binding of HuR to the 5′UTR of Caspase-2 mRNA in DLD-1 cells. ( a ) An RNP-IP assay was performed in combination with RT-PCR from total cell lysates of DLD-1 cells to amplify mRNA species specifically bound by HuR. HuR-bound mRNA was precipitated by addition of a monoclonal HuR antibody (HuR) or, alternatively, the same amount of mouse IgG (IgG) as negative control. After elution from Sepharose beads, the isolated RNA samples were analyzed by RT-PCR using primer pairs, complementary and specific to the coding region of the indicated genes. The length of corresponding PCR products was determined by a DNA ladder. The specific immunoprecipitation (IP) of HuR is confirmed by western blot analysis (W.blot) shown in the right part of the panel. Data shown are representative of two independent experiments giving similar results. ( b , upper panel) Schematic representation of the different splice variants from human caspase-2 mRNA including caspase-2L (v1), caspase-2S (v2), and variant 3 (v3) encoding transcripts. The relative position of start (gray) and stop (dark) codons is depicted by triangles. Boxes show the relative position of exons and lacking exons are symbolized by a continuous line. The doubleheaded arrows indicate different regions (I, III and IV) encompassing variant-specific sequences (lines) or a region (II) commonly found in all three splice variants (dotted). ( b , lower panel) Crosslinking-RNP-IP analysis demonstrating that HuR specifically interacts with the 5′UTR of caspase-2L (v1) and splice variant 3, respectively. RNA-protein interactions were crosslinked with formaldehyde before HuR-bound mRNA was immunoprecipitated by addition of a HuR-specific antibody (HuR) or, alternatively, by the same amount of mouse IgG (IgG). The precipitated RNA samples were analyzed by RT-PCR by using primer pairs, spanning the indicated regions of caspase-2 mRNA (roman numerals). Input levels of different caspase-2 transcripts were isolated before the IP and were assessed by RT-PCR using the same primer pairs. ( c ) Biotin pull-down assay demonstrating a specific HuR binding to the 5′UTR of caspase-2. For pull-down assay, the biotinylated transcript encompassing 241 nucleotides of the 5′UTR of human caspase-2 (5′UTR Casp-2) was incubated with 300 μ g of total cell lysates from DLD-1 cells. The specific binding of HuR in the pull-down material was confirmed by western blotting. Biotinylated RNA from partial human reverse GAPDH (hrg) was used as a negative control, whereas 0.1 μ g of recombinant HuR (GST-HuR) instead of cell lysates was incubated with the same amount of biotinylated 5′UTR of caspase-2 and used as a positive control. Data shown are representative of two independent experiments giving similar results

    Article Snippet: Antibodies raised against HuR, anti-rabbit, anti-mouse and anti-goat horseradish peroxidase linked IgG were purchased from Santa Cruz Biotechnology (Heidelberg, Germany).

    Techniques: Binding Assay, Reverse Transcription Polymerase Chain Reaction, Negative Control, Isolation, Polymerase Chain Reaction, Immunoprecipitation, Western Blot, Variant Assay, Pull Down Assay, Incubation, Recombinant, Positive Control

    Identification of a potent small molecule inhibitor of Plk1 PBD A. The chemical structure of T521: 5-(ethylsulfonyl)-2-(4-fluorophenyl)-4-(phenylsulfonyl) oxazole. B, C, D. The inhibitory effect of T521, Poloxin and TQ on the binding of the PBDs of Plk1, 2 and 3 to the FITC-labeled phosphopeptide was analyzed by FP assay. Briefly, T521, Poloxin or TQ was incubated with Plk1-3 PBD for 1 hr at room temperature (RT) prior to addition of FITC-labeled phosphopeptide. The inhibitory effect was calculated as described in the Materials and Methods. Error bars represent SD. E. ELISA-based PBD binding inhibition assay to determine the inhibitory effect of T521 on the interaction between Plk1 PBD and its binding target Map205 PBM . His-tagged PBD of Plk1 and different concentrations of T521 were added into GST-Map205 PBM -coated plates. After incubation, the plate was washed and then probed with mouse anti-His primary antibody, followed by goat anti-mouse IgG-HRP secondary antibody. After washing, the plate was incubated with TMB solution and the OD 450 was measured. Detailed procedure was described in Methods and Materials. DMSO was used as control. F. T521 inhibits Bub1-Plk1 interaction in vivo using Co-immunoprecipitation (IP) assay. HeLa cells synchronized by double-thymidine block were released into medium containing DMSO or T521 at indicated concentrations for 10 hrs, and then lysed and subject to Bub1 IP. The proteins in the precipitates were separated by 10% SDS-PAGE and probed with the anti-hPlk1 and anti-Bub1 antibodies. Moreover, the Bub1 and Plk1 levels were also determined in the lysates of HeLa cells before IP. β-actin served as the loading control.

    Journal: Oncotarget

    Article Title: Identification of a novel Polo-like kinase 1 inhibitor that specifically blocks the functions of Polo-Box domain

    doi: 10.18632/oncotarget.13603

    Figure Lengend Snippet: Identification of a potent small molecule inhibitor of Plk1 PBD A. The chemical structure of T521: 5-(ethylsulfonyl)-2-(4-fluorophenyl)-4-(phenylsulfonyl) oxazole. B, C, D. The inhibitory effect of T521, Poloxin and TQ on the binding of the PBDs of Plk1, 2 and 3 to the FITC-labeled phosphopeptide was analyzed by FP assay. Briefly, T521, Poloxin or TQ was incubated with Plk1-3 PBD for 1 hr at room temperature (RT) prior to addition of FITC-labeled phosphopeptide. The inhibitory effect was calculated as described in the Materials and Methods. Error bars represent SD. E. ELISA-based PBD binding inhibition assay to determine the inhibitory effect of T521 on the interaction between Plk1 PBD and its binding target Map205 PBM . His-tagged PBD of Plk1 and different concentrations of T521 were added into GST-Map205 PBM -coated plates. After incubation, the plate was washed and then probed with mouse anti-His primary antibody, followed by goat anti-mouse IgG-HRP secondary antibody. After washing, the plate was incubated with TMB solution and the OD 450 was measured. Detailed procedure was described in Methods and Materials. DMSO was used as control. F. T521 inhibits Bub1-Plk1 interaction in vivo using Co-immunoprecipitation (IP) assay. HeLa cells synchronized by double-thymidine block were released into medium containing DMSO or T521 at indicated concentrations for 10 hrs, and then lysed and subject to Bub1 IP. The proteins in the precipitates were separated by 10% SDS-PAGE and probed with the anti-hPlk1 and anti-Bub1 antibodies. Moreover, the Bub1 and Plk1 levels were also determined in the lysates of HeLa cells before IP. β-actin served as the loading control.

    Article Snippet: The plate was further probed for 45 min at 37°C with goat anti-mouse IgG-HRP secondary antibody (Cat# sc-2005; Santa Cruz; 1:2000; 100 μL/well).

    Techniques: Binding Assay, Labeling, FP Assay, Incubation, Enzyme-linked Immunosorbent Assay, Inhibition, In Vivo, Immunoprecipitation, Blocking Assay, SDS Page

    Quantification of assembled hybrid-IgG/IgA on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with HRP-goat anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.

    Journal: PLoS ONE

    Article Title: Production of Hybrid-IgG/IgA Plantibodies with Neutralizing Activity against Shiga Toxin 1

    doi: 10.1371/journal.pone.0080712

    Figure Lengend Snippet: Quantification of assembled hybrid-IgG/IgA on sandwich ELISA. A. Hybrid-IgG/IgA in extracts of transgenic A. thaliana leaves, which contained the indicated amounts of total soluble protein (TSP), was captured with immobilized goat anti-mouse κ and then detected with HRP-goat anti-mouse IgA (α chain-specific). The samples were from dimer Tg plants (closed circles) or wild-type plants (closed triangles). B. Standard curve for quantification of IgA. IgA molecules that had been captured by the immobilized goat anti-mouse κ chain were detected with HRP-goat anti-mouse IgA on ELISA. Various concentrations of purified mouse myeloma protein TEPC 15 were used to generate a standard curve. Data are expressed as means ± SD of triplicate determinations. Error bars underneath the symbols are not visible. The results are representative of three experiments.

    Article Snippet: Protein Detection System (Millipore, Billerica, MA, USA) with HRP-goat anti-mouse IgA (α chain-specific) (1∶500 dilution; SouthernBiotech, Birmingham, AL, USA), goat anti-mouse kappa (2 µg/ml; SouthernBiotech) plus HRP-donkey anti-goat IgG (0.4 µg/ml; Santa Cruz Biotechnology, Santa Cruz, CA, USA), or rabbit anti-mouse J chain (1 µg/ml; Santa Cruz Biotechnology) plus HRP-goat anti-rabbit IgG (1∶500 dilution; Zymed, South San Francisco, CA, USA).

    Techniques: Sandwich ELISA, Transgenic Assay, Enzyme-linked Immunosorbent Assay, Purification

    Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV IgG or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse IgG-HRP, as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P

    Journal: Infection and Immunity

    Article Title: Pathogenic Acanthamoeba spp. Secrete a Mannose-Induced Cytolytic Protein That Correlates with the Ability To Cause Disease

    doi: 10.1128/IAI.71.11.6243-6255.2003

    Figure Lengend Snippet: Anti-MIP-133 inhibition of MIP-133 collagenolytic activity and trophozoite migration. (A) ELISA. Ten-microgram samples of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, 15.6 μg of the MIP-133 protein coincubated with a 1:75 dilution of chicken anti-MIP-133 antiserum (ImS), PBS, or 0.1 mg of collagenase (Col) for 72 h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV IgG or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse IgG-HRP, as described in Materials and Methods. Plates were then read at an OD at 405 nm. ***, significantly different from values from MIP-133 treatments ( P

    Article Snippet: Rabbit anti-Chinese hamster IgA hyperimmune serum ( ) was then added to a 1:2 dilution and incubated for 2 h. Plates were washed, and a 1:1,000 dilution of goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology) was added.

    Techniques: Inhibition, Activity Assay, Migration, Enzyme-linked Immunosorbent Assay, Incubation

    Specific binding of the chicken anti-MIP-133 antiserum. (A) Western blotting. Crude supernatants taken from A. castellanii trophozoites grown in mannose were resolved by SDS-PAGE and transferred to PVDF membranes. Membranes were first incubated with chicken anti-MIP-133 antiserum, followed by rabbit anti-chicken IgG-alkaline phosphatase, as described in Materials and Methods. The membranes were then washed and developed with Nitro Blue Tetrazolium-BCIP stock solution. The arrow indicates the 133-kDa band. (B) ELISA. Ninety-six-well plates were coated with 50 μg of MIP-133 and allowed to dry. After drying, wells were blocked and incubated with a 1:50, 1:75, or 1:100 dilution of either the chicken anti-MIP-133 antiserum or preimmune chicken antiserum. Wells were then washed and incubated with goat anti-chicken IgY-HRP. ELISA plates were developed and read at an OD at 405 nm. Bars and error bars represent the means ± SE of results from triplicate experiments. ***, significantly different from values obtained with preimmune serum at the same dilutions ( P

    Journal: Infection and Immunity

    Article Title: Pathogenic Acanthamoeba spp. Secrete a Mannose-Induced Cytolytic Protein That Correlates with the Ability To Cause Disease

    doi: 10.1128/IAI.71.11.6243-6255.2003

    Figure Lengend Snippet: Specific binding of the chicken anti-MIP-133 antiserum. (A) Western blotting. Crude supernatants taken from A. castellanii trophozoites grown in mannose were resolved by SDS-PAGE and transferred to PVDF membranes. Membranes were first incubated with chicken anti-MIP-133 antiserum, followed by rabbit anti-chicken IgG-alkaline phosphatase, as described in Materials and Methods. The membranes were then washed and developed with Nitro Blue Tetrazolium-BCIP stock solution. The arrow indicates the 133-kDa band. (B) ELISA. Ninety-six-well plates were coated with 50 μg of MIP-133 and allowed to dry. After drying, wells were blocked and incubated with a 1:50, 1:75, or 1:100 dilution of either the chicken anti-MIP-133 antiserum or preimmune chicken antiserum. Wells were then washed and incubated with goat anti-chicken IgY-HRP. ELISA plates were developed and read at an OD at 405 nm. Bars and error bars represent the means ± SE of results from triplicate experiments. ***, significantly different from values obtained with preimmune serum at the same dilutions ( P

    Article Snippet: Rabbit anti-Chinese hamster IgA hyperimmune serum ( ) was then added to a 1:2 dilution and incubated for 2 h. Plates were washed, and a 1:1,000 dilution of goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology) was added.

    Techniques: Binding Assay, Western Blot, SDS Page, Incubation, Enzyme-linked Immunosorbent Assay

    Inhibition of MIP-133-mediated CPE by mucosal anti-MIP-133 antibodies from immunized Chinese hamsters. (A) ELISA. Ninety-six-well plates were coated with 50 μg of MIP-133 and allowed to dry in carbonate buffer. After drying, wells were blocked and incubated with a 1:2 dilution of pooled enteric wash from immunized hamsters. Wells were then washed and incubated with a 1:2 dilution of rabbit anti-Chinese hamster IgA hyperimmune serum, washed, and further incubated with a 1:1,000 dilution of goat anti-rabbit IgG-HRP. ELISA plates were developed and read at an OD at 405 nm. (B) Inhibition of CPE. MIP-133 protein samples were adjusted to 1.5, 7.8, and 15.6 μg of protein in 25 μl of PBS before addition to HCE cells in 96-well microtiter plates for 18 h. Protein samples were either used alone or coincubated with a 1:50 dilution of pooled IgA enteric wash from immunized hamsters (ImEW) or of control enteric wash from PBS-immunized animals (CEW). All final volumes were 200 μl. CPE were assessed spectrophotometrically. Each bar and error bar show the mean ± SE of triplicate counts. * and **, significantly different from values for untreated controls ( P

    Journal: Infection and Immunity

    Article Title: Pathogenic Acanthamoeba spp. Secrete a Mannose-Induced Cytolytic Protein That Correlates with the Ability To Cause Disease

    doi: 10.1128/IAI.71.11.6243-6255.2003

    Figure Lengend Snippet: Inhibition of MIP-133-mediated CPE by mucosal anti-MIP-133 antibodies from immunized Chinese hamsters. (A) ELISA. Ninety-six-well plates were coated with 50 μg of MIP-133 and allowed to dry in carbonate buffer. After drying, wells were blocked and incubated with a 1:2 dilution of pooled enteric wash from immunized hamsters. Wells were then washed and incubated with a 1:2 dilution of rabbit anti-Chinese hamster IgA hyperimmune serum, washed, and further incubated with a 1:1,000 dilution of goat anti-rabbit IgG-HRP. ELISA plates were developed and read at an OD at 405 nm. (B) Inhibition of CPE. MIP-133 protein samples were adjusted to 1.5, 7.8, and 15.6 μg of protein in 25 μl of PBS before addition to HCE cells in 96-well microtiter plates for 18 h. Protein samples were either used alone or coincubated with a 1:50 dilution of pooled IgA enteric wash from immunized hamsters (ImEW) or of control enteric wash from PBS-immunized animals (CEW). All final volumes were 200 μl. CPE were assessed spectrophotometrically. Each bar and error bar show the mean ± SE of triplicate counts. * and **, significantly different from values for untreated controls ( P

    Article Snippet: Rabbit anti-Chinese hamster IgA hyperimmune serum ( ) was then added to a 1:2 dilution and incubated for 2 h. Plates were washed, and a 1:1,000 dilution of goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology) was added.

    Techniques: Inhibition, Enzyme-linked Immunosorbent Assay, Incubation

    Collagenolytic activity of the MIP-133 protein. Ten micrograms of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, PBS, or 0.1 mg of collagenase (Col) for 24 (A) and 72 (B) h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV IgG or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse IgG-HRP, as described in Materials and Methods. Plates were developed and read at an OD at 405 nm. Bars and error bars represent the means ± SE of triplicate experiments. *, **, and ***, significantly different from values for PBS-treated controls ( P

    Journal: Infection and Immunity

    Article Title: Pathogenic Acanthamoeba spp. Secrete a Mannose-Induced Cytolytic Protein That Correlates with the Ability To Cause Disease

    doi: 10.1128/IAI.71.11.6243-6255.2003

    Figure Lengend Snippet: Collagenolytic activity of the MIP-133 protein. Ten micrograms of human collagen types I and IV were incubated and dried onto 96-well plates. Wells were treated with either 15.6 μg of the MIP-133 protein, PBS, or 0.1 mg of collagenase (Col) for 24 (A) and 72 (B) h. Sample wells were then washed three times and incubated with mouse anti-collagen type IV IgG or mouse anti-collagen type I IgG as the primary antibody, followed by goat anti-mouse IgG-HRP, as described in Materials and Methods. Plates were developed and read at an OD at 405 nm. Bars and error bars represent the means ± SE of triplicate experiments. *, **, and ***, significantly different from values for PBS-treated controls ( P

    Article Snippet: Rabbit anti-Chinese hamster IgA hyperimmune serum ( ) was then added to a 1:2 dilution and incubated for 2 h. Plates were washed, and a 1:1,000 dilution of goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology) was added.

    Techniques: Activity Assay, Incubation

    Anti- Leishmania IgG and IgG2 serum levels in hamsters immunised with L. amazonensis antigens (LaAg) and infected with L. braziliensis . Golden hamsters (5–6 per group) were immunised with IN LaAg (•), IM LaAg (▴) or PBS (□). Two weeks after the last immunisation, hamsters were challenged with L. braziliensis . A) IgG and IgG2 serum levels were determined 114 days post-infection by ELISA. B) Correlation between lesion thickness and anti-leishmanial IgG (r = 0.78, p

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Intranasal Vaccination with Leishmanial Antigens Protects Golden Hamsters (Mesocricetus auratus) Against Leishmania (Viannia) braziliensis Infection

    doi: 10.1371/journal.pntd.0003439

    Figure Lengend Snippet: Anti- Leishmania IgG and IgG2 serum levels in hamsters immunised with L. amazonensis antigens (LaAg) and infected with L. braziliensis . Golden hamsters (5–6 per group) were immunised with IN LaAg (•), IM LaAg (▴) or PBS (□). Two weeks after the last immunisation, hamsters were challenged with L. braziliensis . A) IgG and IgG2 serum levels were determined 114 days post-infection by ELISA. B) Correlation between lesion thickness and anti-leishmanial IgG (r = 0.78, p

    Article Snippet: Plasma samples were diluted 1∶5000 for IgG and 1∶200 for IgG2 and detected by horseradish peroxidase-labelled goat anti-hamster IgG (Santa Cruz Biotechnology, Santa Cruz, California, USA) and biotin–conjugated mouse anti-Syrian hamster IgG2 (Becton Dickinson, New Jersey, USA).

    Techniques: Infection, Enzyme-linked Immunosorbent Assay

    Expression of CD23 in mouse AECs Cell lysates (50 µg) derived from primary nasal ( A ), tracheal ( B ), and lung ( B ) epithelial cells were electrophoresed on a 12 % SDS-PAGE gel under reducing condition. The separated proteins were transferred onto a nitrocellulose membrane, blotted with rat anti-mouse CD23 mAb (B3B4) followed by HRP-conjugated rabbit anti-rat IgG Ab. Proteins were visualized using the ECL method. Lysates (50 µg) from mouse spleen or CHO cells were used as a positive or negative control, respectively. β-tubulin was used as an internal control. Arrows indicate mouse CD23 and β-tubulin. ( C ) Immunohistochemical staining of mouse lung. Normal mouse lung was prepared in OCT medium and cryosectioned at 5 µm. Frozen tissue sections were fixed and permeabilized with ice-cold acetone and blocked with 10% normal goat serum. A spleen section was used as a positive control. Sections were incubated with rabbit anti-CD23 Ab or normal rabbit IgG, followed by staining with Alexa Fluor 555-conjugated goat anti-rabbit Ab. Nuclei were stained with DAPI. Images were captured using a Zeiss LSM510 confocal microscope. Samples were visualized under consisten contrast and brightness settings.

    Journal: Mucosal immunology

    Article Title: Inhibition of CD23-mediated IgE transcytosis suppresses the initiation and development of allergic airway inflammation

    doi: 10.1038/mi.2015.16

    Figure Lengend Snippet: Expression of CD23 in mouse AECs Cell lysates (50 µg) derived from primary nasal ( A ), tracheal ( B ), and lung ( B ) epithelial cells were electrophoresed on a 12 % SDS-PAGE gel under reducing condition. The separated proteins were transferred onto a nitrocellulose membrane, blotted with rat anti-mouse CD23 mAb (B3B4) followed by HRP-conjugated rabbit anti-rat IgG Ab. Proteins were visualized using the ECL method. Lysates (50 µg) from mouse spleen or CHO cells were used as a positive or negative control, respectively. β-tubulin was used as an internal control. Arrows indicate mouse CD23 and β-tubulin. ( C ) Immunohistochemical staining of mouse lung. Normal mouse lung was prepared in OCT medium and cryosectioned at 5 µm. Frozen tissue sections were fixed and permeabilized with ice-cold acetone and blocked with 10% normal goat serum. A spleen section was used as a positive control. Sections were incubated with rabbit anti-CD23 Ab or normal rabbit IgG, followed by staining with Alexa Fluor 555-conjugated goat anti-rabbit Ab. Nuclei were stained with DAPI. Images were captured using a Zeiss LSM510 confocal microscope. Samples were visualized under consisten contrast and brightness settings.

    Article Snippet: HRP-conjugated bovine anti-goat IgG Ab was from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Expressing, Derivative Assay, SDS Page, Negative Control, Immunohistochemistry, Staining, Positive Control, Incubation, Microscopy

    Epithelial CD23 facilitates airway inflammation after OVA sensitization and challenge in chimeric mice A. Mice were sensitized (i.p.) with OVA or left untreated. Lung and trachea epithelial cells were isolated and cell lysates (50 µg) were subjected to 12 % SDS-PAGE gel electrophoresis under reducing conditions. Proteins were transferred onto nitrocellulose membranes and blotted with rat-anti mouse CD23 mAb (B3B4) followed by HRP-conjugated rabbit anti-rat IgG Ab. Proteins were visualized using ECL. Arrows indicate mouse CD23 and β-tubulin. B–D. WT/WT, CD23KO/WT, WT/CD23KO chimeric mice were i.p. sensitized with 100 µg OVA plus 4 mg alum at day 0 and subsequently injected (i.p.) with 100 µg OVA on day 7 and 14. Mice were challenged on day 21 with nebulized 1 % OVA for 30 min. 5 h after OVA challenge, sera were collected and OVA quantitated by ELISA (B). 24 h after OVA challenge, BAL fluid and sera were collected and OVA-specific IgE (C) and IL-4 (D) concentrations assessed by ELISA. *P

    Journal: Mucosal immunology

    Article Title: Inhibition of CD23-mediated IgE transcytosis suppresses the initiation and development of allergic airway inflammation

    doi: 10.1038/mi.2015.16

    Figure Lengend Snippet: Epithelial CD23 facilitates airway inflammation after OVA sensitization and challenge in chimeric mice A. Mice were sensitized (i.p.) with OVA or left untreated. Lung and trachea epithelial cells were isolated and cell lysates (50 µg) were subjected to 12 % SDS-PAGE gel electrophoresis under reducing conditions. Proteins were transferred onto nitrocellulose membranes and blotted with rat-anti mouse CD23 mAb (B3B4) followed by HRP-conjugated rabbit anti-rat IgG Ab. Proteins were visualized using ECL. Arrows indicate mouse CD23 and β-tubulin. B–D. WT/WT, CD23KO/WT, WT/CD23KO chimeric mice were i.p. sensitized with 100 µg OVA plus 4 mg alum at day 0 and subsequently injected (i.p.) with 100 µg OVA on day 7 and 14. Mice were challenged on day 21 with nebulized 1 % OVA for 30 min. 5 h after OVA challenge, sera were collected and OVA quantitated by ELISA (B). 24 h after OVA challenge, BAL fluid and sera were collected and OVA-specific IgE (C) and IL-4 (D) concentrations assessed by ELISA. *P

    Article Snippet: HRP-conjugated bovine anti-goat IgG Ab was from Santa Cruz Biotechnology (Santa Cruz, CA).

    Techniques: Mouse Assay, Isolation, SDS Page, Nucleic Acid Electrophoresis, Injection, Enzyme-linked Immunosorbent Assay

    Specific humoral responses elicited by immunization of mice with microneme proteins. The reactivity of immunoglobulins anti-STAg was determined by ELISA in serum samples collected from both immunized (TgMICs) and control (PBS) mice 15 days after the last antigen injection. Each point/bar represents the average absorbance ± SD of the serum samples from 4 animals. (A) Absorbance provided by the reaction of serum IgG with STAg. (B) Absorbance provided by the reaction of serum IgG1 and IgG2a (diluted 1:25) with STAg. The average absorbance ± SD generated by the reaction of serum IgG1 or IgG2a from each group of immunized mice was significantly higher than the corresponding values provided by control mice, with the exception of the TgMIC6-immunized group, whose results were not significantly different of those of the control group. Three independent experiments were performed, and data from one representative experiment is shown. Asterisks represent statistical significant differences (*p

    Journal: PLoS ONE

    Article Title: Vaccination with Recombinant Microneme Proteins Confers Protection against Experimental Toxoplasmosis in Mice

    doi: 10.1371/journal.pone.0143087

    Figure Lengend Snippet: Specific humoral responses elicited by immunization of mice with microneme proteins. The reactivity of immunoglobulins anti-STAg was determined by ELISA in serum samples collected from both immunized (TgMICs) and control (PBS) mice 15 days after the last antigen injection. Each point/bar represents the average absorbance ± SD of the serum samples from 4 animals. (A) Absorbance provided by the reaction of serum IgG with STAg. (B) Absorbance provided by the reaction of serum IgG1 and IgG2a (diluted 1:25) with STAg. The average absorbance ± SD generated by the reaction of serum IgG1 or IgG2a from each group of immunized mice was significantly higher than the corresponding values provided by control mice, with the exception of the TgMIC6-immunized group, whose results were not significantly different of those of the control group. Three independent experiments were performed, and data from one representative experiment is shown. Asterisks represent statistical significant differences (*p

    Article Snippet: Plates were then incubated at 37°C for 1 h, washed four times, and incubated with horseradish-peroxidase-conjugated goat anti-mouse IgG, IgG1, or IgG2b (Santa Cruz Biotechnology), at 1:5000 dilution in blocking buffer, for 1 h, at 37°C.

    Techniques: Mouse Assay, Enzyme-linked Immunosorbent Assay, Injection, Generated

    SDS-PAGE and western blot analysis of native and recombinant microneme proteins. SDS-PAGE of recombinant proteins (panels A, B, and C, Coomassie Blue stained) or native (panel D, silver-stained) proteins. Heterologous expression was noted in E . coli (DE3) and recombinant proteins were detected in inclusion bodies. Lane 1: protein expression before induction. Lane 2: protein expression after induction. Lane 3: purified and refolded histidine-tagged recombinant proteins, displayed apparent molecular masses of 70-kDa (TgMIC1, panel A), 80-kDa (TgMIC4, panel B), and 30-kDa (TgMIC6, panel C). Panel E shows the electrophoretical profile of the Lac+ fraction, composed of the native proteins TgMIC1 (53-kDa) and TgMIC4 (68-kDa). Lane M: Molecular mass markers. Reactivity of recombinant and native microneme proteins with anti-Lac+ mouse serum was examined by western blot (Panel E), developed with peroxidase-conjugated goat anti-mouse IgG.

    Journal: PLoS ONE

    Article Title: Vaccination with Recombinant Microneme Proteins Confers Protection against Experimental Toxoplasmosis in Mice

    doi: 10.1371/journal.pone.0143087

    Figure Lengend Snippet: SDS-PAGE and western blot analysis of native and recombinant microneme proteins. SDS-PAGE of recombinant proteins (panels A, B, and C, Coomassie Blue stained) or native (panel D, silver-stained) proteins. Heterologous expression was noted in E . coli (DE3) and recombinant proteins were detected in inclusion bodies. Lane 1: protein expression before induction. Lane 2: protein expression after induction. Lane 3: purified and refolded histidine-tagged recombinant proteins, displayed apparent molecular masses of 70-kDa (TgMIC1, panel A), 80-kDa (TgMIC4, panel B), and 30-kDa (TgMIC6, panel C). Panel E shows the electrophoretical profile of the Lac+ fraction, composed of the native proteins TgMIC1 (53-kDa) and TgMIC4 (68-kDa). Lane M: Molecular mass markers. Reactivity of recombinant and native microneme proteins with anti-Lac+ mouse serum was examined by western blot (Panel E), developed with peroxidase-conjugated goat anti-mouse IgG.

    Article Snippet: Plates were then incubated at 37°C for 1 h, washed four times, and incubated with horseradish-peroxidase-conjugated goat anti-mouse IgG, IgG1, or IgG2b (Santa Cruz Biotechnology), at 1:5000 dilution in blocking buffer, for 1 h, at 37°C.

    Techniques: SDS Page, Western Blot, Recombinant, Staining, Expressing, Purification

    Experimental Protocol. (A) In the first experimental procedure mice were subcutaneously (s.c.) vaccinated with microneme proteins emulsified in Freund’s complete adjuvant. Mice were boosted at the same dose and regimen on day 15 and 30 after first injection, now emulsified in Freund’s incomplete adjuvant. Fifteen days after the last injection, blood and spleen samples were collected to assess serum IgG, in vitro T cell proliferation, and cytokine concentrations. (B) One month after the last immunization procedure, the mice were orally infected with 80 cysts of the ME49 strain and the mortality was monitored daily for 1 month. To evaluate the tissue cyst burden, the brain of the mice infected with 40 cysts was removed 1 month after the challenge and the mean number of cysts per brain was determined. Additionally, blood samples from mice challenged with 40 cysts were collected 30 days after T . gondii challenge and the serum cytokine levels were analyzed.

    Journal: PLoS ONE

    Article Title: Vaccination with Recombinant Microneme Proteins Confers Protection against Experimental Toxoplasmosis in Mice

    doi: 10.1371/journal.pone.0143087

    Figure Lengend Snippet: Experimental Protocol. (A) In the first experimental procedure mice were subcutaneously (s.c.) vaccinated with microneme proteins emulsified in Freund’s complete adjuvant. Mice were boosted at the same dose and regimen on day 15 and 30 after first injection, now emulsified in Freund’s incomplete adjuvant. Fifteen days after the last injection, blood and spleen samples were collected to assess serum IgG, in vitro T cell proliferation, and cytokine concentrations. (B) One month after the last immunization procedure, the mice were orally infected with 80 cysts of the ME49 strain and the mortality was monitored daily for 1 month. To evaluate the tissue cyst burden, the brain of the mice infected with 40 cysts was removed 1 month after the challenge and the mean number of cysts per brain was determined. Additionally, blood samples from mice challenged with 40 cysts were collected 30 days after T . gondii challenge and the serum cytokine levels were analyzed.

    Article Snippet: Plates were then incubated at 37°C for 1 h, washed four times, and incubated with horseradish-peroxidase-conjugated goat anti-mouse IgG, IgG1, or IgG2b (Santa Cruz Biotechnology), at 1:5000 dilution in blocking buffer, for 1 h, at 37°C.

    Techniques: Mouse Assay, Injection, In Vitro, Infection

    Specific binding ELISA of hE16 to plant-derived DIII. Serial dilutions of hE16 purified from mammalian or plant cells were incubated in sample wells coated with plant-produced WNV DIII and detected with an HRP-conjugated anti-human gamma antibody. A commercial generic human IgG was used as a negative control. Mean ± SD of samples from three independent experiments is presented.

    Journal: BioMed Research International

    Article Title: A Plant-Produced Antigen Elicits Potent Immune Responses against West Nile Virus in Mice

    doi: 10.1155/2014/952865

    Figure Lengend Snippet: Specific binding ELISA of hE16 to plant-derived DIII. Serial dilutions of hE16 purified from mammalian or plant cells were incubated in sample wells coated with plant-produced WNV DIII and detected with an HRP-conjugated anti-human gamma antibody. A commercial generic human IgG was used as a negative control. Mean ± SD of samples from three independent experiments is presented.

    Article Snippet: After washing with PBST, the plates were incubated with an HRP-conjugated goat anti-mouse IgG1 (Santa Cruz Biotech) or anti-mouse IgG2a (Southern Biotech).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Derivative Assay, Purification, Incubation, Produced, Negative Control

    In vivo immunogenicity of K. pneumoniae EVs. ( a ) K. pneumoniae EV-reactive IgG antibody in serum from mice immunized with 10, 100, 100 ng of K. pneumoniae EVs. This antibody was measured by ELISA ( n =5; * P

    Journal: Experimental & Molecular Medicine

    Article Title: Vaccination with Klebsiella pneumoniae-derived extracellular vesicles protects against bacteria-induced lethality via both humoral and cellular immunity

    doi: 10.1038/emm.2015.59

    Figure Lengend Snippet: In vivo immunogenicity of K. pneumoniae EVs. ( a ) K. pneumoniae EV-reactive IgG antibody in serum from mice immunized with 10, 100, 100 ng of K. pneumoniae EVs. This antibody was measured by ELISA ( n =5; * P

    Article Snippet: The serum was diluted with the reagent diluent (1:500) and was then incubated in the EV-coated plate for 2 h. After incubation, the plates were washed and treated with 200 ng ml−1 of horseradish peroxidase-conjugated goat anti-mouse immunoglobulin G (IgG) antibody (Santa Cruz Biotechnology, CA, USA) for 2 h. After washing the plates, the enhanced chemiluminescence substrate (Thermo Scientific, Kenilworth, NJ, USA) was added and analyzed using a Victor Wallac 1420 apparatus (PerkinElmer, Waltham, MA, USA).

    Techniques: In Vivo, Mouse Assay, Enzyme-linked Immunosorbent Assay

    effect of drug treatment on Hsc70 and protein disulphide isomerase (PDI) expression in small intestinal villi isolated from ECwt-infected mice. A: flow cytometric analysis was performed on intestinal epithelial cells (IEC) isolated from villi from ECwt-infected mice (n = 2 mice for each experimental group) that had been treated with ibuprofen (IBF) (20 mg/kg/day), diclofenac (DCF) (1 mg/kg/day), pioglitazone (PGZ)(30 mg/kg/day), rosiglitazone (RGZ) (4 mg/kg/day), N-acetylcysteine (NAC) (18 mg/kg/day), ascorbic acid (AA) (20 mg/kg/day) or difenoxilate sodium (7.5 mg/kg/day) during three days post-inoculation (d.p.i.). Goat primary antibodies (Abs) against Hsc70 or PDI and fluorescein isothiocyanate (FITC)-conjugated mouse anti-goat IgG secondary Abs were used. Immunofluorescence analysis was performed on a Cyan (Dako) flow cytometer using a FlowJo software; B: radio immunoprecipitation assay lysates from villi isolated from ECwt-infected mice (n = 3 mice for each experimental group) that had been treated with NAC (18 mg/kg/day) during three days after 24 h post-inoculation. were added to ELISA plates coated with rabbit polyclonal Abs against Hsc70 or PDI. Goat Abs against Hsc70 or PDI were used as detection Abs and the reaction was revealed using horseradish peroxidase (HRP)-conjugated donkey anti-goat Abs and phenylenediamine dihydrochloride substrate before reading at optical density (OD) 492 nm . Lysates from uninfected villi were used as a control. Data are expressed as mean OD 492 nm Hsc70 or PDI antigen. Graph shows significant increase of Hsc70 and PDI expression (p

    Journal: Memórias do Instituto Oswaldo Cruz

    Article Title: Inhibition of rotavirus ECwt infection in ICR suckling mice by N-acetylcysteine, peroxisome proliferator-activated receptor gamma agonists and cyclooxygenase-2 inhibitors

    doi: 10.1590/0074-0276108062013011

    Figure Lengend Snippet: effect of drug treatment on Hsc70 and protein disulphide isomerase (PDI) expression in small intestinal villi isolated from ECwt-infected mice. A: flow cytometric analysis was performed on intestinal epithelial cells (IEC) isolated from villi from ECwt-infected mice (n = 2 mice for each experimental group) that had been treated with ibuprofen (IBF) (20 mg/kg/day), diclofenac (DCF) (1 mg/kg/day), pioglitazone (PGZ)(30 mg/kg/day), rosiglitazone (RGZ) (4 mg/kg/day), N-acetylcysteine (NAC) (18 mg/kg/day), ascorbic acid (AA) (20 mg/kg/day) or difenoxilate sodium (7.5 mg/kg/day) during three days post-inoculation (d.p.i.). Goat primary antibodies (Abs) against Hsc70 or PDI and fluorescein isothiocyanate (FITC)-conjugated mouse anti-goat IgG secondary Abs were used. Immunofluorescence analysis was performed on a Cyan (Dako) flow cytometer using a FlowJo software; B: radio immunoprecipitation assay lysates from villi isolated from ECwt-infected mice (n = 3 mice for each experimental group) that had been treated with NAC (18 mg/kg/day) during three days after 24 h post-inoculation. were added to ELISA plates coated with rabbit polyclonal Abs against Hsc70 or PDI. Goat Abs against Hsc70 or PDI were used as detection Abs and the reaction was revealed using horseradish peroxidase (HRP)-conjugated donkey anti-goat Abs and phenylenediamine dihydrochloride substrate before reading at optical density (OD) 492 nm . Lysates from uninfected villi were used as a control. Data are expressed as mean OD 492 nm Hsc70 or PDI antigen. Graph shows significant increase of Hsc70 and PDI expression (p

    Article Snippet: HRP-conjugated donkey anti-goat IgG Ab (0.4 µg/mL; SC-2020, Santa Cruz Biotechnology Inc) was used as a secondary Ab and the reaction was developed with intensified luminescence (Pierce) or AEC.

    Techniques: Expressing, Isolation, Infection, Mouse Assay, Flow Cytometry, Immunofluorescence, Cytometry, Software, Radio Immunoprecipitation, Enzyme-linked Immunosorbent Assay