horseradish peroxidase linked anti goat igg Santa Cruz Biotechnology Search Results


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  • 89
    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
    Hrp Linked Goat Anti Rabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 896 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology hrp 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
    Hrp Linked Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 709 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase linked 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
    Horseradish Peroxidase Linked Anti Goat Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish 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
    Horseradish Peroxidase Linked Goat Anti Rabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 49 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
    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
    Horseradish Peroxidase Hrp Linked Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology 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
    Peroxidase Linked Goat Anti Rabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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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
    Peroxidase Linked Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology donkey anti goat igg hrp linked 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.
    Donkey Anti Goat Igg Hrp Linked Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 16 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
    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 conjugated goat anti mouse igg
    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
    Horseradish Peroxidase Conjugated Goat Anti Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 386 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology peroxidase linked 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
    Peroxidase Linked Secondary Antibodies, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology hrp conjugated goat anti mouse igg1
    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.
    Hrp Conjugated Goat Anti Mouse Igg1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology hrp
    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 horseradish 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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    Santa Cruz Biotechnology horseradish peroxidase hrp conjugated goat against mouse 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.
    Horseradish Peroxidase Hrp Conjugated Goat Against Mouse Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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

    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

    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