goat anti rabbit  (Bio-Rad)

 
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    Name:
    Goat anti Rabbit IgG Fc
    Description:

    Catalog Number:
    5213-2504
    Price:
    None
    Applications:
    Immunohistology, ELISA, Western Blotting
    Format:
    HRP, Biotin, FITC, HRP, Purified
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    Structured Review

    Bio-Rad goat anti rabbit

    https://www.bioz.com/result/goat anti rabbit/product/Bio-Rad
    Average 99 stars, based on 193 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit - by Bioz Stars, 2021-01
    99/100 stars

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    Incubation:

    Article Title: Xin Fu Kang oral liquid inhibits excessive myocardial mitophagy in a rat model of advanced heart failure
    Article Snippet: .. After washing and incubation with a goat-anti-rabbit secondary antibody conjugated to horseradish peroxidase (HRP) at a ratio of 1:10000, protein bands were detected by Bio-Rad Chemi-DocXRS (Bio-Rad Laboratories, California, US). .. Data analysis was performed using GraphPad Prism 5.0 software.

    Article Title: Pharmacological treatment with galectin-1 protects against renal ischaemia-reperfusion injury
    Article Snippet: .. After washing, the cells were incubated with a goat anti-rabbit Ab conjugated with FITC (Serotec, Oxford, UK; 1:100 in normal goat serum 1.5%) for 1 h. The slides were mounted with a solution containing glycerol and PBS (1:1). .. Negative control samples were incubated only with normal goat serum without primary Ab.

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  • 99
    Bio-Rad goat anti rabbit immunoglobulin g horseradish peroxidase
    Western blot analysis of σ A  in growing and developing  M. xanthus  cells. DK1622 cells were collected at 0, 9, 12, 15, 18, and 24 h after the onset of development (lanes 1 to 6), resuspended in sample buffer, and boiled for 5 min. Equal amounts of  M. xanthus  protein, as judged by measuring total protein in sonic lysates of the same samples, were separated by SDS-10% PAGE and electrotransferred to a nitrocellulose filter, which was incubated with a polyclonal antiserum to  B. subtilis  σ 43  and visualized with goat anti-rabbit immunoglobulin G-horseradish peroxidase. The σ A  is indicated by an arrow, and protein standards are marked in kilodaltons.
    Goat Anti Rabbit Immunoglobulin G Horseradish Peroxidase, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit immunoglobulin g horseradish peroxidase/product/Bio-Rad
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit immunoglobulin g horseradish peroxidase - by Bioz Stars, 2021-01
    99/100 stars
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    90
    Bio-Rad peroxidase conjugated goat anti rabbit igg
    Localization of <t>ΔCT–P-selectin</t> in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit <t>IgG</t> conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.
    Peroxidase Conjugated Goat Anti Rabbit Igg, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxidase conjugated goat anti rabbit igg/product/Bio-Rad
    Average 90 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    peroxidase conjugated goat anti rabbit igg - by Bioz Stars, 2021-01
    90/100 stars
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    88
    Bio-Rad goat anti rabbit igg conjugated to horse radish peroxidase
    ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from <t>Mmp-8</t> −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 <t>IgG,</t> or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P
    Goat Anti Rabbit Igg Conjugated To Horse Radish Peroxidase, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg conjugated to horse radish peroxidase/product/Bio-Rad
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    91
    Bio-Rad horseradish peroxidase conjugated goat anti rabbit immunoglobulin g
    Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody <t>(IgG)</t> response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P
    Horseradish Peroxidase Conjugated Goat Anti Rabbit Immunoglobulin G, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated goat anti rabbit immunoglobulin g/product/Bio-Rad
    Average 91 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated goat anti rabbit immunoglobulin g - by Bioz Stars, 2021-01
    91/100 stars
      Buy from Supplier

    Image Search Results


    Western blot analysis of σ A  in growing and developing  M. xanthus  cells. DK1622 cells were collected at 0, 9, 12, 15, 18, and 24 h after the onset of development (lanes 1 to 6), resuspended in sample buffer, and boiled for 5 min. Equal amounts of  M. xanthus  protein, as judged by measuring total protein in sonic lysates of the same samples, were separated by SDS-10% PAGE and electrotransferred to a nitrocellulose filter, which was incubated with a polyclonal antiserum to  B. subtilis  σ 43  and visualized with goat anti-rabbit immunoglobulin G-horseradish peroxidase. The σ A  is indicated by an arrow, and protein standards are marked in kilodaltons.

    Journal: Journal of Bacteriology

    Article Title: Identification of the ?4514 Regulatory Region, a Developmental Promoter of Myxococcus xanthus That Is Transcribed In Vitro by the Major Vegetative RNA Polymerase

    doi: 10.1128/JB.184.12.3348-3359.2002

    Figure Lengend Snippet: Western blot analysis of σ A in growing and developing M. xanthus cells. DK1622 cells were collected at 0, 9, 12, 15, 18, and 24 h after the onset of development (lanes 1 to 6), resuspended in sample buffer, and boiled for 5 min. Equal amounts of M. xanthus protein, as judged by measuring total protein in sonic lysates of the same samples, were separated by SDS-10% PAGE and electrotransferred to a nitrocellulose filter, which was incubated with a polyclonal antiserum to B. subtilis σ 43 and visualized with goat anti-rabbit immunoglobulin G-horseradish peroxidase. The σ A is indicated by an arrow, and protein standards are marked in kilodaltons.

    Article Snippet: Immunodetection with goat anti-rabbit immunoglobulin G-horseradish peroxidase (Bio-Rad) and chemiluminescence (ECL; Amersham Pharmacia Biotech) was performed according to the manufacturer's instructions.

    Techniques: Western Blot, Polyacrylamide Gel Electrophoresis, Incubation

    Localization of ΔCT–P-selectin in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit IgG conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.

    Journal: The Journal of Cell Biology

    Article Title: Role of P-Selectin Cytoplasmic Domain in Granular Targeting In Vivo and in Early Inflammatory Responses

    doi:

    Figure Lengend Snippet: Localization of ΔCT–P-selectin in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit IgG conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.

    Article Snippet: The antibody bound to P-selectin was detected with a horseradish peroxidase-conjugated goat anti–rabbit IgG (Bio-Rad, Hercules, CA) and an enhanced chemiluminescence kit ( Sigma Chemical Co. , St. Louis, MO).

    Techniques: Electron Microscopy, Labeling, Mouse Assay, Staining

    Flow cytometry analysis of P-selectin expression on platelets. Wild-type and ΔCT platelets were stained for membrane P-selectin and analyzed by flow cytometry. In the resting state, platelets of both genotypes displayed virtually no P-selectin on their plasma membranes. Thrombin activation induced in wild-type as well as in mutant platelets a similar increase in mean fluorescence with ∼90% of P-selectin–positive platelets. Representative histograms are shown. Shaded area , negative control staining with only the FITC-conjugated goat anti–rabbit IgG.

    Journal: The Journal of Cell Biology

    Article Title: Role of P-Selectin Cytoplasmic Domain in Granular Targeting In Vivo and in Early Inflammatory Responses

    doi:

    Figure Lengend Snippet: Flow cytometry analysis of P-selectin expression on platelets. Wild-type and ΔCT platelets were stained for membrane P-selectin and analyzed by flow cytometry. In the resting state, platelets of both genotypes displayed virtually no P-selectin on their plasma membranes. Thrombin activation induced in wild-type as well as in mutant platelets a similar increase in mean fluorescence with ∼90% of P-selectin–positive platelets. Representative histograms are shown. Shaded area , negative control staining with only the FITC-conjugated goat anti–rabbit IgG.

    Article Snippet: The antibody bound to P-selectin was detected with a horseradish peroxidase-conjugated goat anti–rabbit IgG (Bio-Rad, Hercules, CA) and an enhanced chemiluminescence kit ( Sigma Chemical Co. , St. Louis, MO).

    Techniques: Flow Cytometry, Cytometry, Expressing, Staining, Activation Assay, Mutagenesis, Fluorescence, Negative Control

    ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from Mmp-8 −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from Mmp-8 −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Binding Assay, Mouse Assay, Expressing, Incubation, Software, Two Tailed Test

    TIMP-1 is co-localized with MMP-8 and MMP-9 on the surface of activated human PMNs: Human PMNs were activated at 37°C with PAF at 10 −7 M for 15 min followed by fMLP at 10 −7 M for 30 min. Cells were double immunostained with Alexa 546 and murine anti-MMP-9 IgG ( A , second panel), or murine anti-human MMP-8 IgG ( B , second panel) or non-immune murine (Ms) IgG ( C , second panel) and with Alexa 488 and rabbit anti-TIMP-1 IgG ( A and B third panels) or non-immune rabbit (Rb) IgG ( C , third panel). The anti-MMP-8 and anti-MMP-9 IgGs used recognize both pro and active forms of these MMPs. Cells were examined using a Normarski objective ( A-C , left panels) and co-localization of MMPs and TIMP-1 on the surface of the activated PMNs was assessed by confocal microscopy (see merged images in the right panels for A-C ). The white bars are 5 microns in length. Note the strong co-localization of TIMP-1 with both MMP-8 and MMP-9 on the surface of activated PMNs. The results shown are representative of at least 3 different PMN preparations.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: TIMP-1 is co-localized with MMP-8 and MMP-9 on the surface of activated human PMNs: Human PMNs were activated at 37°C with PAF at 10 −7 M for 15 min followed by fMLP at 10 −7 M for 30 min. Cells were double immunostained with Alexa 546 and murine anti-MMP-9 IgG ( A , second panel), or murine anti-human MMP-8 IgG ( B , second panel) or non-immune murine (Ms) IgG ( C , second panel) and with Alexa 488 and rabbit anti-TIMP-1 IgG ( A and B third panels) or non-immune rabbit (Rb) IgG ( C , third panel). The anti-MMP-8 and anti-MMP-9 IgGs used recognize both pro and active forms of these MMPs. Cells were examined using a Normarski objective ( A-C , left panels) and co-localization of MMPs and TIMP-1 on the surface of the activated PMNs was assessed by confocal microscopy (see merged images in the right panels for A-C ). The white bars are 5 microns in length. Note the strong co-localization of TIMP-1 with both MMP-8 and MMP-9 on the surface of activated PMNs. The results shown are representative of at least 3 different PMN preparations.

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Confocal Microscopy

    Exogenous Timp-1 reconstitutes the binding of exogenous proMmp-9 and proMmp-8 to Timp-1 −/− PMNs: In A , PAF- and fMLP-activated PMNs from Mmp-9 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-9, and then immunostained with rabbit anti-Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488. In B , PAF- and fMLP-activated PMNs from Mmp-8 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-8, and then immunostained with rabbit anti-Mmp-8 IgG, or non-immune rabbit IgG followed by goat- anti-rabbit F(ab) 2 -conjugated to Alexa 488. In A-B , the antibodies used detect both the pro and active forms of the Mmps. Data are mean + SEM; n = 150–200 cells per group. Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: Exogenous Timp-1 reconstitutes the binding of exogenous proMmp-9 and proMmp-8 to Timp-1 −/− PMNs: In A , PAF- and fMLP-activated PMNs from Mmp-9 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-9, and then immunostained with rabbit anti-Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488. In B , PAF- and fMLP-activated PMNs from Mmp-8 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-8, and then immunostained with rabbit anti-Mmp-8 IgG, or non-immune rabbit IgG followed by goat- anti-rabbit F(ab) 2 -conjugated to Alexa 488. In A-B , the antibodies used detect both the pro and active forms of the Mmps. Data are mean + SEM; n = 150–200 cells per group. Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Binding Assay, Mouse Assay, Incubation, Two Tailed Test

    Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody (IgG) response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P

    Journal: Vaccine

    Article Title: Recombinant Attenuated Listeria monocytogenes Vaccine Expressing Francisella tularensis IglC Induces Protection in Mice Against Aerosolized Type A F. tularensis

    doi: 10.1016/j.vaccine.2008.12.014

    Figure Lengend Snippet: Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody (IgG) response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P

    Article Snippet: Protein expression by recombinant L. monocytogenes was analyzed by Western blotting using rabbit polyclonal antibodies specific to AcpA, Bfr, DnaK, GroEL, IglC, KatG, or Pld at a dilution of 1:5,000 and subsequently horseradish peroxidase-conjugated goat anti-rabbit immunoglobulin G (Bio-Rad) at a dilution of 1:25,000.

    Techniques: Recombinant, Mouse Assay, Plasmid Preparation, Expressing, Enzyme-linked Immunosorbent Assay