horseradish peroxidase hrp conjugated rabbit anti mouse igg  (Agilent technologies)

 
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    Agilent technologies horseradish peroxidase hrp conjugated rabbit anti mouse igg
    Staphylococcus aureus LAC* releases SpA. S. aureus was grown to an OD 600 of 1.2. Cell wall extracts (CW) were diluted 1:5 prior to loading on the gel, and supernatant samples (SN) were not diluted. Protein A was detected using <t>HRP-conjugated</t> rabbit <t>IgG</t> (A), SdrE was detected using anti-SdrE IgG (B), and V8 was detected using anti-V8 serum (C). S. aureus LAC* sbi was grown to an OD 600 of 0.3 or 1.2 as indicated (D). Cell wall extracts were diluted 1:20, and supernatant samples were not diluted. Size markers are indicated (kDa).
    Horseradish Peroxidase Hrp Conjugated Rabbit Anti Mouse Igg, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Protein A Is Released into the Staphylococcus aureus Culture Supernatant with an Unprocessed Sorting Signal"

    Article Title: Protein A Is Released into the Staphylococcus aureus Culture Supernatant with an Unprocessed Sorting Signal

    Journal: Infection and Immunity

    doi: 10.1128/IAI.03122-14

    Staphylococcus aureus LAC* releases SpA. S. aureus was grown to an OD 600 of 1.2. Cell wall extracts (CW) were diluted 1:5 prior to loading on the gel, and supernatant samples (SN) were not diluted. Protein A was detected using HRP-conjugated rabbit IgG (A), SdrE was detected using anti-SdrE IgG (B), and V8 was detected using anti-V8 serum (C). S. aureus LAC* sbi was grown to an OD 600 of 0.3 or 1.2 as indicated (D). Cell wall extracts were diluted 1:20, and supernatant samples were not diluted. Size markers are indicated (kDa).
    Figure Legend Snippet: Staphylococcus aureus LAC* releases SpA. S. aureus was grown to an OD 600 of 1.2. Cell wall extracts (CW) were diluted 1:5 prior to loading on the gel, and supernatant samples (SN) were not diluted. Protein A was detected using HRP-conjugated rabbit IgG (A), SdrE was detected using anti-SdrE IgG (B), and V8 was detected using anti-V8 serum (C). S. aureus LAC* sbi was grown to an OD 600 of 0.3 or 1.2 as indicated (D). Cell wall extracts were diluted 1:20, and supernatant samples were not diluted. Size markers are indicated (kDa).

    Techniques Used:

    LytM contributes to release of protein A by LAC*. (A and B) Culture supernatants from LAC* sbi and LAC* sbi lytM grown to the OD 600 indicated were probed with HRP-labeled rabbit IgG in Western immunoblotting. Supernatants harvested at an OD 600 of 0.3 were concentrated 8-fold before being loaded on a gel, and supernatants harvested at an OD 600 of 1.2 were concentrated 2-fold. Size markers are indicated (kDa). (C) Protein A on the surface of LAC* sbi and LAC* sbi lytM was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured by flow cytometry. Values are plotted as a percentage of the mean fluorescence intensity measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean values, and error bars indicate the standard errors of the means of three independent experiments. (D) Protein was captured from culture supernatants using chicken anti-SpA polyclonal IgY and detected using biotin-conjugated mouse monoclonal anti-SpA IgG followed by streptavidin-HRP in an ELISA. Values are expressed as a percentage of total released SpA measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean percent release from four independent experiments. Error bars represent the standard errors of the means. **, P = 0.006; ***, P = 0.0003; ns, not significant ( P > 0.05).
    Figure Legend Snippet: LytM contributes to release of protein A by LAC*. (A and B) Culture supernatants from LAC* sbi and LAC* sbi lytM grown to the OD 600 indicated were probed with HRP-labeled rabbit IgG in Western immunoblotting. Supernatants harvested at an OD 600 of 0.3 were concentrated 8-fold before being loaded on a gel, and supernatants harvested at an OD 600 of 1.2 were concentrated 2-fold. Size markers are indicated (kDa). (C) Protein A on the surface of LAC* sbi and LAC* sbi lytM was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured by flow cytometry. Values are plotted as a percentage of the mean fluorescence intensity measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean values, and error bars indicate the standard errors of the means of three independent experiments. (D) Protein was captured from culture supernatants using chicken anti-SpA polyclonal IgY and detected using biotin-conjugated mouse monoclonal anti-SpA IgG followed by streptavidin-HRP in an ELISA. Values are expressed as a percentage of total released SpA measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean percent release from four independent experiments. Error bars represent the standard errors of the means. **, P = 0.006; ***, P = 0.0003; ns, not significant ( P > 0.05).

    Techniques Used: Labeling, Western Blot, Fluorescence, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay

    Release of protein A into S. aureus culture supernatants can be inhibited by altering the sorting signal. (A) Protein A on the surface of LAC* spa sbi (pSpA) (black bars) and LAC* spa sbi (pSpAΩSdrESS) (white bars) was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured using flow cytometry. Values are expressed as a percentage of the mean fluorescence intensity measured for LAC* spa sbi (pSpA) grown in broth supplemented with ATc (312.5 ng/ml). Bars represent the mean of three independent experiments. Error bars represent the standard errors of the means. ns, not significant ( P > 0.05). (B) LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) were grown in broth supplemented with ATc (312.5 ng/ml), and culture supernatants were probed with HRP-conjugated rabbit IgG. Size markers are indicated (kDa). (C) Quantification of SpA in culture supernatants of LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) by ELISA. Bacteria were grown in broth supplemented with ATc (312.5 ng/ml), and SpA was captured from culture supernatants using chicken anti-SpA polyclonal IgY. Bound SpA was detected using biotin-labeled mouse monoclonal anti-SpA IgG and HRP-conjugated streptavidin in an ELISA. The absorbance at 450 nm was measured, and readings from wells incubated with culture supernatants from LAC* spa sbi (pRMC2) were subtracted from the mean readings for LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) to account for background. Values for LAC* spa sbi (pSpA ΩSdrESS) are expressed as a percentage of the values measured for LAC* spa sbi (pSpA). Bars represent the mean of three independent experiments, and error bars represent the standard errors of the means. ***, P
    Figure Legend Snippet: Release of protein A into S. aureus culture supernatants can be inhibited by altering the sorting signal. (A) Protein A on the surface of LAC* spa sbi (pSpA) (black bars) and LAC* spa sbi (pSpAΩSdrESS) (white bars) was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured using flow cytometry. Values are expressed as a percentage of the mean fluorescence intensity measured for LAC* spa sbi (pSpA) grown in broth supplemented with ATc (312.5 ng/ml). Bars represent the mean of three independent experiments. Error bars represent the standard errors of the means. ns, not significant ( P > 0.05). (B) LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) were grown in broth supplemented with ATc (312.5 ng/ml), and culture supernatants were probed with HRP-conjugated rabbit IgG. Size markers are indicated (kDa). (C) Quantification of SpA in culture supernatants of LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) by ELISA. Bacteria were grown in broth supplemented with ATc (312.5 ng/ml), and SpA was captured from culture supernatants using chicken anti-SpA polyclonal IgY. Bound SpA was detected using biotin-labeled mouse monoclonal anti-SpA IgG and HRP-conjugated streptavidin in an ELISA. The absorbance at 450 nm was measured, and readings from wells incubated with culture supernatants from LAC* spa sbi (pRMC2) were subtracted from the mean readings for LAC* spa sbi (pSpA) and LAC* spa sbi (pSpAΩSdrESS) to account for background. Values for LAC* spa sbi (pSpA ΩSdrESS) are expressed as a percentage of the values measured for LAC* spa sbi (pSpA). Bars represent the mean of three independent experiments, and error bars represent the standard errors of the means. ***, P

    Techniques Used: Labeling, Fluorescence, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay, Incubation

    Replacing the SpA sorting signal with the sorting signal from SdrE reduces release of SpA by LAC*. (A) Protein A on the surface of LAC* sbi , LAC* sbi [SpAΩSdrESS], and LAC* sbi lytM [SpAΩSdrESS] was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured using flow cytometry. Values are expressed as a percentage of the mean fluorescence intensity measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean values, and error bars indicate the standard errors of the means of three independent experiments. (B) Protein A was captured from culture supernatants using chicken anti-SpA polyclonal IgY and detected using biotin-conjugated mouse monoclonal anti-SpA IgG followed by streptavidin-HRP in an ELISA. The absorbance at 450 nm was measured, and the mean reading from wells incubated with culture supernatants from LAC* spa sbi were subtracted from the readings for all other wells to account for background. Values are expressed as a percentage of total released SpA measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean of four independent experiments. Error bars represent the standard errors of the means. **, P = 0.007; ***, P
    Figure Legend Snippet: Replacing the SpA sorting signal with the sorting signal from SdrE reduces release of SpA by LAC*. (A) Protein A on the surface of LAC* sbi , LAC* sbi [SpAΩSdrESS], and LAC* sbi lytM [SpAΩSdrESS] was detected using FITC-labeled rabbit IgG, and the fluorescence intensity was measured using flow cytometry. Values are expressed as a percentage of the mean fluorescence intensity measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean values, and error bars indicate the standard errors of the means of three independent experiments. (B) Protein A was captured from culture supernatants using chicken anti-SpA polyclonal IgY and detected using biotin-conjugated mouse monoclonal anti-SpA IgG followed by streptavidin-HRP in an ELISA. The absorbance at 450 nm was measured, and the mean reading from wells incubated with culture supernatants from LAC* spa sbi were subtracted from the readings for all other wells to account for background. Values are expressed as a percentage of total released SpA measured for LAC* sbi grown to an OD 600 of 0.3. Bars represent the mean of four independent experiments. Error bars represent the standard errors of the means. **, P = 0.007; ***, P

    Techniques Used: Labeling, Fluorescence, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay, Incubation

    Release of D3D4 reporter protein into S. aureus culture supernatants can be inhibited by altering the sorting signal. (A) Amino acid sequences of SpA and SdrE sorting signals. Amino acid coordinates are indicated. Cell wall extracts (B) and culture supernatants (C) from LAC* spa sbi (pD3D4-SpASS) and LAC* spa sbi (pD3D4-SdrESS) were probed with rabbit anti-D3D4 IgG. Bound antibody was detected using HRP-conjugated goat anti-rabbit IgG. Size markers are indicated (kDa).
    Figure Legend Snippet: Release of D3D4 reporter protein into S. aureus culture supernatants can be inhibited by altering the sorting signal. (A) Amino acid sequences of SpA and SdrE sorting signals. Amino acid coordinates are indicated. Cell wall extracts (B) and culture supernatants (C) from LAC* spa sbi (pD3D4-SpASS) and LAC* spa sbi (pD3D4-SdrESS) were probed with rabbit anti-D3D4 IgG. Bound antibody was detected using HRP-conjugated goat anti-rabbit IgG. Size markers are indicated (kDa).

    Techniques Used:

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    Lysis:

    Article Title: Protein A Is Released into the Staphylococcus aureus Culture Supernatant with an Unprocessed Sorting Signal
    Article Snippet: To extract cell wall-associated proteins, cultures of S. aureus were harvested, washed in phosphate-buffered saline (PBS), and resuspended to an OD600 of 5 or 10 in lysis buffer (50 mM Tris-HCl, 20 mM MgCl2 , pH 7.5) supplemented with raffinose (30%, wt/vol) and complete protease inhibitors (40 μl/ml; Roche). .. Blots were probed with horseradish peroxidase (HRP)-conjugated rabbit anti-mouse IgG (1:2,000 or 1:500; Dako) to detect SpA.

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    Agilent technologies goat anti mouse rabbit igg conjugated to horse radish peroxidase
    Goat Anti Mouse Rabbit Igg Conjugated To Horse Radish Peroxidase, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    goat anti mouse rabbit igg conjugated to horse radish peroxidase - by Bioz Stars, 2020-04
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