streptavidin-pod enzyme conjugate Search Results


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  • 99
    Millipore streptavidin peroxidase conjugate
    Semaphorin 3A specifically binds sAPPα. (A) Wells in a 96-well plate were coated with either 50 ng sAPPα 695 (APP), 1 µg BSA or 50 ng Semaphorin 3A (Sema3A), blocked with 1% BSA and overlayed with different concentrations of Sema3A or sAPPα 695 (as indicated below the lanes). After washing, binding was determined by probing with anti-Sema3A antibody. The graph shows concentration-dependent binding of Sema3A to sAPPα 695 by densitometric quantification of the immunodots using NIH Image J. Bars represent averages of three independent experiments performed in triplicate each. The blot illustrates a representative experiment. (B) Wells in a 96-well plate were coated with 100 ng sAPPα 695 (APP), blocked with 1% BSA and incubated with increasing volumes of conditioned medium containing alkaline phosphatase-conjugated Semaphorin 3A (Sema3A-AP). After washing, binding was determined by measuring alkaline phosphatase activity. Bars represent averages of three independent experiments performed in triplicate. (C) <t>Streptavidin-coated</t> beads were incubated with biotinylated sAPPα 695 (bAPP) and Sema3A-AP-conditioned medium or control (non-transfected) medium. After washing, binding was evaluated by measuring alkaline phosphatase activity associated with the beads. Bars represent averages of three independent experiments.
    Streptavidin Peroxidase Conjugate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 534 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin peroxidase conjugate/product/Millipore
    Average 99 stars, based on 534 article reviews
    Price from $9.99 to $1999.99
    streptavidin peroxidase conjugate - by Bioz Stars, 2020-08
    99/100 stars
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    89
    Roche streptavidin pod enzyme conjugate
    Semaphorin 3A specifically binds sAPPα. (A) Wells in a 96-well plate were coated with either 50 ng sAPPα 695 (APP), 1 µg BSA or 50 ng Semaphorin 3A (Sema3A), blocked with 1% BSA and overlayed with different concentrations of Sema3A or sAPPα 695 (as indicated below the lanes). After washing, binding was determined by probing with anti-Sema3A antibody. The graph shows concentration-dependent binding of Sema3A to sAPPα 695 by densitometric quantification of the immunodots using NIH Image J. Bars represent averages of three independent experiments performed in triplicate each. The blot illustrates a representative experiment. (B) Wells in a 96-well plate were coated with 100 ng sAPPα 695 (APP), blocked with 1% BSA and incubated with increasing volumes of conditioned medium containing alkaline phosphatase-conjugated Semaphorin 3A (Sema3A-AP). After washing, binding was determined by measuring alkaline phosphatase activity. Bars represent averages of three independent experiments performed in triplicate. (C) <t>Streptavidin-coated</t> beads were incubated with biotinylated sAPPα 695 (bAPP) and Sema3A-AP-conditioned medium or control (non-transfected) medium. After washing, binding was evaluated by measuring alkaline phosphatase activity associated with the beads. Bars represent averages of three independent experiments.
    Streptavidin Pod Enzyme Conjugate, supplied by Roche, used in various techniques. Bioz Stars score: 89/100, based on 63 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin pod enzyme conjugate/product/Roche
    Average 89 stars, based on 63 article reviews
    Price from $9.99 to $1999.99
    streptavidin pod enzyme conjugate - by Bioz Stars, 2020-08
    89/100 stars
      Buy from Supplier

    88
    R&D Systems streptavidin pod enzyme conjugate
    Semaphorin 3A specifically binds sAPPα. (A) Wells in a 96-well plate were coated with either 50 ng sAPPα 695 (APP), 1 µg BSA or 50 ng Semaphorin 3A (Sema3A), blocked with 1% BSA and overlayed with different concentrations of Sema3A or sAPPα 695 (as indicated below the lanes). After washing, binding was determined by probing with anti-Sema3A antibody. The graph shows concentration-dependent binding of Sema3A to sAPPα 695 by densitometric quantification of the immunodots using NIH Image J. Bars represent averages of three independent experiments performed in triplicate each. The blot illustrates a representative experiment. (B) Wells in a 96-well plate were coated with 100 ng sAPPα 695 (APP), blocked with 1% BSA and incubated with increasing volumes of conditioned medium containing alkaline phosphatase-conjugated Semaphorin 3A (Sema3A-AP). After washing, binding was determined by measuring alkaline phosphatase activity. Bars represent averages of three independent experiments performed in triplicate. (C) <t>Streptavidin-coated</t> beads were incubated with biotinylated sAPPα 695 (bAPP) and Sema3A-AP-conditioned medium or control (non-transfected) medium. After washing, binding was evaluated by measuring alkaline phosphatase activity associated with the beads. Bars represent averages of three independent experiments.
    Streptavidin Pod Enzyme Conjugate, supplied by R&D Systems, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin pod enzyme conjugate/product/R&D Systems
    Average 88 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    streptavidin pod enzyme conjugate - by Bioz Stars, 2020-08
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    99
    Jackson Immuno pod conjugated streptavidin
    Reactivity of mAbs against apoA-I in the lipid-free state or on reconstituted discoidal HDL by ELISA. Biotinylated Cys-apoA-I in the lipid-free state or on discoidal HDL were added to 96-well microplates coated with <t>streptavidin.</t> After washing, Ab#19-17, Ab#20-7, Ab#124-2, or Ab#187-2 were added to the plates with increasing concentrations, and then detected with <t>POD-conjugated</t> anti-mouse IgG antibody.
    Pod Conjugated Streptavidin, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pod conjugated streptavidin/product/Jackson Immuno
    Average 99 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    pod conjugated streptavidin - by Bioz Stars, 2020-08
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    90
    Roche streptavidin pod conjugate
    Reactivity of mAbs against apoA-I in the lipid-free state or on reconstituted discoidal HDL by ELISA. Biotinylated Cys-apoA-I in the lipid-free state or on discoidal HDL were added to 96-well microplates coated with <t>streptavidin.</t> After washing, Ab#19-17, Ab#20-7, Ab#124-2, or Ab#187-2 were added to the plates with increasing concentrations, and then detected with <t>POD-conjugated</t> anti-mouse IgG antibody.
    Streptavidin Pod Conjugate, supplied by Roche, used in various techniques. Bioz Stars score: 90/100, based on 162 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin pod conjugate/product/Roche
    Average 90 stars, based on 162 article reviews
    Price from $9.99 to $1999.99
    streptavidin pod conjugate - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    Image Search Results


    Semaphorin 3A specifically binds sAPPα. (A) Wells in a 96-well plate were coated with either 50 ng sAPPα 695 (APP), 1 µg BSA or 50 ng Semaphorin 3A (Sema3A), blocked with 1% BSA and overlayed with different concentrations of Sema3A or sAPPα 695 (as indicated below the lanes). After washing, binding was determined by probing with anti-Sema3A antibody. The graph shows concentration-dependent binding of Sema3A to sAPPα 695 by densitometric quantification of the immunodots using NIH Image J. Bars represent averages of three independent experiments performed in triplicate each. The blot illustrates a representative experiment. (B) Wells in a 96-well plate were coated with 100 ng sAPPα 695 (APP), blocked with 1% BSA and incubated with increasing volumes of conditioned medium containing alkaline phosphatase-conjugated Semaphorin 3A (Sema3A-AP). After washing, binding was determined by measuring alkaline phosphatase activity. Bars represent averages of three independent experiments performed in triplicate. (C) Streptavidin-coated beads were incubated with biotinylated sAPPα 695 (bAPP) and Sema3A-AP-conditioned medium or control (non-transfected) medium. After washing, binding was evaluated by measuring alkaline phosphatase activity associated with the beads. Bars represent averages of three independent experiments.

    Journal: PLoS ONE

    Article Title: Secreted Human Amyloid Precursor Protein Binds Semaphorin 3a and Prevents Semaphorin-Induced Growth Cone Collapse

    doi: 10.1371/journal.pone.0022857

    Figure Lengend Snippet: Semaphorin 3A specifically binds sAPPα. (A) Wells in a 96-well plate were coated with either 50 ng sAPPα 695 (APP), 1 µg BSA or 50 ng Semaphorin 3A (Sema3A), blocked with 1% BSA and overlayed with different concentrations of Sema3A or sAPPα 695 (as indicated below the lanes). After washing, binding was determined by probing with anti-Sema3A antibody. The graph shows concentration-dependent binding of Sema3A to sAPPα 695 by densitometric quantification of the immunodots using NIH Image J. Bars represent averages of three independent experiments performed in triplicate each. The blot illustrates a representative experiment. (B) Wells in a 96-well plate were coated with 100 ng sAPPα 695 (APP), blocked with 1% BSA and incubated with increasing volumes of conditioned medium containing alkaline phosphatase-conjugated Semaphorin 3A (Sema3A-AP). After washing, binding was determined by measuring alkaline phosphatase activity. Bars represent averages of three independent experiments performed in triplicate. (C) Streptavidin-coated beads were incubated with biotinylated sAPPα 695 (bAPP) and Sema3A-AP-conditioned medium or control (non-transfected) medium. After washing, binding was evaluated by measuring alkaline phosphatase activity associated with the beads. Bars represent averages of three independent experiments.

    Article Snippet: The wells were washed six times with PBS, incubated with horseradish peroxidase-conjugated streptavidin (Sigma) for 1 h and developed with SuperSignal ELISA Femto Substrate.

    Techniques: Binding Assay, Concentration Assay, Incubation, Activity Assay, Transfection

    Antigen capture by the MP65/bglu mAb. Panel A and B. Dose-response, β-glucan and MP65p capture curves. An Fc-specific, goat anti mouse IgG coating was used for the oriented binding of the bsmAb, at various concentrations, to the ELISA plates. Plate-bound bsmAb was then reacted with different doses of biotinylated laminarin (Panel A) or MP65p (Panel B). The amount of captured antigens was revealed by the addition of peroxidase-conjugated streptavidin followed by the enzyme substrate. O.D. 450 nm readings are the mean from duplicate wells after subtraction of O.D. values from the negative controls (wells with no antigen or no bsmAbs). R 2 values of the resulting capture curves were calculated by linear regression analysis. Panel C. Dual antigen capture by the bsmAb. The ELISA plate-bound bsmAb (0.2 μgml) was reacted in comparison with different doses of biotinylated laminarin or biotinylated MP65p or with a mixture containing both biotynilated laminarin and MP65p. The ELISA assay was performed as described above for data in Panels A and B.

    Journal: PLoS ONE

    Article Title: A Murine, Bispecific Monoclonal Antibody Simultaneously Recognizing β-Glucan and MP65 Determinants in Candida Species

    doi: 10.1371/journal.pone.0148714

    Figure Lengend Snippet: Antigen capture by the MP65/bglu mAb. Panel A and B. Dose-response, β-glucan and MP65p capture curves. An Fc-specific, goat anti mouse IgG coating was used for the oriented binding of the bsmAb, at various concentrations, to the ELISA plates. Plate-bound bsmAb was then reacted with different doses of biotinylated laminarin (Panel A) or MP65p (Panel B). The amount of captured antigens was revealed by the addition of peroxidase-conjugated streptavidin followed by the enzyme substrate. O.D. 450 nm readings are the mean from duplicate wells after subtraction of O.D. values from the negative controls (wells with no antigen or no bsmAbs). R 2 values of the resulting capture curves were calculated by linear regression analysis. Panel C. Dual antigen capture by the bsmAb. The ELISA plate-bound bsmAb (0.2 μgml) was reacted in comparison with different doses of biotinylated laminarin or biotinylated MP65p or with a mixture containing both biotynilated laminarin and MP65p. The ELISA assay was performed as described above for data in Panels A and B.

    Article Snippet: Wells were washed again and the amount of bound antigen was evaluated by the addition of horse-radish peroxidase-conjugated streptavidin (Sigma-Aldrich) followed by 3,3′,5,5′-tetramethylbenzidine-H2 O2 substrate solution (1-step Ultra-TMB ELISA, Thermo Scientific, USA).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

    Inhibition of biotin- G-S 59-1553 or biotin- G-S 470-1553 binding to fibronectin by unlabeled ShdA passenger domain or truncated peptides. (A) Thirty-three nanomolar biotinylated G-S 59-1553 was incubated in wells coated with fibronectin (0.25 μg) with increasing amounts of G-S 59-1553 (solid triangles), GST (solid squares), G-S 59-480 (solid circles), or G-S 470-1553 (open circles). (B) Thirty-three nanomolar biotinylated G-S 470-1553 was incubated in wells coated with fibronectin (0.25 μg) with increasing amounts of G-S 480-581 (solid triangles); G-S 602-1048 (open squares); G-S 1086-1553 (solid circles); G-S 470-1553 (open circles); a combination of G-S 480-581 , G-S 602-1048 , and G-S 1086-1553 (diamonds); or GST (solid squares). In each case, biotin associated with each well following washing was determined by ELISA using streptavidin conjugated with horseradish peroxidase. The mean A 410 values from six identical wells ± standard errors, expressed as percentages of values for control wells lacking added test peptides, are plotted.

    Journal: Journal of Bacteriology

    Article Title: Fibronectin Binding to the Salmonella enterica Serotype Typhimurium ShdA Autotransporter Protein Is Inhibited by a Monoclonal Antibody Recognizing the A3 Repeat

    doi: 10.1128/JB.186.15.4931-4939.2004

    Figure Lengend Snippet: Inhibition of biotin- G-S 59-1553 or biotin- G-S 470-1553 binding to fibronectin by unlabeled ShdA passenger domain or truncated peptides. (A) Thirty-three nanomolar biotinylated G-S 59-1553 was incubated in wells coated with fibronectin (0.25 μg) with increasing amounts of G-S 59-1553 (solid triangles), GST (solid squares), G-S 59-480 (solid circles), or G-S 470-1553 (open circles). (B) Thirty-three nanomolar biotinylated G-S 470-1553 was incubated in wells coated with fibronectin (0.25 μg) with increasing amounts of G-S 480-581 (solid triangles); G-S 602-1048 (open squares); G-S 1086-1553 (solid circles); G-S 470-1553 (open circles); a combination of G-S 480-581 , G-S 602-1048 , and G-S 1086-1553 (diamonds); or GST (solid squares). In each case, biotin associated with each well following washing was determined by ELISA using streptavidin conjugated with horseradish peroxidase. The mean A 410 values from six identical wells ± standard errors, expressed as percentages of values for control wells lacking added test peptides, are plotted.

    Article Snippet: Alternatively, biotinylated protein ligand was detected with 1/1,000 streptavidin-horseradish peroxidase polymer conjugate (Sigma) in PBS, pH 7.4, and 0.04% Tween 20.

    Techniques: Inhibition, Binding Assay, Incubation, Enzyme-linked Immunosorbent Assay

    Reactivity of mAbs against apoA-I in the lipid-free state or on reconstituted discoidal HDL by ELISA. Biotinylated Cys-apoA-I in the lipid-free state or on discoidal HDL were added to 96-well microplates coated with streptavidin. After washing, Ab#19-17, Ab#20-7, Ab#124-2, or Ab#187-2 were added to the plates with increasing concentrations, and then detected with POD-conjugated anti-mouse IgG antibody.

    Journal: Scientific Reports

    Article Title: Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies

    doi: 10.1038/s41598-017-03208-8

    Figure Lengend Snippet: Reactivity of mAbs against apoA-I in the lipid-free state or on reconstituted discoidal HDL by ELISA. Biotinylated Cys-apoA-I in the lipid-free state or on discoidal HDL were added to 96-well microplates coated with streptavidin. After washing, Ab#19-17, Ab#20-7, Ab#124-2, or Ab#187-2 were added to the plates with increasing concentrations, and then detected with POD-conjugated anti-mouse IgG antibody.

    Article Snippet: Wells were washed with T-PBS, and then incubated for 30 min at 37 °C with 1.0 μg/ml POD-conjugated streptavidin (Jackson ImmunoResearch) in G-PBS (100 μl/well).

    Techniques: Enzyme-linked Immunosorbent Assay

    Sandwich ELISA for detection of lipid-free and HDL-bound apoA-I. ApoA-I in the lipid-free state ( A ), on reconstituted discoidal HDL ( B ) and spherical HDL ( C ), and human plasma HDL ( D ) were added to the plates coated with Ab#124-2. After washing, biotinylated Ab#19-17, Ab#20-7, or Ab#187-2 were added to the plates, and then detected with POD-conjugated streptavidin.

    Journal: Scientific Reports

    Article Title: Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies

    doi: 10.1038/s41598-017-03208-8

    Figure Lengend Snippet: Sandwich ELISA for detection of lipid-free and HDL-bound apoA-I. ApoA-I in the lipid-free state ( A ), on reconstituted discoidal HDL ( B ) and spherical HDL ( C ), and human plasma HDL ( D ) were added to the plates coated with Ab#124-2. After washing, biotinylated Ab#19-17, Ab#20-7, or Ab#187-2 were added to the plates, and then detected with POD-conjugated streptavidin.

    Article Snippet: Wells were washed with T-PBS, and then incubated for 30 min at 37 °C with 1.0 μg/ml POD-conjugated streptavidin (Jackson ImmunoResearch) in G-PBS (100 μl/well).

    Techniques: Sandwich ELISA

    Reactivity of the present monoclonal antibodies to full-length and the N-terminal 1–83 fragment of apoA-I. Biotinylated full-length apoA-I or its N-terminal 1–83 fragment (0.3 μM) in G-PBS, or PBS (for examining the background value) was added to 96-well microplates coated with streptavidin, and then incubated for 30 min at 37 °C. After washing the wells with T-PBS, hybridoma supernatants, 500-fold diluted with G-PBS, were added to the wells (100 μl/well) and incubated at 37 °C for 30 min. After washing, POD-conjugated anti-mouse IgG antibody diluted at 1:5000 in G-PBS (100 μl/well) was added and incubated for 30 min at 37 °C. The wells were washed and bound POD activity was determined colorimetrically (see Materials and Methods). *** P

    Journal: Scientific Reports

    Article Title: Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies

    doi: 10.1038/s41598-017-03208-8

    Figure Lengend Snippet: Reactivity of the present monoclonal antibodies to full-length and the N-terminal 1–83 fragment of apoA-I. Biotinylated full-length apoA-I or its N-terminal 1–83 fragment (0.3 μM) in G-PBS, or PBS (for examining the background value) was added to 96-well microplates coated with streptavidin, and then incubated for 30 min at 37 °C. After washing the wells with T-PBS, hybridoma supernatants, 500-fold diluted with G-PBS, were added to the wells (100 μl/well) and incubated at 37 °C for 30 min. After washing, POD-conjugated anti-mouse IgG antibody diluted at 1:5000 in G-PBS (100 μl/well) was added and incubated for 30 min at 37 °C. The wells were washed and bound POD activity was determined colorimetrically (see Materials and Methods). *** P

    Article Snippet: Wells were washed with T-PBS, and then incubated for 30 min at 37 °C with 1.0 μg/ml POD-conjugated streptavidin (Jackson ImmunoResearch) in G-PBS (100 μl/well).

    Techniques: Incubation, Activity Assay