protein binding microtiter plates Search Results


high-throughput ppase assay high protein-binding polystyrene microtiter plates  (Corning Life Sciences)
90
Corning Life Sciences high-throughput ppase assay high protein-binding polystyrene microtiter plates
A high-throughput phosphatase assay that monitors endogenous activity toward specific phosphoprotein substrates. A, recombinant phosphorylated substrate is adsorbed onto a <t>polystyrene</t> <t>microtiter</t> plate, the immobilized phosphosubstrate are treated with PPase lysate, and the dephosphorylation reaction is halted with the addition of a phosphatase inhibitor mixture. B, the remaining phosphosubstrate is labeled with anti-phosphoprotein primary antibody, biotinylated secondary antibody, and streptavidin-HRP for colorimetric detection. Phosphatase activity is determined by the drop in phosphoprotein signal in lysate-treated samples relative to negative controls.
High Throughput Ppase Assay High Protein Binding Polystyrene Microtiter Plates, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/high+throughput+ppase+assay+high+protein+binding+polystyrene+microtiter+plates/pmc03591670-69-5-8
Average 90 stars, based on 1 article reviews
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96-well microtiter plates with extra-high binding capacity for proteins  (DYNEX tech)
90
DYNEX tech 96-well microtiter plates with extra-high binding capacity for proteins
L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto <t>microtiter</t> plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.
96 Well Microtiter Plates With Extra High Binding Capacity For Proteins, supplied by DYNEX tech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/96+well+microtiter+plates+with+extra+high+binding+capacity+for+proteins/pmc01574011-78-22-32
Average 90 stars, based on 1 article reviews
96-well microtiter plates with extra-high binding capacity for proteins - by Bioz Stars, 2026-10
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low protein-binding polypropylene 96-well microtiter plate  (Corning Life Sciences)
90
Corning Life Sciences low protein-binding polypropylene 96-well microtiter plate
L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto <t>microtiter</t> plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.
Low Protein Binding Polypropylene 96 Well Microtiter Plate, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/low+protein+binding+polypropylene+96+well+microtiter+plate/pmc08582585-50-32-38
Average 90 stars, based on 1 article reviews
low protein-binding polypropylene 96-well microtiter plate - by Bioz Stars, 2026-10
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high-protein-binding capacity 96-well microtiter plates  (AGC Techno Glass Co Ltd)
90
AGC Techno Glass Co Ltd high-protein-binding capacity 96-well microtiter plates
L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto <t>microtiter</t> plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.
High Protein Binding Capacity 96 Well Microtiter Plates, supplied by AGC Techno Glass Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/high+protein+binding+capacity+96+well+microtiter+plates/pm37369727-308-13-15
Average 90 stars, based on 1 article reviews
high-protein-binding capacity 96-well microtiter plates - by Bioz Stars, 2026-10
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high-protein binding microtiter plates 517  (Corning Life Sciences)
90
Corning Life Sciences high-protein binding microtiter plates 517
L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto <t>microtiter</t> plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.
High Protein Binding Microtiter Plates 517, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/high+protein+binding+microtiter+plates+517/ppr0218702-301-0-5
Average 90 stars, based on 1 article reviews
high-protein binding microtiter plates 517 - by Bioz Stars, 2026-10
90/100 stars
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low protein binding polypropylene microtiter plates  (Corning Life Sciences)
90
Corning Life Sciences low protein binding polypropylene microtiter plates
L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto <t>microtiter</t> plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.
Low Protein Binding Polypropylene Microtiter Plates, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/protein+binding+microtiter+plates/low+protein+binding+polypropylene+microtiter+plate/pmc03022150-37-7-12
Average 90 stars, based on 1 article reviews
low protein binding polypropylene microtiter plates - by Bioz Stars, 2026-10
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A high-throughput phosphatase assay that monitors endogenous activity toward specific phosphoprotein substrates. A, recombinant phosphorylated substrate is adsorbed onto a polystyrene microtiter plate, the immobilized phosphosubstrate are treated with PPase lysate, and the dephosphorylation reaction is halted with the addition of a phosphatase inhibitor mixture. B, the remaining phosphosubstrate is labeled with anti-phosphoprotein primary antibody, biotinylated secondary antibody, and streptavidin-HRP for colorimetric detection. Phosphatase activity is determined by the drop in phosphoprotein signal in lysate-treated samples relative to negative controls.

Journal: Molecular & Cellular Proteomics : MCP

Article Title: A High-throughput Assay for Phosphoprotein-specific Phosphatase Activity in Cellular Extracts *

doi: 10.1074/mcp.O112.024059

Figure Lengend Snippet: A high-throughput phosphatase assay that monitors endogenous activity toward specific phosphoprotein substrates. A, recombinant phosphorylated substrate is adsorbed onto a polystyrene microtiter plate, the immobilized phosphosubstrate are treated with PPase lysate, and the dephosphorylation reaction is halted with the addition of a phosphatase inhibitor mixture. B, the remaining phosphosubstrate is labeled with anti-phosphoprotein primary antibody, biotinylated secondary antibody, and streptavidin-HRP for colorimetric detection. Phosphatase activity is determined by the drop in phosphoprotein signal in lysate-treated samples relative to negative controls.

Article Snippet: High-throughput PPase Assay High protein-binding polystyrene microtiter plates (Corning Costar, Lowell, MA) were coated overnight with the indicated amounts of recombinant phosphorylated MAPK.

Techniques: High Throughput Screening Assay, Phosphatase Assay, Activity Assay, Recombinant, De-Phosphorylation Assay, Labeling

ELISA-based quantification of recombinant pMAPKs adsorbed to 96-well plates. A–C, Twofold dilution series (relative level 1.0 = ∼400 ng) of pERK (A), pJNK (B), and pp38 (C) were adsorbed onto polystyrene microtiter plates and detected by ELISA using phospho-specific antibodies. The detection saturates at ∼75 ng for pERK (A), ∼400 ng for pJNK (B), and ∼75 ng for pp38 (C). Arrows indicate the quantity of pMAPKs used in the PPase assay. Data are shown as the mean ± S.E. of three independent assay replicates.

Journal: Molecular & Cellular Proteomics : MCP

Article Title: A High-throughput Assay for Phosphoprotein-specific Phosphatase Activity in Cellular Extracts *

doi: 10.1074/mcp.O112.024059

Figure Lengend Snippet: ELISA-based quantification of recombinant pMAPKs adsorbed to 96-well plates. A–C, Twofold dilution series (relative level 1.0 = ∼400 ng) of pERK (A), pJNK (B), and pp38 (C) were adsorbed onto polystyrene microtiter plates and detected by ELISA using phospho-specific antibodies. The detection saturates at ∼75 ng for pERK (A), ∼400 ng for pJNK (B), and ∼75 ng for pp38 (C). Arrows indicate the quantity of pMAPKs used in the PPase assay. Data are shown as the mean ± S.E. of three independent assay replicates.

Article Snippet: High-throughput PPase Assay High protein-binding polystyrene microtiter plates (Corning Costar, Lowell, MA) were coated overnight with the indicated amounts of recombinant phosphorylated MAPK.

Techniques: Enzyme-linked Immunosorbent Assay, Recombinant

L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto microtiter plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.

Journal:

Article Title: Dexamethasone enhances interaction of endogenous Annexin 1 with L-selectin and triggers shedding of L-selectin in the monocytic cell line U-937

doi: 10.1038/sj.bjp.0705413

Figure Lengend Snippet: L-selectin binding to ANXA1 is calcium-dependent and involves the N-terminal domain of ANXA1. (a) Comparison of the amounts of ANXA1 detected after presentation of the protein by a specific mAb or after direct binding to plastic. A monoclonal ANXA1 antibody was coated onto microtiter plates (3 μg ml−1) to capture varying concentrations of ANXA1 (mAB1-A+ANXA1). This binding was compared to the binding for the same range of ANXA1 recombinant protein concentrations directly coated on extra-high binding capacity plastic (ANXA1). In both cases, ANXA1 was detected with a polyclonal ANXA1 antibody and showed no major difference between the two methods, (b–d) Direct binding between annexins and L-selectin chimeric protein (Lec-IgM) in the presence or absence of calcium, (b) Increasing concentrations of Lec-IgM (black square) were immobilized on plastic and then incubated with 9.4 μg ml−1 of ANXA1. Internal control for nonspecific binding was determined in the presence of human IgM (hIgM) (open square), (c) Lec-IgM or human IgM were added to increasing concentrations of ANXA1, either directly coated on the plastic (ANXA1) or presented by the monoclonal antibody mAB1-A (mAB-1A+ANXA1). Presence of the ANXA1 in the assay was detected with a polyclonal antibody (mAB1-A+ANXA1) as in (a), (d) Effect of the presence of calcium of the N-terminal domain of ANXA1 on the interaction between ANXA1 and Lec-IgM. Binding of Lec-IgM (0.125 μg ml−1) to increasing concentrations of ANXA1 was compared to the binding to the same concentration range of the chimeric protein ANXA1-5 (N-terminal domain of ANXA1 (1–26) and core domain of ANXA5) or to an unrelated protein, ANXA5. Experiments were done in PBS+1 mM Ca2++1 mM Mg2+ with or without 10 mM EDTA (+EDTA). Each point represents the mean±s.e.m. of three independent experiments done in duplicates.

Article Snippet: Measurement of L-selectin binding to immobilized annexin proteins The sandwich ELISA used to determine L-selectin binding to ANXA1 was performed in 96-well microtiter plates with extra-high binding capacity for proteins (Immulon 4HBX, Dynex, Chantilly, VA, U.S.A.).

Techniques: Binding Assay, Comparison, Recombinant, Incubation, Control, Concentration Assay