streptavidin beaded agarose  (Millipore)


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    Structured Review

    Millipore streptavidin beaded agarose
    Purification of a larger NRE-associated protein complex. ( A ) Comparison of complete HeLa cell nuclear extract (lane 1) with extracts depleted by preincubation with biotinylated NRE–RNA and adsorption on <t>streptavidin</t> beads (lanes 2 and 4) or depleted by preincubation with poly(U) Sepharose in the presence of 2 M KCl (lane 3). Release of NRE-bound proteins from streptavidin beads by RNase treatment (lane 5). ▸, 65-kDa protein; ○, depleted 65-kDa protein; [cirf], enriched proteins; R, RNase A.
    Streptavidin Beaded Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin beaded agarose/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin beaded agarose - by Bioz Stars, 2020-04
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    Images

    1) Product Images from "A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA"

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi:

    Purification of a larger NRE-associated protein complex. ( A ) Comparison of complete HeLa cell nuclear extract (lane 1) with extracts depleted by preincubation with biotinylated NRE–RNA and adsorption on streptavidin beads (lanes 2 and 4) or depleted by preincubation with poly(U) Sepharose in the presence of 2 M KCl (lane 3). Release of NRE-bound proteins from streptavidin beads by RNase treatment (lane 5). ▸, 65-kDa protein; ○, depleted 65-kDa protein; [cirf], enriched proteins; R, RNase A.
    Figure Legend Snippet: Purification of a larger NRE-associated protein complex. ( A ) Comparison of complete HeLa cell nuclear extract (lane 1) with extracts depleted by preincubation with biotinylated NRE–RNA and adsorption on streptavidin beads (lanes 2 and 4) or depleted by preincubation with poly(U) Sepharose in the presence of 2 M KCl (lane 3). Release of NRE-bound proteins from streptavidin beads by RNase treatment (lane 5). ▸, 65-kDa protein; ○, depleted 65-kDa protein; [cirf], enriched proteins; R, RNase A.

    Techniques Used: Purification, Adsorption

    Related Articles

    In Vitro:

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Paragraph title: In vitro DNA-protein binding assay. ... Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry.

    Synthesized:

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Biotine-labeled, double-stranded oligonucleotide probes corresponding to the different binding sites were synthesized by Isogen. .. Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry.

    Purification:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: For depletion or purification of the NRE binding activity, nuclear extracts (100 μg protein) were incubated with 1 μg biotinylated probe N in 150 μl binding buffer for 30 min at 4°C. .. The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer.

    Electrophoresis:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer. .. Undepleted or depleted extracts corresponding to 10 μg extract input and wash or eluate fractions corresponding to 50 μg extract input were separated by electrophoresis on SDS/polyacrylamide gels and silver stained.

    Incubation:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: For depletion or purification of the NRE binding activity, nuclear extracts (100 μg protein) were incubated with 1 μg biotinylated probe N in 150 μl binding buffer for 30 min at 4°C. .. The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer.

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Binding of proteins to the specific probes of the TNF-α and COX-2 promoters was analyzed by a DNA-protein binding assay, by using streptavidin-coated beads to bind biotinylated DNA probe, which was incubated with nuclear extract proteins. .. Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry.

    Activity Assay:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: For depletion or purification of the NRE binding activity, nuclear extracts (100 μg protein) were incubated with 1 μg biotinylated probe N in 150 μl binding buffer for 30 min at 4°C. .. The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer.

    Polyacrylamide Gel Electrophoresis:

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry. .. The bound proteins were eluted in loading buffer and separated by 4 to 15% PAGE, followed by Western blot analysis with the indicated antibodies.

    Staining:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer. .. Undepleted or depleted extracts corresponding to 10 μg extract input and wash or eluate fractions corresponding to 50 μg extract input were separated by electrophoresis on SDS/polyacrylamide gels and silver stained.

    Sequencing:

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: The control probe was an irrelevant DNA sequence (5′-biotine-TTACCAACTGAGCCATCTCC-3′). .. Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry.

    Western Blot:

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry. .. The bound proteins were eluted in loading buffer and separated by 4 to 15% PAGE, followed by Western blot analysis with the indicated antibodies.

    Binding Assay:

    Article Title: A cellular 65-kDa protein recognizes the negative regulatory element of human papillomavirus late mRNA
    Article Snippet: .. The RNA and associated proteins were then bound for 20 min at 20°C to 200 μl 4% streptavidin-beaded agarose (Sigma) equilibrated in binding buffer. .. The unbound fraction was removed, the beads were washed twice in 500 μl binding buffer, and once in binding buffer with 300 mM KCl.

    Article Title: African Swine Fever Virus Blocks the Host Cell Antiviral Inflammatory Response through a Direct Inhibition of PKC-?-Mediated p300 Transactivation ▿
    Article Snippet: Paragraph title: In vitro DNA-protein binding assay. ... Briefly, 500 μg of nuclear extract proteins from stimulated or unstimulated Jurkat-pcDNA and Jurkat-A238L cells was mixed with 5 μg of biotinylated probe and 50 μl of 4% streptavidin beaded agarose (Sigma) with 70% slurry.

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  • 86
    Millipore adherent biotinylated cells
    PrP C interacts with a 80 kDa protein in microdomains of 1C11 5-HT and 1C11 NE neuronal cells. Lipid rafts from 1C11 5-HT , 1C11 NE and 1C11 precursor cells were prepared after biotinylation of membrane proteins. PrP C was immunoprecipitated either with an anti-N-ter monoclonal antibody (SAF34) or an anti-C-ter antibody (Bar221) covalently linked to sepharose beads. The <t>biotinylated</t> PrP C complexes were separated on a 12% SDS-PAGE to visualize all the PrP C species (A) and on an 8% gel to better separate PrP C co-immunoprecipitated protein of higher apparent molecular mass (B). Biotinylated proteins were revealed with streptavidin peroxidase conjugate. The 80 kDa protein that co-immunoprecipitates with PrP C in 1C11 5-HT is indicated by an arrow.
    Adherent Biotinylated Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adherent biotinylated cells/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adherent biotinylated cells - by Bioz Stars, 2020-04
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    86
    Millipore irdye800cw streptavidin overlay
    Crosslinking with BioATP-HDZ. ( A ) Structure of 2-azidoadenosine 5′-trisphosphate 2′,3′-biotin-long-chain-hydrazone (BioATP-HDZ). A highly reactive nitrene is produced by UV exposure and can form a covalent bond with a neighboring peptide backbone or amino acid side chain of the protein. ( B ) Fast-twitch skeletal muscle SR membranes were specifically labeled by 10 µM BioATP-HDZ and detected by <t>IRDye800CW-streptavidin</t> in-gel overlay. The left panel is the streptavidin in-gel overlay and the right panel is the CBB stain of the same gel. Lane 1 – non-labeled SR membranes; lane 2 – SR membranes labeled with BioATP-HDZ; lane 3 – competition of BioATP-HDZ labeling by ATP in SR membranes. ( C ) Western blot with anti-RyR1 (pseudo-colored red) and anti-SERCA2 (pseudo-colored green) antibodies.
    Irdye800cw Streptavidin Overlay, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/irdye800cw streptavidin overlay/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    85
    Millipore biotinylated merozoite library
    Recombinant P. falciparum merozoite proteins recapitulate known biochemical activities. The interactions between recombinant MSP1-MSP7 ( A ), and P12-P41 ( B ) were detected in both bait-prey orientations by screening the P. falciparum merozoite library with the indicated prey proteins using the AVEXIS assay. Baits labeled with an asterisk were below threshold levels required for the assay. Bar charts show mean ± S.D.; n = 3. C , Recombinant <t>biotinylated</t> EBA175 (top panel) and EBA140 (bottom panel) immobilized on fluorescent streptavidin-coated beads bound to untreated erythrocytes (blue line). Binding was blocked by pre-treating the erythrocytes with neuraminidase (red line) or, for EBA175, pre-incubating erythrocytes with an anti-GYPA monoclonal antibody (dotted green line). Negative controls were Cd4d3 + 4-coated beads (black line).
    Biotinylated Merozoite Library, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated merozoite library/product/Millipore
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    biotinylated merozoite library - by Bioz Stars, 2020-04
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    Image Search Results


    PrP C interacts with a 80 kDa protein in microdomains of 1C11 5-HT and 1C11 NE neuronal cells. Lipid rafts from 1C11 5-HT , 1C11 NE and 1C11 precursor cells were prepared after biotinylation of membrane proteins. PrP C was immunoprecipitated either with an anti-N-ter monoclonal antibody (SAF34) or an anti-C-ter antibody (Bar221) covalently linked to sepharose beads. The biotinylated PrP C complexes were separated on a 12% SDS-PAGE to visualize all the PrP C species (A) and on an 8% gel to better separate PrP C co-immunoprecipitated protein of higher apparent molecular mass (B). Biotinylated proteins were revealed with streptavidin peroxidase conjugate. The 80 kDa protein that co-immunoprecipitates with PrP C in 1C11 5-HT is indicated by an arrow.

    Journal: PLoS ONE

    Article Title: The Cellular Prion Protein Interacts with the Tissue Non-Specific Alkaline Phosphatase in Membrane Microdomains of Bioaminergic Neuronal Cells

    doi: 10.1371/journal.pone.0006497

    Figure Lengend Snippet: PrP C interacts with a 80 kDa protein in microdomains of 1C11 5-HT and 1C11 NE neuronal cells. Lipid rafts from 1C11 5-HT , 1C11 NE and 1C11 precursor cells were prepared after biotinylation of membrane proteins. PrP C was immunoprecipitated either with an anti-N-ter monoclonal antibody (SAF34) or an anti-C-ter antibody (Bar221) covalently linked to sepharose beads. The biotinylated PrP C complexes were separated on a 12% SDS-PAGE to visualize all the PrP C species (A) and on an 8% gel to better separate PrP C co-immunoprecipitated protein of higher apparent molecular mass (B). Biotinylated proteins were revealed with streptavidin peroxidase conjugate. The 80 kDa protein that co-immunoprecipitates with PrP C in 1C11 5-HT is indicated by an arrow.

    Article Snippet: Adherent biotinylated cells were washed and GSL were isolated as above, except they were diluted in NET buffer (150 mM NaCl, 50 mM Tris HCl pH 7.4, 5 mM EDTA) containing 1% Tx-100 (Calbiochem) and heated 1 h at 37°C in order to improve solubilisation of proteins embedded into cholesterol and to allow further immunoprecipitation of PrPC complexes.

    Techniques: Immunoprecipitation, SDS Page

    Crosslinking with BioATP-HDZ. ( A ) Structure of 2-azidoadenosine 5′-trisphosphate 2′,3′-biotin-long-chain-hydrazone (BioATP-HDZ). A highly reactive nitrene is produced by UV exposure and can form a covalent bond with a neighboring peptide backbone or amino acid side chain of the protein. ( B ) Fast-twitch skeletal muscle SR membranes were specifically labeled by 10 µM BioATP-HDZ and detected by IRDye800CW-streptavidin in-gel overlay. The left panel is the streptavidin in-gel overlay and the right panel is the CBB stain of the same gel. Lane 1 – non-labeled SR membranes; lane 2 – SR membranes labeled with BioATP-HDZ; lane 3 – competition of BioATP-HDZ labeling by ATP in SR membranes. ( C ) Western blot with anti-RyR1 (pseudo-colored red) and anti-SERCA2 (pseudo-colored green) antibodies.

    Journal: PLoS ONE

    Article Title: Identification of ATP-Binding Regions in the RyR1 Ca2+ Release Channel

    doi: 10.1371/journal.pone.0048725

    Figure Lengend Snippet: Crosslinking with BioATP-HDZ. ( A ) Structure of 2-azidoadenosine 5′-trisphosphate 2′,3′-biotin-long-chain-hydrazone (BioATP-HDZ). A highly reactive nitrene is produced by UV exposure and can form a covalent bond with a neighboring peptide backbone or amino acid side chain of the protein. ( B ) Fast-twitch skeletal muscle SR membranes were specifically labeled by 10 µM BioATP-HDZ and detected by IRDye800CW-streptavidin in-gel overlay. The left panel is the streptavidin in-gel overlay and the right panel is the CBB stain of the same gel. Lane 1 – non-labeled SR membranes; lane 2 – SR membranes labeled with BioATP-HDZ; lane 3 – competition of BioATP-HDZ labeling by ATP in SR membranes. ( C ) Western blot with anti-RyR1 (pseudo-colored red) and anti-SERCA2 (pseudo-colored green) antibodies.

    Article Snippet: Visualization of the photoaffinity labeled polypeptides was performed by IRDye800CW-streptavidin overlay either in-gel or after an over-night transfer to Immobilon-FL (Millipore).

    Techniques: Produced, Labeling, Staining, Western Blot

    Quantification of the binding affinity of BioATP-HDZ to RyR1. SR membranes were labeled with 10 µM BioATP-HDZ in the absence or presence of increasing concentrations of ATP. The crosslinking of BioATP-HDZ to RyR1 was determined by IRDye800CW-streptavidin in-gel overlay (pseudo-colored green, A ), and the signal was normalized to its respective CBB stain intensity at 700 nm (pseudo-colored red, B ). ( C ) Quantification of BioATP-HDZ crosslinking to RyR1 as the mean of 3 independent experiments ± SEM. The IC 50 determined by non-linear regression was 0.6±0.2 mM.

    Journal: PLoS ONE

    Article Title: Identification of ATP-Binding Regions in the RyR1 Ca2+ Release Channel

    doi: 10.1371/journal.pone.0048725

    Figure Lengend Snippet: Quantification of the binding affinity of BioATP-HDZ to RyR1. SR membranes were labeled with 10 µM BioATP-HDZ in the absence or presence of increasing concentrations of ATP. The crosslinking of BioATP-HDZ to RyR1 was determined by IRDye800CW-streptavidin in-gel overlay (pseudo-colored green, A ), and the signal was normalized to its respective CBB stain intensity at 700 nm (pseudo-colored red, B ). ( C ) Quantification of BioATP-HDZ crosslinking to RyR1 as the mean of 3 independent experiments ± SEM. The IC 50 determined by non-linear regression was 0.6±0.2 mM.

    Article Snippet: Visualization of the photoaffinity labeled polypeptides was performed by IRDye800CW-streptavidin overlay either in-gel or after an over-night transfer to Immobilon-FL (Millipore).

    Techniques: Binding Assay, Labeling, Staining

    Detection of BioATP-HDZ-labeled tryptic fragments. SR membranes were labeled with BioATP-HDZ in the absence ( A , B ) and presence ( C , D ) of ATP. Following the crosslinking, the SR membranes were digested with trypsin, solubilized with 2% CHAPS and separated by sucrose gradient centrifugation. Sucrose gradient fractions were analyzed by SDS-PAGE and labeled fragments were detected by in-gel IRDye800CW-streptavidin overlay at 800 nm. ( A , C ). The gels were then stained with CBB and scanned at 700 nm ( B , D ). Sucrose gradient RyR1 peak fractions are shown; fraction 20 was analyzed as an internal control for BioATP-HDZ labeling of SERCA. The number of the sucrose gradient fraction run in each lane is labeled above gels in A–D. ( E ) Purified RyR1 crosslinked with BioATP-HDZ, digested with trypsin and transferred to immobilon-FL membrane: lane 1 – molecular weight standards; lane 2 – IRDye800CW-streptavidin overlay; lane 3 – CBB staining. ( F ) Immunoblotting of the trypsin-digested labeled RyR1 with a specific antibody against RyR1 amino acid sequence 416–434. ( G ) Plot of the normalized relative fluorescence (RFU) calculated for individual BioATP-HDZ-labeled tryptic fragments of RyR1 detected in SR membranes (blue) and purified RyR1 (red), error bars represent SEM (N = 3) and * indicates p

    Journal: PLoS ONE

    Article Title: Identification of ATP-Binding Regions in the RyR1 Ca2+ Release Channel

    doi: 10.1371/journal.pone.0048725

    Figure Lengend Snippet: Detection of BioATP-HDZ-labeled tryptic fragments. SR membranes were labeled with BioATP-HDZ in the absence ( A , B ) and presence ( C , D ) of ATP. Following the crosslinking, the SR membranes were digested with trypsin, solubilized with 2% CHAPS and separated by sucrose gradient centrifugation. Sucrose gradient fractions were analyzed by SDS-PAGE and labeled fragments were detected by in-gel IRDye800CW-streptavidin overlay at 800 nm. ( A , C ). The gels were then stained with CBB and scanned at 700 nm ( B , D ). Sucrose gradient RyR1 peak fractions are shown; fraction 20 was analyzed as an internal control for BioATP-HDZ labeling of SERCA. The number of the sucrose gradient fraction run in each lane is labeled above gels in A–D. ( E ) Purified RyR1 crosslinked with BioATP-HDZ, digested with trypsin and transferred to immobilon-FL membrane: lane 1 – molecular weight standards; lane 2 – IRDye800CW-streptavidin overlay; lane 3 – CBB staining. ( F ) Immunoblotting of the trypsin-digested labeled RyR1 with a specific antibody against RyR1 amino acid sequence 416–434. ( G ) Plot of the normalized relative fluorescence (RFU) calculated for individual BioATP-HDZ-labeled tryptic fragments of RyR1 detected in SR membranes (blue) and purified RyR1 (red), error bars represent SEM (N = 3) and * indicates p

    Article Snippet: Visualization of the photoaffinity labeled polypeptides was performed by IRDye800CW-streptavidin overlay either in-gel or after an over-night transfer to Immobilon-FL (Millipore).

    Techniques: Labeling, Gradient Centrifugation, SDS Page, Staining, Purification, Molecular Weight, Sequencing, Fluorescence

    Recombinant P. falciparum merozoite proteins recapitulate known biochemical activities. The interactions between recombinant MSP1-MSP7 ( A ), and P12-P41 ( B ) were detected in both bait-prey orientations by screening the P. falciparum merozoite library with the indicated prey proteins using the AVEXIS assay. Baits labeled with an asterisk were below threshold levels required for the assay. Bar charts show mean ± S.D.; n = 3. C , Recombinant biotinylated EBA175 (top panel) and EBA140 (bottom panel) immobilized on fluorescent streptavidin-coated beads bound to untreated erythrocytes (blue line). Binding was blocked by pre-treating the erythrocytes with neuraminidase (red line) or, for EBA175, pre-incubating erythrocytes with an anti-GYPA monoclonal antibody (dotted green line). Negative controls were Cd4d3 + 4-coated beads (black line).

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: A Library of Functional Recombinant Cell-surface and Secreted P. falciparum Merozoite Proteins *

    doi: 10.1074/mcp.O113.028357

    Figure Lengend Snippet: Recombinant P. falciparum merozoite proteins recapitulate known biochemical activities. The interactions between recombinant MSP1-MSP7 ( A ), and P12-P41 ( B ) were detected in both bait-prey orientations by screening the P. falciparum merozoite library with the indicated prey proteins using the AVEXIS assay. Baits labeled with an asterisk were below threshold levels required for the assay. Bar charts show mean ± S.D.; n = 3. C , Recombinant biotinylated EBA175 (top panel) and EBA140 (bottom panel) immobilized on fluorescent streptavidin-coated beads bound to untreated erythrocytes (blue line). Binding was blocked by pre-treating the erythrocytes with neuraminidase (red line) or, for EBA175, pre-incubating erythrocytes with an anti-GYPA monoclonal antibody (dotted green line). Negative controls were Cd4d3 + 4-coated beads (black line).

    Article Snippet: The prey pentamers were screened against the whole biotinylated merozoite library, and positive interactions identified by detecting colorimetric turnover of nitrocefin (Calbiochem, San Diego, CA) at 485 nm.

    Techniques: Recombinant, Labeling, Binding Assay