streptavidin Search Results


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  • 98
    Thermo Fisher streptavidin
    Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 10410 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore streptavidin peroxidase
    Streptavidin Peroxidase, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1414 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin agarose beads
    Streptavidin Agarose Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5686 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher dynabeads m 280 streptavidin
    Dynabeads M 280 Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4115 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin beads
    Streptavidin Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4272 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin horse radish peroxidase
    Streptavidin Horse Radish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 233 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin coated magnetic beads
    Streptavidin Coated Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5239 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin magnetic beads
    Streptavidin Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3325 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Miltenyi Biotec streptavidin microbeads
    Streptavidin Microbeads, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 99/100, based on 3221 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin alexa fluor 488 conjugate
    Streptavidin Alexa Fluor 488 Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin phycoerythrin
    Streptavidin Phycoerythrin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 6232 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher hrp conjugated streptavidin
    Hrp Conjugated Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1459 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore streptavidin agarose beads
    In vitro palmitoylation of VAMP7 by DHHC18 and DHHC20. a Schematic cartoon of constructs used, with important cysteines highlighted. Cys222 and Cys15 are the active sites of DHHC18 and DHHC20, respectively. Cys183 in VAMP7 is the site of palmitoylation. b Cartoon model of potential membrane docking of DHHC18 isoform 2 via Cys138. The full-length DHHC18 features the two N-terminal TMDs, securing the DHHC active site to the membrane. The short isoform, lacking these TMDs, may be anchored to the membrane via palmitoylation of Cys138, allowing its active-site access to the membrane environment required for its activity. c Schematic representation of the on-plate palmitoylation assay (OPPA). Briefly, the target (VAMP7, featuring both His6 and FLAG-tags) is bound to a Ni-NTA plate. The DHHC PAT is added with clickable PAA-CoA and the reaction is quenched at specific time points using NEM. Biotin is subsequently clicked on to the PAA-modified target, VAMP7 is eluted and then bound to an anti-FLAG plate. <t>Streptavidin-Eu3+</t> can then be used to quantify palmitoylated VAMP7, and a steady-state slope can be calculated. d Results of OPPA experiments of VAMP7-WT and VAMP7-C183A, palmitoylated by constructs of DHHC18 and DHHC20 ( n ≥ 12, geometric mean ± SEM shown).
    Streptavidin Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2391 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin agarose
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Streptavidin Agarose, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2017 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies streptavidin hrp
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Streptavidin Hrp, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 2444 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore streptavidin agarose
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Streptavidin Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 1589 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher streptavidin apc
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Streptavidin Apc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1992 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore streptavidin hrp
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Streptavidin Hrp, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1433 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno cy3 conjugated streptavidin
    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by <t>streptavidin</t> resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.
    Cy3 Conjugated Streptavidin, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 99/100, based on 1681 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    Atto 740 belongs to a new generation of fluorescent labels for the near infrared spectral region The dye is designed for application in the area of life science e g
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    N/A
    Source Bacterium Streptomyces avidinii The Streptavidin preparation contains an N and C terminal shortened variant core streptavidin with improved properties concerning homogeneity solubility resistance towards proteolytic degradation and accessibility of
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    N/A
    Streptavidin Streptavidin Streptavidin
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    Image Search Results


    In vitro palmitoylation of VAMP7 by DHHC18 and DHHC20. a Schematic cartoon of constructs used, with important cysteines highlighted. Cys222 and Cys15 are the active sites of DHHC18 and DHHC20, respectively. Cys183 in VAMP7 is the site of palmitoylation. b Cartoon model of potential membrane docking of DHHC18 isoform 2 via Cys138. The full-length DHHC18 features the two N-terminal TMDs, securing the DHHC active site to the membrane. The short isoform, lacking these TMDs, may be anchored to the membrane via palmitoylation of Cys138, allowing its active-site access to the membrane environment required for its activity. c Schematic representation of the on-plate palmitoylation assay (OPPA). Briefly, the target (VAMP7, featuring both His6 and FLAG-tags) is bound to a Ni-NTA plate. The DHHC PAT is added with clickable PAA-CoA and the reaction is quenched at specific time points using NEM. Biotin is subsequently clicked on to the PAA-modified target, VAMP7 is eluted and then bound to an anti-FLAG plate. Streptavidin-Eu3+ can then be used to quantify palmitoylated VAMP7, and a steady-state slope can be calculated. d Results of OPPA experiments of VAMP7-WT and VAMP7-C183A, palmitoylated by constructs of DHHC18 and DHHC20 ( n ≥ 12, geometric mean ± SEM shown).

    Journal: Communications Biology

    Article Title: Dynamic palmitoylation events following T-cell receptor signaling

    doi: 10.1038/s42003-020-1063-5

    Figure Lengend Snippet: In vitro palmitoylation of VAMP7 by DHHC18 and DHHC20. a Schematic cartoon of constructs used, with important cysteines highlighted. Cys222 and Cys15 are the active sites of DHHC18 and DHHC20, respectively. Cys183 in VAMP7 is the site of palmitoylation. b Cartoon model of potential membrane docking of DHHC18 isoform 2 via Cys138. The full-length DHHC18 features the two N-terminal TMDs, securing the DHHC active site to the membrane. The short isoform, lacking these TMDs, may be anchored to the membrane via palmitoylation of Cys138, allowing its active-site access to the membrane environment required for its activity. c Schematic representation of the on-plate palmitoylation assay (OPPA). Briefly, the target (VAMP7, featuring both His6 and FLAG-tags) is bound to a Ni-NTA plate. The DHHC PAT is added with clickable PAA-CoA and the reaction is quenched at specific time points using NEM. Biotin is subsequently clicked on to the PAA-modified target, VAMP7 is eluted and then bound to an anti-FLAG plate. Streptavidin-Eu3+ can then be used to quantify palmitoylated VAMP7, and a steady-state slope can be calculated. d Results of OPPA experiments of VAMP7-WT and VAMP7-C183A, palmitoylated by constructs of DHHC18 and DHHC20 ( n ≥ 12, geometric mean ± SEM shown).

    Article Snippet: SILAC-labeled heavy and light samples were then mixed and allowed to bind to streptavidin-agarose beads (Novagen) for 90 min at room temperature.

    Techniques: In Vitro, Construct, Activity Assay, Modification

    Enrichment of Jurkat T-cell palmitome before and after anti-CD28/anti-CD3-costimulation by acyl-biotin exchange. a Schematic representation of acyl-biotin exchange (ABE) protocol coupled with SILAC for quantitation of palmitoylated proteins via LC-MS/MS. Briefly, Jurkat cells grown in heavy SILAC media (blue) were lysed and free thiols were blocked with NEM. After cleaving palmitoyl groups with HA, previously palmitoylated thiols are biotinylated with HPDP-biotin, allowing for streptavidin enrichment. For control cells grown in light SILAC media (red), HA is omitted, preventing biotinylation. Proteins quantified with heavy/light intensity ratios > 2.0 are considered enriched and palmitoylated. b Volcano plot showing high-confidence palmitoylated proteins prior to stimulation ( n = 6, p

    Journal: Communications Biology

    Article Title: Dynamic palmitoylation events following T-cell receptor signaling

    doi: 10.1038/s42003-020-1063-5

    Figure Lengend Snippet: Enrichment of Jurkat T-cell palmitome before and after anti-CD28/anti-CD3-costimulation by acyl-biotin exchange. a Schematic representation of acyl-biotin exchange (ABE) protocol coupled with SILAC for quantitation of palmitoylated proteins via LC-MS/MS. Briefly, Jurkat cells grown in heavy SILAC media (blue) were lysed and free thiols were blocked with NEM. After cleaving palmitoyl groups with HA, previously palmitoylated thiols are biotinylated with HPDP-biotin, allowing for streptavidin enrichment. For control cells grown in light SILAC media (red), HA is omitted, preventing biotinylation. Proteins quantified with heavy/light intensity ratios > 2.0 are considered enriched and palmitoylated. b Volcano plot showing high-confidence palmitoylated proteins prior to stimulation ( n = 6, p

    Article Snippet: SILAC-labeled heavy and light samples were then mixed and allowed to bind to streptavidin-agarose beads (Novagen) for 90 min at room temperature.

    Techniques: Quantitation Assay, Liquid Chromatography with Mass Spectroscopy

    Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by streptavidin resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.

    Journal: Scientific Reports

    Article Title: Vesicular stomatitis virus G protein transmembrane region is crucial for the hemi-fusion to full fusion transition

    doi: 10.1038/s41598-018-28868-y

    Figure Lengend Snippet: Replacement of the VSV G TM region with TM regions from other membrane fusion proteins resulted in similar protein expression levels and plasma membrane localization. ( a ) Sequences of the TM regions of VSV G, Syntaxin 1 A, VAMP2 and influenza HA. ( b and c ) VSV G TM replacement did not lead to dramatic changes in the expression levels of VSV G in HeLa cells. ( d ) WT and chimeric VSV G localized onto the plasma membrane. HeLa cells were transfected with plasmids encoding WT or chimeric VSV G proteins fused with EGFP. ( e and f ) Biotinylation assays to quantify membrane-localized WT or chimeric VSV G proteins. Total VSV G levels in cells (I: input) and membrane-localized G protein levels (P: pull down by streptavidin resin) were determined by western blot. The ratio of biotinylated VSV G to total G protein was calculated. Compared to WT VSV G, chimeric mutants showed similar levels of membrane localization. Mean ± SEM.

    Article Snippet: Biotinylated membrane proteins were pulled down by streptavidin agarose resin (Thermo fisher scientific, 20349) following the manufacturer’s instructions.

    Techniques: Expressing, Transfection, Western Blot