strepavidin  (Thermo Fisher)


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    Structured Review

    Thermo Fisher strepavidin
    Fig. 3. Raft disruption interferes with the initiation of Fas signaling. ( A ) Disruption of rafts following cholesterol depletion by MβCD. Brij 98-solubilized PNS of thymocytes (2 × 10 8 ) untreated or treated with MβCD (10 mM for 12 min at 37°C) were fractionated on a sucrose gradient. Molecules in each fraction were resolved by SDS–PAGE and blotted with the indicated probes. Fas, Fyn and GM1 were analyzed under reducing conditions while Thy-1 and LAT under non-reducing conditions. ( B ) Blockade of the membrane recruitment of FADD and caspase-8 by MβCD. Thymocytes (1.6 × 10 8 ) pretreated or not with MβCD as in (A) were left unstimulated or stimulated with 2.5 µg/ml Jo2 mAb plus 5 µg/ml protein A for 5 min at 37°C. Membrane fractions were then prepared from PNS, resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively. ( C ) Inhibition of the Fas-triggered DISC formation by MβCD. Thymocytes (1.6 × 10 8 ) were left untreated or treated with MβCD as in (A), before being stimulated with 2.5 µg/ml biotinylated Jo2 mAb plus 5 µg/ml <t>streptavidin</t> for 5 min at 37°C. Following membrane solubilization by 1% Triton X-100 at 4°C, the DISC was immunoprecipitated with protein A–Sepharose via the Jo2 mAb used for stimulation. As a control for the DISC isolation, lysate from unstimulated cells was immunoprecipitated with 0.25 µg/ml Jo2 mAb plus 0.5 µg/ml streptavidin and protein A–Sepharose as described in Methods. Fas immunoprecipitates were resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively.
    Strepavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/strepavidin/product/Thermo Fisher
    Average 96 stars, based on 16 article reviews
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    strepavidin - by Bioz Stars, 2022-11
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    Images

    1) Product Images from "An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes"

    Article Title: An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes

    Journal: EMBO Reports

    doi: 10.1093/embo-reports/kvf022

    Fig. 3. Raft disruption interferes with the initiation of Fas signaling. ( A ) Disruption of rafts following cholesterol depletion by MβCD. Brij 98-solubilized PNS of thymocytes (2 × 10 8 ) untreated or treated with MβCD (10 mM for 12 min at 37°C) were fractionated on a sucrose gradient. Molecules in each fraction were resolved by SDS–PAGE and blotted with the indicated probes. Fas, Fyn and GM1 were analyzed under reducing conditions while Thy-1 and LAT under non-reducing conditions. ( B ) Blockade of the membrane recruitment of FADD and caspase-8 by MβCD. Thymocytes (1.6 × 10 8 ) pretreated or not with MβCD as in (A) were left unstimulated or stimulated with 2.5 µg/ml Jo2 mAb plus 5 µg/ml protein A for 5 min at 37°C. Membrane fractions were then prepared from PNS, resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively. ( C ) Inhibition of the Fas-triggered DISC formation by MβCD. Thymocytes (1.6 × 10 8 ) were left untreated or treated with MβCD as in (A), before being stimulated with 2.5 µg/ml biotinylated Jo2 mAb plus 5 µg/ml streptavidin for 5 min at 37°C. Following membrane solubilization by 1% Triton X-100 at 4°C, the DISC was immunoprecipitated with protein A–Sepharose via the Jo2 mAb used for stimulation. As a control for the DISC isolation, lysate from unstimulated cells was immunoprecipitated with 0.25 µg/ml Jo2 mAb plus 0.5 µg/ml streptavidin and protein A–Sepharose as described in Methods. Fas immunoprecipitates were resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively.
    Figure Legend Snippet: Fig. 3. Raft disruption interferes with the initiation of Fas signaling. ( A ) Disruption of rafts following cholesterol depletion by MβCD. Brij 98-solubilized PNS of thymocytes (2 × 10 8 ) untreated or treated with MβCD (10 mM for 12 min at 37°C) were fractionated on a sucrose gradient. Molecules in each fraction were resolved by SDS–PAGE and blotted with the indicated probes. Fas, Fyn and GM1 were analyzed under reducing conditions while Thy-1 and LAT under non-reducing conditions. ( B ) Blockade of the membrane recruitment of FADD and caspase-8 by MβCD. Thymocytes (1.6 × 10 8 ) pretreated or not with MβCD as in (A) were left unstimulated or stimulated with 2.5 µg/ml Jo2 mAb plus 5 µg/ml protein A for 5 min at 37°C. Membrane fractions were then prepared from PNS, resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively. ( C ) Inhibition of the Fas-triggered DISC formation by MβCD. Thymocytes (1.6 × 10 8 ) were left untreated or treated with MβCD as in (A), before being stimulated with 2.5 µg/ml biotinylated Jo2 mAb plus 5 µg/ml streptavidin for 5 min at 37°C. Following membrane solubilization by 1% Triton X-100 at 4°C, the DISC was immunoprecipitated with protein A–Sepharose via the Jo2 mAb used for stimulation. As a control for the DISC isolation, lysate from unstimulated cells was immunoprecipitated with 0.25 µg/ml Jo2 mAb plus 0.5 µg/ml streptavidin and protein A–Sepharose as described in Methods. Fas immunoprecipitates were resolved by SDS–PAGE and blotted with Fas-, FADD- and caspase-8-specific antibodies, respectively.

    Techniques Used: SDS Page, Inhibition, Immunoprecipitation, Isolation

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