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Flag magnetic beads

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Flag magnetic beads are small, spherical particles with a magnetic core that can be used for various laboratory applications. The core function of these beads is to enable magnetic separation and isolation of target biomolecules or cells from complex samples.

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Lab products found in correlation

Chemidoc imager, by Bio-Rad (2 mentions) Clarity or clarity max substrate, by Bio-Rad (2 mentions) 3xflag peptide, by Merck Group (2 mentions) Ab111733, by Proteintech (2 mentions) F3165, by Merck Group (2 mentions) Mg132, by Thermo Fisher Scientific (1 mentions) Mg132, by MedChemExpress (1 mentions) Sab1305535 40tst, by Merck Group (1 mentions) F7425, by Merck Group (1 mentions)

Close spelling variants of this product

Anti-Flag magnetic beads Anti-FLAG L5 Magnetic Beads Anti-FLAG M2 Magnetic Beads Flag-beads Magnetic beads

4 protocols using flag magnetic beads

1

Ubiquitination Assay with HA-Ub

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ESCC cells transfected with HA-Ub were treated with MG132 (MedChemExpress, HY-13259) with or without F806, and then ubiquitination assays were performed using denature-IP [34 (link), 59 (link)]. Briefly, cells were harvested with EBC buffer containing 4% SDS and 20 μM MG132, boiled at 95 °C for 15 min, sonicated and centrifuged. The supernatant was diluted with SDS-free EBC buffer till its concentration became one tenth of the original value, and then was used for ANLN immunoprecipitation with ANLN antibody and protein A/G magnetic beads. For immunoprecipitation using HEK293T cells, plasmids encoding HA-Ub and Flag-ANLN were co-transfected and cells were treated with MG132 for 8 h before harvest, after which Flag-ANLN was immunoprecipitated with Flag magnetic beads (Thermo Fisher Scientific, UI294205).
Cao Y.F., Xie L., Tong B.B., Chu M.Y., Shi W.Q., Li X., He J.Z., Wang S.H., Wu Z.Y., Deng D.X., Zheng Y.Q., Li Z.M., Xu X.E., Liao L.D., Cheng Y.W., Li L.Y., Xu L.Y, & Li E.M. (2022). Targeting USP10 induces degradation of oncogenic ANLN in esophageal squamous cell carcinoma. Cell Death and Differentiation, 30(2), 527-543.
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2

Co-immunoprecipitation of Arabidopsis Proteins

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Total protein from 12-day-old seedlings co-expressing ProUBQ:mCherry-CPK4-myc and ProUBQ:Venus-PUB44-Flag or ProUBQ:mCherry-CPK4-myc and ProUBQ:PUB25-Flag were extracted with protein extraction buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 1 mM EDTA, 1% NP-40, 10% glycerol, 50 mM MG132, and 1× protease inhibitor mix). Protein concentration was determined by Bicinchoninic Acid kit (SK1060-1, Coolaber). An equal amount of total protein was mixed and incubated with flag-magnetic beads (Thermo Fisher) at 4 °C overnight. The magnetic beads were washed 4 times with the 1 × extraction buffer and boiled with 1 × SDS loading buffer at 95 °C for 5 min. The proteins were separated on SDS-PAGE and detected with anti-myc (SAB1305535-40TST, Sigma, 1:5000 dilution) and anti-Flag antibodies (F7425, Sigma, 1:5000 dilution). For NaCl treatment, seedlings were incubated in 1/2 MS solution with 150 mM NaCl for 4 h.
Fan W., Liao X., Tan Y., Wang X., Schroeder J.I, & Li Z. (2023). Arabidopsis PLANT U-BOX44 down-regulates osmotic stress signaling by mediating Ca2+-DEPENDENT PROTEIN KINASE4 degradation. The Plant cell, 35(10).
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3

Immunoprecipitation of NCOA7 and E2-crimson

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U87MG cells were stably transduced with vectors carrying RRL.sin.cPPT.CMV/Flag-NCOA7.WPRE or RRL.sin.cPPT.CMV/Flag-E2-crimson-.WPRE and selected with 1 μg/ml puromycin. 15-22 x 106 cells were washed twice in cold PBS and resuspended in lysis buffer (20mM Hepes-NaOH pH 7.5, 150 mM NaCl, 1% NP-40, protease inhibitor cocktail), the lysates clarified by centrifugation at 1000g, for 10 min at 4°C and then incubated with Flag-magnetic beads (Life Technologies) for 3 hr at 4°C. The beads were washed 5 times and the immunoprecipitated proteins eluted using 3x Flag peptide (150 μg/ml, Sigma-Aldrich) for 1.5-2 hr. Cell lysates and immunoprecipitation eluates were supplemented with sample buffer (50 mM Tris-HCl pH 6.8, 2% SDS, 5% glycerol, 100 mM DTT, 0.02% bromphenol blue), resolved by SDS-PAGE and analyzed by immunoblotting using primary antibodies specific for the Flag epitope (Sigma-Aldrich F3165), tubulin (mouse monoclonal DM1A, Sigma-Aldrich T9026), ATP6V1B2 (Proteintech 15097-1-AP), ATP6V1A (Proteintech 17115-1-AP), ATP6V1E1 (Abcam Ab111733), ATP6V1G2 (Proteintech 25316-1-AP), followed by secondary horseradish peroxidase-conjugated anti-mouse, or anti-rabbit immunoglobulin antibodies and chemiluminescence Clarity or Clarity max substrate (Bio-Rad). A Bio-Rad ChemiDoc imager was used.
Doyle T., Moncorgé O., Bonaventure B., Pollpeter D., Lussignol M., Tauziet M., Apolonia L., Catanese M.T., Goujon C, & Malim M.H. (2018). The interferon inducible isoform of NCOA7 inhibits endosome-mediated viral entry. Nature microbiology, 3(12), 1369-1376.
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4

Immunoprecipitation of NCOA7 and E2-crimson

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U87MG cells were stably transduced with vectors carrying RRL.sin.cPPT.CMV/Flag-NCOA7.WPRE or RRL.sin.cPPT.CMV/Flag-E2-crimson-.WPRE and selected with 1 μg/ml puromycin. 15-22 x 106 cells were washed twice in cold PBS and resuspended in lysis buffer (20mM Hepes-NaOH pH 7.5, 150 mM NaCl, 1% NP-40, protease inhibitor cocktail), the lysates clarified by centrifugation at 1000g, for 10 min at 4°C and then incubated with Flag-magnetic beads (Life Technologies) for 3 hr at 4°C. The beads were washed 5 times and the immunoprecipitated proteins eluted using 3x Flag peptide (150 μg/ml, Sigma-Aldrich) for 1.5-2 hr. Cell lysates and immunoprecipitation eluates were supplemented with sample buffer (50 mM Tris-HCl pH 6.8, 2% SDS, 5% glycerol, 100 mM DTT, 0.02% bromphenol blue), resolved by SDS-PAGE and analyzed by immunoblotting using primary antibodies specific for the Flag epitope (Sigma-Aldrich F3165), tubulin (mouse monoclonal DM1A, Sigma-Aldrich T9026), ATP6V1B2 (Proteintech 15097-1-AP), ATP6V1A (Proteintech 17115-1-AP), ATP6V1E1 (Abcam Ab111733), ATP6V1G2 (Proteintech 25316-1-AP), followed by secondary horseradish peroxidase-conjugated anti-mouse, or anti-rabbit immunoglobulin antibodies and chemiluminescence Clarity or Clarity max substrate (Bio-Rad). A Bio-Rad ChemiDoc imager was used.
Doyle T., Moncorgé O., Bonaventure B., Pollpeter D., Lussignol M., Tauziet M., Apolonia L., Catanese M.T., Goujon C, & Malim M.H. (2018). The interferon inducible isoform of NCOA7 inhibits endosome-mediated viral entry. Nature microbiology, 3(12), 1369-1376.
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