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Anti c myc magnetic beads

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Anti-c-Myc magnetic beads are a laboratory tool used for the isolation and purification of proteins that are tagged with the c-Myc epitope. These beads are coated with antibodies that specifically bind to the c-Myc tag, allowing for the efficient capture and recovery of the target protein from complex biological samples.

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Lab products found in correlation

Anti flag m2 magnetic bead, by Merck Group (3 mentions) Quantstudio 6 flex real time pcr system, by Thermo Fisher Scientific (2 mentions) High capacity cdna reverse transcription kit, by Thermo Fisher Scientific (2 mentions) Anti rabbit igg peroxidase, by Cell Signaling Technology (1 mentions) Enhanced chemi luminescence (ecl), by Thermo Fisher Scientific (1 mentions) Dynabeads m 280, by Thermo Fisher Scientific (1 mentions) Anti flag m2 magnetic beads, by Thermo Fisher Scientific (1 mentions) Integrin β1, by Sino Biological (1 mentions) Protein a g magnetic bead, by Thermo Fisher Scientific (1 mentions) Protease inhibitor, by Roche (1 mentions) Phosphatase inhibitor, by Roche (1 mentions) Anti c fos antibody, by Cell Signaling Technology (1 mentions) Anti plk1 antibody, by Cell Signaling Technology (1 mentions) Magna rip kit, by Merck Group (1 mentions) 18s rrna, by Thermo Fisher Scientific (1 mentions) Cfx connect real time system, by Bio-Rad (1 mentions) Rneasy lipid tissue mini kit, by Qiagen (1 mentions) E z n a total rna kit, by Omega Bio-Tek (1 mentions)

8 protocols using anti c myc magnetic beads

1

Co-Immunoprecipitation of Myc-PATZ1 and PATZ2

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Whole-cell lysates (10 mM Hepes-KOH [pH 7.9], 2 mM MgCl2, 0.1 mMEDTA, 10 mM KCl, 0.5% NP-40) of HEK293T cells transfected with plasmids encoding Myc-PATZ1 (Keskin et al, 2015 (link)) and tagGFP- or tagRFP-PATZ2 were immunoprecipitated with anti–c-Myc magnetic beads (88842; Thermo Fisher Scientific). Bound beads were washed five times with ice-cold wash buffer (50 mM Hepes-KOH [pH 7.9], 100 mM KCl, 2% NP-40) and boiled in 1X Laemmli Buffer for 5 min. Precipitated proteins were resolved on 14% SDS–PAGE gels, transferred onto polyvinylidene difluoride (PVDF) membranes (88518; Thermo Fisher Scientific), and blotted with peroxidase-coupled anti-Myc (11814150001; Roche) or anti-GFP or anti-tRFP antibodies (Evrogen AB011, AB233), followed by anti-rabbit IgG–peroxidase (7074; Cell Signaling). Reactivity was revealed by enhanced chemiluminescence (ECL) (34580; Thermo Fisher Scientific) and visualized using a G-BOX Chemi XX6 documentation system (Syngene).
Piepoli S., Barakat S., Nogay L., Şimşek B., Akkose U., Taskiran H., Tolay N., Gezen M., Yeşilada C.Y., Tuncay M., Adebali O., Atilgan C, & Erman B. (2022). Sibling rivalry among the ZBTB transcription factor family: homodimers versus heterodimers. Life Science Alliance, 5(11), e202201474.
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2

Immunoprecipitation of Aminopeptidase N

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For
in vivoanalysis, first, we prepared anti-APN antibody-conjugated magnetic beads by coupling 100 µg mouse anti-human APN monoclonal antibody (ANOC9121; Otsuka Pharmaceutical Co., Ltd., Tokyo, Japan) to 5 mg tosylactivated Dynabeads (M-280; Invitrogen, Carlsbad, CA, USA), according to the manufacturer’s instruction. Thereafter, 0.25 mg of these magnetic beads were used for the immunoprecipitation of human serum containing 200 ng APN. For
in vitroanalysis, the supernatant of the cell culture of HEK293T cells overexpressing myc-APN and FLAG-CCL2 was used for immunoprecipitation with anti-c-myc magnetic beads (Thermo Fisher Scientific, Waltham, MA, USA) or anti-FLAG magnetic beads (MBL, Nagoya, Japan).
Fujita M., Yamamoto H., Yoshida N., Ono R., Matsuoka T, & Kihara S. (2020). Atheroprotective Roles of Adiponectin via CCL2 Inhibition. Journal of Atherosclerosis and Thrombosis, 28(11), 1204-1213.
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3

Endogenous and Exogenous Co-Immunoprecipitation of RPLP1 and NS4B

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For immunoprecipitation of endogenous RPLP1, PK15 cells transfected with the plasmids pcDNA3.1-NS4B-Flag were lysed by WB and IP lysis buffer (containing 1 mM PMSF) on ice for 0.5 h. Lysates were collected into microcentrifuge tube and centrifugated at 4°C for 0.5 h. The anti-Flag-M2 magnetic beads (#M8823, Sigma Aldrich) were placed in magnetic separator to discard the storage buffer. After washed with TBS, the equilibrated magnetic beads were co-incubated with the supernatant of protein extracts at RT for 2 h with gentle mixing to capture the Flag fusion proteins. Finally, the magnetic beads were collected with magnetic separator and washed five times with TBS followed by detecting target protein with WB.
For exogenous co-IP, HEK-293 T cells co-transfected with the plasmids pcDNA3.1-NS4B-Flag and pcDNA3.1-RPLP1-Myc. Simultaneously, cells co-transfected with pcDNA3.1-NS4B-Flag and pcDNA3.1-Myc as well as pcDNA3.1-RPLP1-Myc and pcDNA3.1-Flag were set as control. At 48 h post transfection (hpt), the cells were lysed and the supernatant was co-incubated with equilibrated anti-Flag-M2 magnetic beads or anti-c-Myc magnetic beads (#88842, Thermo Fisher Scientific), and the subsequent steps were identical to those of endogenous co-IP assay.
Zhang L., Lin J., Weng M., Wen Y., Zhang Y, & Deng W. (2022). RPLP1, an NS4B-interacting protein, enhances production of CSFV through promoting translation of viral genome. Virulence, 13(1), 370-386.
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4

Immunoprecipitation of Integrin Complexes

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HEK293T cells were transfected with the plasmids containing gene of CD81 (#HG14244-CY, Sino Biological), Integrin αV (#27290, Addgene), Integrin β1 (#HG10587-CM, Sino Biological) or Integrin β5 (#HG10779-CM, Sino Biological) using Lipofectamine 2000 according to the manufacture’s manual. Twenty-four hours after transfection, medium was switched to Freestyle 293 expression medium and cells were incubated for 4 hours. Subsequently, cells were harvested in cold PBS and resuspended in cell lysis buffer (50 mM Tris-HCl pH7.5, 150 mM NaCl, 1 mM MgCl2, 0.1 mM CaCl2, 0.5% Brij98) containing phosphatase inhibitors (Roche) and protease inhibitors (Roche). Cell lysates were rotated for 1 hour at 4°C and then supernatants were collected after centrifugation at 17,000 × g for 10 min. The obtained lysates were rotated with protein A/G magnetic beads (Thermo Fisher) for 20 min at 4°C. After centrifugation at 1,000 × g for 2 min, the supernatants were subjected to anti-c-Myc magnetic beads (Thermo Fisher) and rotated overnight at 4°C. After washing in the buffer (50 mM Tris-HCl pH7.5, 150 mM NaCl, 1 mM MgCl2, 0.1 mM CaCl2, 0.5% Brij98) three times, precipitated proteins were eluted by boiling with 1 × Laemmli buffer. Each protein was detected by immunoblotting.
Oguri Y., Shinoda K., Kim H., Alba D.L., Bolus W.R., Wang Q., Brown Z., Pradhan R.N., Tajima K., Yoneshiro T., Ikeda K., Chen Y., Cheang R.T., Tsujino K., Kim C.R., Greiner V.J., Datta R., Yang C., Atabai K., McManus M.T., Koliwad S.K., Spiegelman B.M, & Kajimura S. (2020). CD81 controls beige fat progenitor cell growth and energy balance via FAK signaling. Cell, 182(3), 563-577.e20.
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5

Immunoprecipitation and Western Blotting

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Protein (1 mg) extracts from cells transfected with Flag-Plk1, Myc-NRDC, or Flag-tagged WTPlk3 and Plk3 mutants were subjected to IP with 40 µl of anti-Flag (M2) Magnetic Beads (M8823, Sigma) or anti–c-Myc Magnetic Beads (88842; Thermo Scientific) at 4 °C overnight followed by Western blotting with anti-Plk1 antibody (4513, Cell Signaling Technology), anti-NRDC (A-6) (sc-137199; Santa Cruz Biotechnology), or anti–c-Fos antibody (2250, Cell Signaling Technology).
Fu J., Ling J., Li C.F., Tsai C.L., Yin W., Hou J., Chen P., Cao Y., Kang Y., Sun Y., Xia X., Jiang Z., Furukawa K., Lu Y., Wu M., Huang Q., Yao J., Hawke D.H., Pan B.F., Zhao J., Huang J., Wang H., Bahassi E.I., Stambrook P.J., Huang P., Fleming J.B., Maitra A., Tainer J.A., Hung M.C., Lin C, & Chiao P.J. (2024). Nardilysin-regulated scission mechanism activates polo-like kinase 3 to suppress the development of pancreatic cancer. Nature Communications, 15, 3149.
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6

RIP Assay for YTHDF2 Binding to EBV Genes

Cited 2 times
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RIP was conducted using the Magna RIP kit (Cat #17–700, Millipore) following the manufacturer’s instructions. In brief, Akata (EBV+) cells expressing YTHDF2-Myc or YTHDF2 (K281R/K571R/K572R, RRR)-Myc were treated with IgG cross-linking for 24 h and then lysed using the RIP lysis buffer provided in the kit. A portion of the lysate (10%) was saved as the input sample. The anti-c-Myc magnetic beads (Cat #88842, Thermo Scientific) were washed with RIP buffer and incubated with RNA overnight at 4°C. On the following day, the beads were collected and washed six times with the RIP wash buffer. The enriched RNA-protein complex was digested with proteinase K, and the released RNA was purified using phenol-chloroform extraction. The purified RNA was then subjected to reverse transcription for subsequent qPCR analysis using the primers for ZTA, RTA BALF5, BGLF4, BLLF1, and MALAT1 as we previously described (7 (link), 13 (link))
Sugiokto F.G., Saiada F., Zhang K, & Li R. (2024). SUMOylation of the m6A reader YTHDF2 by PIAS1 promotes viral RNA decay to restrict EBV replication. mBio, 15(2), e03168-23.
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7

RNA Isolation, cDNA Synthesis, and Protein Analysis

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RNA was isolated from tissue samples and IHHs with the RNeasy Lipid Tissue Mini Kit (Qiagen, Hilden, Germany) or the EZNA Total RNA Kit (Omega Bio-Tek, Norcross, GA). cDNA was synthesized using the High-Capacity cDNA Reverse Transcription Kit (Thermo Fisher Scientific). Relative quantification was performed with the QuantStudio 6 Flex Real-Time PCR System (Thermo Fisher Scientific) or the CFX Connect Real-Time System (Bio-Rad, Hercules, CA). The relative quantities of the target transcripts were calculated after normalization of the data to the endogenous control, 18S rRNA (Thermo Fisher Scientific). Co-immunoprecipitation was carried out using anti-MYC antibodies according to the manufacturer's instructions (Anti-c-MYC Magnetic Beads; Thermo Fisher Scientific). Western blot analysis was performed as described previously [31 (link)] (see Supplementary Table S1 for antibody information).
Xia Y., Caputo M., Cansby E., Anand S.K., Sütt S., Henricsson M., Porosk R., Marschall H.U., Blüher M, & Mahlapuu M. (2021). STE20-type kinase TAOK3 regulates hepatic lipid partitioning. Molecular Metabolism, 54, 101353.
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8

RNA Isolation and Protein Interaction

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RNA was isolated from tissue samples and cultured human hepatocytes and the following cDNA synthesis was performed, as described in the Supporting Materials, http://links.lww.com/HC9/A206. Coimmunoprecipitation was carried out using anti-MYC (Anti-c-MYC Magnetic Beads; Thermo Fisher Scientific) or anti-FLAG (Anti-FLAG M2 Magnetic Beads; Sigma-Aldrich) antibodies, according to the manufacturer’s instructions. Western blot analysis was performed as described previously27 (link) (Supplemental Table S1, http://links.lww.com/HC9/A121, for antibody information).
Xia Y., Andersson E., Anand S.K., Cansby E., Caputo M., Kumari S., Porosk R., Kilk K., Nair S., Marschall H.U., Blüher M, & Mahlapuu M. (2023). Silencing of STE20-type kinase TAOK1 confers protection against hepatocellular lipotoxicity through metabolic rewiring. Hepatology Communications, 7(4), e0037.
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