Protein a g agarose

Manufactured by GenDEPOT

Protein A/G-Agarose is a solid-phase support matrix used for the purification of immunoglobulins and other proteins that bind to Protein A or Protein G. It consists of purified Protein A and Protein G covalently coupled to crosslinked agarose beads.

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Lab products found in correlation

H 125, by Santa Cruz Biotechnology (1 mentions) Anti srf antibody, by Cell Signaling Technology (1 mentions) Anti tead4 antibody, by Abcam (1 mentions) Ne per nuclear and cytoplasmic protein extraction kit, by Thermo Fisher Scientific (1 mentions) Epiquik in vivo universal protein sumoylation assay kit, by Epigentek (1 mentions) Dynabeads protein a beads, by Thermo Fisher Scientific (1 mentions)

3 protocols using protein a g agarose

Chromatin Immunoprecipitation (ChIP) Assay

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DNA in cells from two confluent 100-mm culture dishes (∼2 × 10⁷ cells total) was pretreated with 1.5 mM ethylene glycol bis(succinimidylsuccinate) (Sigma) for 30 min at room temperature to capture proteins indirectly bound to DNA, and then crosslinked by incubating with 1% formaldehyde for 15 min. After DNA crosslinking, cells were sonicated by Bioruptor (BMS Co.) in SDS lysis buffer (50 mM Tris-Cl pH 8.0, 1% SDS and 10 mM EDTA) and diluted 10-fold with dilution buffer (16.7 mM Tris-Cl pH 8.0, 167 mM NaCl, 1.1% Triton X-100 and 1.2 mM EDTA) and processed for ChIP assays using 2 μg of anti-YAP antibody (H-125, Santa Cruz Biotechnology), anti-TEAD4 antibody (Abcam) or anti-SRF antibody (Cell Signaling) and Protein A/G agarose (GenDEPOT). YAP 5SA is used for maximal efficiency in YAP binding to the chromatin. See Supplementary Table 1 for primers used.

Kim T., Yang S.J., Hwang D., Song J., Kim M., Kyum Kim S., Kang K., Ahn J., Lee D., Kim M.Y., Kim S., Seung Koo J., Seok Koh S., Kim S.Y, & Lim D.S. (2015). A basal-like breast cancer-specific role for SRF–IL6 in YAP-induced cancer stemness. Nature Communications, 6, 10186.

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STAT3-Mediated EGFR Regulation in Mammospheres

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Proteins extracts of mammospheres treated with DMSO as a control or dihydroconiferyl ferulate (50 μM) were prepared in lysis buffer (20 mM Hepes, 10 mM EGTA, 40 mM glycerol 2-phosphate, 2.5 mM MgCl₂ 6H₂O, 1% NP-40, pH 7.5). IP was performed using 1 μg of Stat3 antibody (sc-482) and 500 μg of protein. Protein A/G-Agarose (P9203-100, GenDEPOT) was used to precipitate the protein complex, which was then analyzed using SDS-PAGE, followed by immunoblotting with the EGFR antibody (#4267s).

Ko Y.C., Liu R., Sun H.N., Yun B.S., Choi H.S, & Lee D.S. (2022). Dihydroconiferyl Ferulate Isolated from Dendropanax morbiferus H.Lév. Suppresses Stemness of Breast Cancer Cells via Nuclear EGFR/c-Myc Signaling. Pharmaceuticals, 15(6), 664.

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In Vitro Sumoylation of Menin

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We performed an in vitro SUMOylation assay with endogenously-expressed or overexpressed proteins. Briefly, HEK 293T cells were transfected with pcDNA3.1-Xpress-MEN1 (WT or Y603F, Y603D, K493R, K609R mutants) and pcDNA3-HA-SUMO-1 using iMFectin. 24 h after transfection, cells were lysed in NP-40 buffer. SUMOylated-Menin proteins were immunoprecipitated with Dynabeads^™ Protein A beads (Invitrogen) coupled to Xpress tags or Protein A/G-Agarose (GenDEPOT) coupled to a Menin antibody and visualized with HA or SUMO1 antibodies. In other experiments we also pulldown Dynabeads^™ Protein A beads (Invitrogen) coupled to HA or Menin antibody and visualized Menin-SUMOylation by blotting against Xpress and HA respectively. We analyzed SUMOylation of Menin by using the EpiQuik^™ In Vivo Universal Protein Sumoylation Assay Kit (EPIGENTEK). Briefly, nuclear lysates from mESCs were prepared using the NE-PER cytoplasmic and nuclear protein extraction kit (ThermoFisher Scientific). SUMOylated proteins were pulldown using Dynabeads^™ Protein A beads and 10 μg of pulldown protein was used for the assay. SUMOylation intensity was calculated against a standard curve prepared from recombinant SUMO protein according to the manufacturer’s protocol.

Paul S., McCourt P.M., Le L.T., Ryu J., Czaja W., Bode A.M., Contreras-Galindo R, & Dong Z. (2024). Fyn-mediated phosphorylation of Menin disrupts telomere maintenance in stem cells. bioRxiv.

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