Agarose beads

Manufactured by Cell Signaling Technology

Agarose beads are a type of gel matrix commonly used in various laboratory techniques. They are made from the polysaccharide agarose, which is extracted from red seaweed. Agarose beads have a porous structure that allows for the separation and purification of biomolecules, such as proteins and nucleic acids, based on their size and charge.

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Lab products found in correlation

Protein a agarose beads, by Cell Signaling Technology (2 mentions) Np 40 buffer, by Beyotime (1 mentions) Phosphatase inhibitor, by Merck Group (1 mentions) Chemidoc xr, by Bio-Rad (1 mentions) Protein a g plus agarose bead, by Santa Cruz Biotechnology (1 mentions) Image lab, by Bio-Rad (1 mentions) Mini protean tgx gel, by Bio-Rad (1 mentions) Hdac3 antibody, by Cell Signaling Technology (1 mentions) Cdc20, by Merck Group (1 mentions) Mda mb 231, by American Type Culture Collection (1 mentions) U2os cell, by American Type Culture Collection (1 mentions) Mcf 7, by American Type Culture Collection (1 mentions) Cyclin b, by Merck Group (1 mentions) Sirt1, by Cell Signaling Technology (1 mentions) Anti acetylated lysine antibody, by Cell Signaling Technology (1 mentions) Protein a g agarose bead, by Roche (1 mentions) Hmgb1, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

Protein A agarose beads (65 citations) Protein G agarose beads (39 citations) Protein A/G agarose beads (21 citations) Protein A/G PLUS-Agarose beads (7 citations) SimpleChIP® Enzymatic Chromatin IP Kit (Agarose Beads) (6 citations) ChIP-Grade Protein G Agarose Beads (4 citations) SimpleChIP Enzymatic Chromatin IP Kit with Agarose Beads (3 citations) ChIP-grade agarose beads with protein G (2 citations)

6 protocols using agarose beads

Immunoprecipitation of Bad Protein

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Ovarian cells were lysed by using NP-40 buffer (Beyotime Biotechnology, Shanghai, China) on ice for 30 min, followed by collection of the supernatants. Subsequently, a primary antibody against Bad was added to the supernatants and incubated overnight at 4°C. Protein A agarose beads (Cell Signaling Technology) were added to the supernatants and incubated for 2 h. The proteins binding to the agarose beads were separated by boiling in SDS sample buffer and detected by Western blot analysis.

Yang S., Li Z, & Luo R. (2020). miR-34c Targets MET to Improve the Anti-Tumor Effect of Cisplatin on Ovarian Cancer. OncoTargets and therapy, 13, 2887-2897.

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p53 Acetylation Immunoprecipitation

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The RAW264.7 cell lysates were immunoprecipitated with 1 μg of anti-p53 antibody overnight at 4 °C, and 30 μL protein A agarose beads (Cell Signaling Technology) was added to the mixture and incubated at 4 °C for 4 h. The agarose beads were collected by centrifugation at 12,000 × g for 60 s at 4 °C and washed 3 times with a lysis buffer. The acetylation level of the p53 was analyzed with western blotting using anti-acetylated-lysine antibody. Immunoprecipitation with mouse IgG was taken as negative control.

Gong L., Shen Y., Wang S., Wang X., Ji H., Wu X., Hu L, & Zhu L. (2023). Nuclear SPHK2/S1P induces oxidative stress and NLRP3 inflammasome activation via promoting p53 acetylation in lipopolysaccharide-induced acute lung injury. Cell Death Discovery, 9, 12.

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Chromatin Immunoprecipitation Assay for OsWRKY7-HA

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The chromatin immunoprecipitation (ChIP) assay was performed using the protocols described in Haring et al. (2007) (link) and Yoon et al. (2022) (link) with some modifications. Firstly, the fresh leaves from the OsWRKY7-HA transgenic plants were collected and the proteins and chromatin were cross-linked using 3% formaldehyde. After the isolation of nuclei, DNA was broken into fragments of approximately 200–800 bp in length by sonication. agarose beads of G and A proteins (Milipore; http://www.emdmilipore.com) were used to preclear the sheared chromatin for 1 hour at 4°C. Anti-HA monoclonal antibody (C29F4, https://www.cellsignal.com) was used for immunoprecipitation together with the precleared agarose beads for 4 hours at 4°C. The washing and reverse cross-linking steps described in Haring et al. (2007) (link) were followed. The enriched chromatin was analyzed by qRT-PCR using the primers listed in Supplementary Table 1. The obtained data were normalized using the fold enrichment method (Haring et al., 2007 (link); Yoon et al., 2022 (link)).

Tun W., Yoon J., Vo K.T., Cho L.H., Hoang T.V., Peng X., Kim E.J., Win K.T., Lee S.W., Jung K.H., Jeon J.S, & An G. (2023). Sucrose preferentially promotes expression of OsWRKY7 and OsPR10a to enhance defense response to blast fungus in rice. Frontiers in Plant Science, 14, 1117023.

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HDAC3 Interaction Assay in Cardiomyocytes

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Cultured NRVM were infected with GFP-CapZβ1 adenovirus. After 24 h of infection, cells were washed twice in ice-cold PBS and lysed in RIPA buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 2 mM EDTA, 1% NP40, 0.1% SDS) plus phosphatase inhibitors (Sigma Aldrich, #P5726, P0044) for 1 h at 4 °C under constant agitation. Following protein extraction, protein lysates were precleared using 25 μL Protein A/G Plus -Agarose beads (Santa Cruz, #sc-2003) for 1 h at 4 °C. Precleared lysates were incubated 24 h with 2 μg of HDAC3 antibody (Cell Signaling Technology; 4668) at 4 °C, then immunocomplexes were isolated by adding Protein A/G Plus -Agarose beads overnight at 4 °C. Beads were washed three times in the binding buffer. SDS-PAGE and Western blotting were performed using 12% Mini-PROTEAN® TGX^™ Gel (Bio-Rad Laboratories, #456-1044). Polyvinylidene difluoride (PVDF) membranes were incubated with GFP primary antibody (Enzo Life Sciences, ADI-SAB-500), followed by horseradish peroxidase (HRP) secondary antibody (anti-mouse) for 1 h at room temperature. Proteins were finally treated with an ECL Plus kit and visualized with the aid of ChemiDoc XRS+ and analyzed with Image Lab (Bio-Rad Laboratories).

Lin Y.H., Warren C.M., Li J., McKinsey T.A, & Russell B. (2016). Myofibril growth during cardiac hypertrophy is regulated through dual phosphorylation and acetylation of the actin capping protein CapZ. Cellular signalling, 28(8), 1015-1024.

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Cell Line Maintenance and Immunodetection

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MCF-7, U2OS, and MDA-MB-231 cells were purchased from ATCC. The MDA-MB-435 cells were kindly shared by Dr. Dinghua Yu at the University of Texas, TX. The Flag-Cdc20 MDA-MB-231 stable cells were prepared by our lab member Dr. Cindy Mandy Wavelet. The 22Rv1, and LNCaP cells were kindly shared by Dr. Jingdan Yu at Northwestern University. MCF-7, MDA-MB-231 cells were cultured in Dulbecco's Modified Eagle Medium (DMEM) supplemented with 10% fetal bovine serum (FBS) and 1% penicillin-streptomycin. Flag-Cdc20 MDA-MB-231 cells were cultured in complete DMEM introduced before with 1 μg/ ml tamoxifen. Following ATCC instruction, the U2OS cells were cultured in McCoy's 5A Medium with 10% FBS and 1% antibiotics. 22Rv1 and LNCaP cells were cultured in RPMI-1640 Medium. The Cdc20, cyclin B and actin antibodies were purchased from Sigma. The actin antibodies were diluted 1:5000. The Cdc20, cyclin B and ubiquitin antibodies were diluted 1:1000. The agarose beads were purchased from Cell Signaling Technology.

Chi J.(., Li H., Zhou Z., Izquierdo-Ferrer J., Xue Y., Wavelet C.M., Schiltz G.E., Zhang B., Cristofanilli M., Lu X., Bahar I, & Wan Y. (2019). A novel strategy to block mitotic progression for targeted therapy. EBioMedicine, 49, 40-54.

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Immunoprecipitation and Acetylation Analysis

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Brain tissue from lesioned cortices were incubated with 1 μg of SIRT1 (Cell Signaling Technology) or HMGB1 anti-acetylated lysine antibody (Cell Signaling Technology) for 2 h at 4 °C. A 10-μl volume of protein A/G agarose beads (Roche, Mannheim, Germany) was added to the samples and incubated overnight. After immunoprecipitation and centrifugation, agarose beads were washed three times with lysis buffer, and the degree of acetylation of SIRT1 or HMGB1 was analyzed by western blotting using an anti-acetylated lysine antibody (Cell Signaling Technology).

Chen X., Chen C., Fan S., Wu S., Yang F., Fang Z., Fu H, & Li Y. (2018). Omega-3 polyunsaturated fatty acid attenuates the inflammatory response by modulating microglia polarization through SIRT1-mediated deacetylation of the HMGB1/NF-κB pathway following experimental traumatic brain injury. Journal of Neuroinflammation, 15, 116.

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