Anti e2f1

Manufactured by Merck Group

Sourced in United States

Anti-E2F1 is a laboratory reagent used for research purposes. It is an antibody that binds to and detects the E2F1 protein, which is a transcription factor involved in the regulation of cell cycle and cell proliferation. The anti-E2F1 reagent can be used in various experimental techniques, such as Western blotting, immunoprecipitation, and immunohistochemistry, to study the expression and localization of the E2F1 protein in biological samples.

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Lab products found in correlation

Ez magna chip chromatin immunoprecipitation kit, by Merck Group (1 mentions) Polyvinylidene fluoride membrane, by Merck Group (1 mentions) Ripa buffer, by Beyotime (1 mentions) Anti gapdh, by Merck Group (1 mentions) Anti p62, by Santa Cruz Biotechnology (1 mentions) Anti gfp, by Transgene (1 mentions) Anti ago2, by Abnova (1 mentions) Anti rara, by Santa Cruz Biotechnology (1 mentions) Anti gabarap, by Proteintech (1 mentions) Anti lc3b, by Novus Biologicals (1 mentions) Ez zyme chromatin prep kit, by Merck Group (1 mentions) Anti actin antibody, by Santa Cruz Biotechnology (1 mentions) Anti cyclin a, by Merck Group (1 mentions) Anti irf1 sc 497, by Santa Cruz Biotechnology (1 mentions)

4 protocols using anti e2f1

Chromatin Immunoprecipitation for Transcription Factors

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ChIP assays were performed using the EZ‐Magna ChIP Chromatin Immunoprecipitation Kit (Millipore) according to the instructions of the manufacturer. Briefly, the MKN45 and BGC823 cells were crosslinked with 1% formaldehyde for 10 min at room temperature. After incubation with anti‐E2F1 (Millipore; #2970117), anti‐H3K4me3 (CST, C42D8), or IgG antibody and protein A/G magnetic beads overnight, immunoprecipitation was performed. Proteinase K was used to digest proteins, and chromatin was extracted and then used in PCR and RT‐qPCR analyses.

Lv B., Ma R., Chen X., Zhang G., Song L., Wang S., Wang Y., Liu H, & Gao P. (2020). E2F1‐activated SPIN1 promotes tumor growth via a MDM2‐p21‐E2F1 feedback loop in gastric cancer. Molecular Oncology, 14(10), 2629-2645.

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Western Blot Protein Detection

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Protein extracts were boiled in RIPA buffer (Beyotime, Shanghai, China) and separated in a SDS–polyacrylamide electrophoresis gel. The proteins were then transferred to a polyvinylidene fluoride membrane (Millipore) and probed with anti-RARA (Santa Cruz), anti-AGO2 (Abnova, Taipei, Taiwan), anti-p62 (Santa Cruz), anti-GABARAP (Proteintech, Chicago, IL, USA), anti-GFP (TransGen Biotech), anti-ULK1 (Novus Biologicals, Littleton, CO, USA), anti-LC3B (Novus Biologicals), anti-DRAM2 (Sigma-Aldrich), anti-E2F1 (Millipore) and anti-GAPDH (Sigma-Aldrich) antibodies.

Chen Z.H., Wang W.T., Huang W., Fang K., Sun Y.M., Liu S.R., Luo X.Q, & Chen Y.Q. (2016). The lncRNA HOTAIRM1 regulates the degradation of PML-RARA oncoprotein and myeloid cell differentiation by enhancing the autophagy pathway. Cell Death and Differentiation, 24(2), 212-224.

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Chromatin Immunoprecipitation of E2F1

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ChIP assays were performed using the EZ-Zyme™ Chromatin Prep Kit and EZ-Magna ChIP™ G Chromatin Immunoprecipitation kits (Millipore) according to the manufacturer's standard protocol. ChIP-DNA was quantified using RT-PCR and the enrichment was expressed as fold enrichment compared with IgG. The antibody used was: anti-E2F1 (Millipore). The primers specific for E2F1 binding sites listed in Supplementary Table S1.

Xu J., Fang Y., Wang X., Wang F., Tian Q., Li Y., Xie X., Cheng X, & Lu W. (2016). CUL2 overexpression driven by CUL2/E2F1/miR-424 regulatory loop promotes HPV16 E7 induced cervical carcinogenesis. Oncotarget, 7(21), 31520-31533.

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IRF-1 Immunoprecipitation and Western Blot Analysis

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WCE from MCF7, MCF7/dnIRF-1, MCF7/control, or MCF10A cells were prepared and subjected to Western Blot analysis or immunoprecipitation as previously described [37] . Briefly, 300 μg of WCE were incubated with 1 μg of polyclonal anti-IRF-1 antibody (sc-13041 Santa Cruz Biotechnology Inc., Santa Cruz, CA.) overnight at 4 °C and then Ultralink immobilized protein A/G-Sepharose (Pierce Biotechnology, Rockford, IL) was added for 2 h at room temperature. After extensive washing, immunoprecipitates were eluted by boiling the beads for 3 min in SDS sample buffer and then subjected to Western Blot analysis. IRF-1 and IRF-1 mutated form (IRF-1 3A) were detected by anti-IRF-1 (sc-497 Santa Cruz Biotechnology) antibody; anti-UbK48 Apu2, anti-E2F1 and anti-CyclinA were from Millipore; anti-IKK-ε was from Active Motive; anti-phospho-IKK epsilon (Ser172) antibody were from Cell Signaling Technology; anti-p21, anti-PCNA were from Santa Cruz Biotechnology. Levels of IRF-1, p21, E2F1, Cyclin A and PCNA proteins, relative to levels of endogenous actin protein were quantified using UVP Vision Works LS Image Acquisition software. Anti-actin antibody (Santa Cruz Biotechnology) was used in each experiment as protein loading control; the secondary antibody was from Calbiochem.

Remoli A.L., Sgarbanti M., Perrotti E., Acchioni M., Orsatti R., Acchioni C., Battistini A., Clarke R, & Marsili G. (2020). IκB kinase-ε-mediated phosphorylation triggers IRF-1 degradation in breast cancer cells. Neoplasia (New York, N.Y.), 22(10), 459-469.

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