Briefly, cell lysates were electrophoresed on 12% Tris-glycine gels (Life Technologies, Carlsbad, CA), transferred to a nitrocellulose membrane and blocked overnight in 5% nonfat dry milk in Tris-Buffered Saline and Tween 20 (TBS-T). The membrane was incubated with the primary Ab, rabbit pAb to TREX1 diluted 1:1000 or mouse monoclonal anti-β-actin Ab (Sigma Aldrich, St. Louis, MO) diluted 1:5000 in 5% non-fat dry milk. After washes with TBS-T, the membrane was incubated with the appropriate horseradish peroxidase (HRP)-conjugated secondary Ab followed by additional washes with TBS-T. The Western blots (WB) were developed with West Pico SuperSignal (Thermo Fisher Scientific, Waltham, MA). The protein bands from WB were scanned and quantified using ImageJ (NIH, Bethesda, MD).
Mouse monoclonal anti β actin ab
Manufactured by Merck Group
Sourced in United States
The mouse monoclonal anti-β-actin antibody is a laboratory reagent used for the detection and quantification of β-actin, a ubiquitous cytoskeletal protein, in various biological samples. This antibody can be employed in a range of immunoassay techniques, including Western blotting, immunohistochemistry, and flow cytometry, to facilitate the analysis of cellular protein expression.
Automatically generated - may contain errors
Lab products found in correlation
Supersignal west pico, by Thermo Fisher Scientific (2 mentions)
Tris glycine gel, by Thermo Fisher Scientific (2 mentions)
Ab87811, by Abcam (1 mentions)
Poly 1 c, by InvivoGen (1 mentions)
Hrp conjugated secondary antibody, by Merck Group (1 mentions)
Z vad fmk, by Merck Group (1 mentions)
Mg132, by Merck Group (1 mentions)
Recombinant human tgf β1, by Thermo Fisher Scientific (1 mentions)
6 well plate, by Iwaki (1 mentions)
Unc0379, by Cayman Chemical (1 mentions)
Tgf β1, by Abcam (1 mentions)
X ray film, by Fujifilm (1 mentions)
7 protocols using mouse monoclonal anti β actin ab
1
Western Blot Quantification of TREX1
2
Immunoblotting for Chromatin Proteins
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The following antibodies were used: a mouse monoclonal Ab anti-EZH2 (clone 144CT2.1.1.5) (Thermo Fisher Scientific, Rockford, USA) (1:250), a rabbit Polyclonal anti-DAB2IP Ab (ab87811, Abcam, Cambridge, UK) (1:500), a rabbit polyclonal anti-H3K27me3Ab (Millipore, CA, USA)(1:250), a mouse monoclonal anti-β-Actin Ab (Sigma, St. Louis, MO) (1:20,000), and a mouse Monoclonal anti-Vimentin Ab (Clone Vim 3B4, Dakocytomation) (1:100).
3
Western Blot Analysis of TREX1
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Briefly, cell lysates were electrophoresed on 12% Tris‐glycine gels (Life Technologies, Carlsbad, CA), transferred to a nitrocellulose membrane and blocked overnight in 5% non‐fat dry milk in Tris‐Buffered Saline and Tween 20 (TBS‐T). The membrane was incubated with the primary Ab, rabbit pAb to TREX1 diluted 1:1000 or mouse monoclonal anti‐β‐actin Ab (Sigma Aldrich, St. Louis, MO) diluted 1:5000 in 5% non‐fat dry milk. After washes with TBS‐T, the membrane was incubated with the appropriate horseradish peroxidase (HRP)‐conjugated secondary Ab followed by additional washes with TBS‐T. The Western blots (WB) were developed with West Pico SuperSignal (Thermo Fisher Scientific, Waltham, MA). The protein bands from WB were scanned and quantified using ImageJ (NIH, Bethesda, MD).
4
Immunoblot Analysis of Signaling Proteins
5
Antibody Detection in Cellular Samples
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The following antibodies were used: rabbit anti-human TSLP (ProSci, Ca, USA) diluted to a ratio of 1:100, rabbit polyclonal anti-human IKKα Ab, clone 14A23 (Millipore, Ca, USA) diluted to 1:100; mouse monoclonal anti-human Ac-His H3 (Lys14) Ab, clone 13HH3-1A5 (Millipore, Ca, USA) diluted to 1:100; and mouse monoclonal anti-β-actin Ab (Sigma, St. Louis, MO, USA) diluted to 1:20,000.
6
Western Blot Analysis of LEF1, CYGB, and β-Actin
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Cell lysates were prepared with RIPA buffer and subjected to western blot analysis using a rabbit anti‐LEF1 polyclonal antibody (Ab; Cell Signaling Technology, Danvers, MA, USA), a rabbit anti‐CYGB polyclonal Ab (Thermo Fisher Scientific), and a mouse anti‐β‐actin monoclonal Ab (Sigma Aldrich, St Louis, MO, USA).
7
TGF-β1 and UNC0379 Influence on Cellular Markers
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The cells were plated in 6-well plates (IWAKI) and maintained in DMEM containing 15% FBS overnight. After adding fresh medium, the cells (6 × 105 cells/well) were treated with 10 ng/ml human recombinant TGF-β1 (PeproTech, Rocky Hill, NJ, United States), 10 μM UNC0379 (Cayman Chemical, Ann Arbor, MI, United States) or TGF-β1 plus UNC0379 for 48 h. The cells were then lysed and subjected to WB with mouse anti-α-SMA monoclonal antibody (Ab) (ab7817; Abcam, Cambridge, United Kingdom), mouse anti-ED-A-FN monoclonal Ab (sc-59825, clone IST-9, ED-A domain-specific; Santa Cruz Biotechnology, Dallas, TX, United States), rabbit anti-SET8 monoclonal Ab (#2996; Cell Signaling Technology, Danvers, MA), mouse anti-H4K20me1 monoclonal Ab (C15200147; Diagenode, Liege, Belgium), or mouse anti-β-actin monoclonal Ab (A5441, clone AC-15; Sigma-Aldrich, St. Louis, MO, United States) (1:1000 dilution) followed by incubation with horseradish peroxidase-conjugated anti-mouse or anti-rabbit IgG (1:2000 dilution). The blot was exposed to an X-ray film (FUJIFILM, Tokyo, Japan) to visualize the immunoreactive signals detected by chemiluminescence. The intensity of the signals on the developed X-ray films was quantified using the ImageJ software (National Institutes of Health, Bethesda, MD, United States).
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