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Anti β actin ba3r

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The Anti-β–actin BA3R is a laboratory reagent used for the detection and quantification of the β-actin protein in biological samples. It is a primary antibody that specifically binds to the β-actin protein, allowing its identification and measurement in various experimental procedures.

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Lab products found in correlation

Iblot, by Thermo Fisher Scientific (1 mentions) Lds sample buffer, by Thermo Fisher Scientific (1 mentions) Anti α tubulin ebiop4d1, by Thermo Fisher Scientific (1 mentions) Protease inhibitor, by Cell Signaling Technology (1 mentions) Bis tris gel, by Thermo Fisher Scientific (1 mentions) Cell lysis buffer, by Cell Signaling Technology (1 mentions) Anti caspase 1, by Cell Signaling Technology (1 mentions) Enhanced chemi luminescence (ecl), by GE Healthcare (1 mentions) Chemidoc xr, by Bio-Rad (1 mentions) Anti p53 fl393, by Santa Cruz Biotechnology (1 mentions) Tris glycin 4 20 gradient gels, by Thermo Fisher Scientific (1 mentions) Enhanced chemi luminescence (ecl), by Thermo Fisher Scientific (1 mentions) Anti hsp90, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

β-actin (705 citations) Anti-β-actin (136 citations) Anti-actin (52 citations) β ACTIN (BA3R; (8 citations)

5 protocols using anti β actin ba3r

1

Western Blot Protocol for Vitamin D Metabolism

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Cells were lysed using RIPA buffer. Samples were mixed with LDS sample buffer (Thermo Scientific) and run on a 10% NuPAGE Tris-Acetate gel (Thermo Scientific). Proteins were transferred using the iBlot (Thermo Fisher) transfer apparatus to nitrocellulose membranes. Membranes were blocked in 5% milk in Tris-buffered saline with Tween 20 (TBS-T) and incubated with either anti-Cyp2R1 (Abcam Inc., Boston, MA), anti-Cyp27A1 EPR7529 (Abcam), anti-Cyp27B1 H-90 (Santa Cruz Biotechnology) or anti-β–actin BA3R (Thermo Fisher) overnight and bands were visualized by chemiluminescence. Densiometric analysis of the bands was performed using ImageJ software.
DiFranco K.M., Mulligan J.K., Sumal A.S, & Diamond G. (2017). Induction of CFTR gene expression by 1,25(OH)2 vitamin D3, 25OH vitamin D3, and vitamin D3 in cultured human airway epithelial cells and in mouse airways. The Journal of steroid biochemistry and molecular biology, 173, 323-332.
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2

Quantification of XBP1s Activation

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Splenic CD4+ T cells isolated from the asthmatic HFD and ND mice were lysed immediately, and subjected for immunoblot of XBP1s. In vitro differentiated TH2 cells were starved for 24 h in serum free medium and then be subjected to different treatments as indicated and cell lysates were prepared for immunoblot analysis of XBP1s. Immunoblot antibodies were anti-XBP1 (M186, sc-7160, Santa Cruz Biotechnology), anti-α-Tubulin (eBioP4D1, eBioscience), anti-β-Actin (BA3R, Thermo Fisher Scientific), anti-IRE1 (B-12, sc-390960, Santa Cruz Biotechnology), anti-phospho-IRE1 (ab48187, Abcam), and anti-ATF6 (F-7, sc-166659, Santa Cruz Biotechnology).
Zheng H., Wu D., Wu X., Zhang X., Zhou Q., Luo Y., Yang X., Chock C.J., Liu M, & Yang X.O. (2018). Leptin Promotes Allergic Airway Inflammation through Targeting the Unfolded Protein Response Pathway. Scientific Reports, 8, 8905.
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3

Analyzing Caspase-1 and IFI16 Activation

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Unless otherwise stated, THP-1 cells were stimulated with PMA (5 ng/mL) and then with IFNγ (25 ng/mL) the following day for 24 hours prior to stimulation. Cells were lysed on ice using Cell Lysis Buffer (Cell Signaling Technologies, Danvers, MA) supplemented with protease inhibitors (1:100, Cell Signaling Technologies, cat# 5872) and stored at -80°C for western blot analysis. Lysates were run on 4–12% BIS-TRIS gels (ThermoFisher, Waltham, MA) in reducing conditions before transfer to nitrocellulose membranes. Blots were blocked and then incubated overnight with anti-caspase-1 (polyclonal, Cell Signaling technologies), anti-β-actin (BA3R, ThermoFisher), or anti-IFI16 (D8B5T, Cell Signaling Technologies) antibodies as indicated, washed, incubated with an appropriate secondary antibody, developed with ECL (GE, Marlborough, MA), and imaged on a BioRad ChemiDoc XRS+.
Karaba A.H., Figueroa A., Massaccesi G., Botto S., DeFilippis V.R, & Cox A.L. (2020). Herpes simplex virus type 1 inflammasome activation in proinflammatory human macrophages is dependent on NLRP3, ASC, and caspase-1. PLoS ONE, 15(2), e0229570.
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4

Immunoblot and Co-immunoprecipitation Analysis

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Whole-cell lysates were subjected to immunoblot analysis using a standard protocol. The antibodies were as follows: anti-Lum (AF2745; RnD systems) and anti-β-Actin (BA3R; MA5-15739; Thermo Fisher Scientific). For co-immunoprecipitations of Lum to FasL or FasL to Lum, we incubated protein A/G magnetic beads with 2 μg of anti-Lum or anti-FasL (MFL3, eBioscience) antibody or isotype control for 4 hours at 4°C. The bead-antibody complexes were washed with cold PBS and then incubated with whole-cell lysates for overnight at 4°C. Following washes with lysis buffer and cold PBS, the bead-immune complexes were then resuspended in Laemmli's sample buffer and boiled for 5 minutes. Samples were then prepared for immuoblot analysis.
Castillo E.F., Zheng H., Van Cabanlong C., Dong F., Luo Y., Yang Y., Liu M., Kao W.W, & Yang X.O. (2016). Lumican negatively controls the pathogenicity of murine encephalitic TH17 cells. European journal of immunology, 46(12), 2852-2861.
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5

Western Blot Analysis of Cellular Proteins

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Cell lysates were separated by electrophoresis on precast Tris-Glycin 4–20% gradient gels (Invitrogen) and transferred to the Protran nitrocellulose membrane (VWR, Chicago, IL). The membranes were incubated with an anti-p53 [FL-393] (Santa Cruz Biotechnology, Santa Cruz, CA), anti-HSP90 (Cell Signaling, Boston, MA), anti-Galectin-1 [EPR3205] (Abcam, Cambridge, MA) and anti-β actin [BA3R] (Thermo). The blots were washed, incubated with appropriate secondary antibody, and developed using enhanced chemiluminescence reagents (ECL; Thermo Fisher).
Gurel Z., Zaro B.W., Pratt M.R, & Sheibani N. (2014). Identification of O-GlcNAc Modification Targets in Mouse Retinal Pericytes: Implication of p53 in Pathogenesis of Diabetic Retinopathy. PLoS ONE, 9(5), e95561.
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