Anti β actin mab

Manufactured by Cell Signaling Technology

Sourced in United States

Anti-β-actin mAb is an immunological reagent used to detect and quantify the expression of the β-actin protein, a widely expressed and abundant cytoskeletal protein found in eukaryotic cells. This monoclonal antibody specifically binds to β-actin, enabling its detection and measurement in various experimental applications.

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Lab products found in correlation

Quantity one software, by Bio-Rad (3 mentions) Cell counting kit 8 (cck8), by Nanjing Jiancheng (1 mentions) Paraquat, by Merck Group (1 mentions) Mitotracker green fm, by Thermo Fisher Scientific (1 mentions) Dulbecco s modified eagle medium dmem, by Thermo Fisher Scientific (1 mentions) Hoechst 33342, by Merck Group (1 mentions) Annexin 5 fitc propidium iodide apoptosis detection kit, by Keygen Biotech (1 mentions) Mdivi 1, by Enzo Life Sciences (1 mentions) Alexa fluor 555 labeled secondary antibody, by Beyotime (1 mentions) Complete protease inhibitor cocktail, by Roche (1 mentions) Fetal calf serum (fcs), by Thermo Fisher Scientific (1 mentions) Chemidoc apparatus, by Bio-Rad (1 mentions) Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (1 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (1 mentions) Doxorubicin, by Merck Group (1 mentions) Dimethyl sulfoxide (dmso), by Fujifilm (1 mentions) Anti jnk pab, by Cell Signaling Technology (1 mentions) Sp600125, by Merck Group (1 mentions) Iblot2 system, by Thermo Fisher Scientific (1 mentions) Hrp conjugated sheep anti mouse igg, by GE Healthcare (1 mentions)

Close spelling variants of this product

Mouse anti-β-actin mAb Anti-β-actin rabbit MAb Anti‐β‐actin (13E5) rabbit mAb β-actin mAb Anti-β-actin β-actin Anti-actin

16 protocols using anti β actin mab

Paraquat-Induced Oxidative Stress Protocols

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Paraquat, 2′, 7′- dichlorodihydrofluorescein diacetate (DCFH-DA), Hoechst 33342 was purchased from Sigma-Aldrich (St Louis, MO, USA). Dulbecco's Modified Eagle Medium (DMEM) used for AT-II cell culture was obtained from Gibco (Carlsbad, CA, USA). Cell counting kit-8 was from Nanjing Jiancheng Bioengineering Institute (Nanjing, China). Annexin V-FITC/propidium iodide (PI) apoptosis detection kit was obtained from Nanjing KeyGen Biotech Co., Ltd. (Nanjing, China). Mitochondrial division inhibitor 1 (Mdivi-1) and anti-Fis1 mAb was purchased from Enzo Life Sciences (Farmingdale, NY, USA). Ascorbic Acid was purchased from Biogot Technology (Nanjing, China). MitoTracker Green FM were provided by Molecular probes (Eugene, OR, USA). Anti-Drp1 mAb, anti-Opa1 mAb, anti-Fis1 mAb, anti-Mfn2 mAb and anti-β-actin mAb used in this study were purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-Cyt C antibody, anti-Cox IV antibody and Alexa Fluor 555 labeled secondary antibody were provided by Beyotime Co., Ltd. (Shanghai, China).

Zhao G., Cao K., Xu C., Sun A., Lu W., Zheng Y., Li H., Hong G., Wu B., Qiu Q, & Lu Z. (2017). Crosstalk between Mitochondrial Fission and Oxidative Stress in Paraquat-Induced Apoptosis in Mouse Alveolar Type II Cells. International Journal of Biological Sciences, 13(7), 888-900.

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Viral Protein Synthesis Regulation

Cited 2 times

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To determine the effect of the drugs on viral protein synthesis, A549 cells were untreated or pretreated with Gem 400 μM and/or Lov 40 μM for 24 h, and infected with SeV and hPIV1 at a MOI of 1 for 24 h. Cells were lysed with Triton-X lysis buffer (20 mM HEPES [pH7.5], 1.5 mM MgCl2, 500 mM NaCl, 0.2 mM EDTA, 1% Triton-X 100 and 20% glycerol), and viral and cellular proteins were analyzed by Western blot analysis using PVDF membranes. Anti-SeV NP (M52, WS16), anti-SeV M (M1), anti-F (M16), anti-hPIV1 NP (P19, P27, P35) mAbs or anti-β-actin mAb (Cell Signaling) were used to detect the proteins (Chambers and Takimoto, 2010 (link); Stone and Takimoto, 2013 (link)). Band intensities were quantitated using BioRad Quantity One software.

Bajimaya S., Hayashi T., Frankl T., Bryk P., Ward B, & Takimoto T. (2016). Cholesterol reducing agents inhibit assembly of type I parainfluenza viruses. Virology, 501, 127-135.

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PD-1 Expression in Activated T Cells

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Sorted mouse T cells were activated and treated with or without DEX (1 × 10⁻⁷ M). After 48 h, cells were collected and lysed in RIPA buffer supplemented with complete protease inhibitor cocktail (Roche, Basel, Switzerland). Protein concentrations were determined using the BCA protein assay kit (Biyotime, Shanghai, China). Cell lysates (20 μg) were separated by SDS-PAGE and transferred into polyvinylidene fluoride (PVDF). The membrane was then blocked with 5 % skim milk in PBST (0.29 % Na₂HPO₄, 0.8 % NaCl, 0.02 % KCl, and 0.05 % Tween-20, pH7.4) for 2 h at room temperature and then incubated with anti-PD-1 mAb (Abcam) at 4°Covernight. After washing three times with PBST, the membrane was incubated with HRP-conjugated secondary antibody (Immunology Consultants Laboratory, Inc.) and detected by enhanced chemiluminescence reagent (Pierce, Rockford, IL, USA). Anti-β-actin mAb (Cell Signaling Technology, USA) was used as internal standard.

Xing K., Gu B., Zhang P, & Wu X. (2015). Dexamethasone enhances programmed cell death 1 (PD-1) expression during T cell activation: an insight into the optimum application of glucocorticoids in anti-cancer therapy. BMC Immunology, 16, 39.

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Investigating ORF6 and NPIPB3 Interaction's Effect on IFN-Stimulated STAT1 Activation

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For testing the effect of ORF6 and NPIPB3 interaction on IFN-stimulated STAT1 activation, lysate from cells expressing single and both of ORF6 and NPIPB3 treated with IFN-β for 15 minutes and 30 minutes was obtained using Western blotting with antiphosphotyrosine STAT1 (Tyr701), and anti-β actin mAb (Cell Signaling Technology). The immune-reactive bands were probed using horseradish peroxidase-conjugated goat antimouse IgG antibodies, and then developed using enhanced chemiluminescence reagents.

Huang S.H., Lee T.Y., Lin Y.J., Wan L., Lai C.H, & Lin C.W. (2015). Phage display technique identifies the interaction of severe acute respiratory syndrome coronavirus open reading frame 6 protein with nuclear pore complex interacting protein NPIPB3 in modulating Type I interferon antagonism. Journal of Microbiology, Immunology, and Infection, 50(3), 277-285.

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Extracellular Vesicle Isolation and Characterization from Transfected 293T Cells

Cited 1 time

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Human embryonic kidney (HEK) 293T cells (ATCC, CRL-11268) were grown in DMEM (Gibco) plus 10% FCS (Gibco). Transfection assays were performed using Lipofectamine 2000 (Invitrogen, Thermo Fisher Scientific)-based method. 293T cells were transfected with vectors expressing either N or Nef^mut/N, and supernatants harvested from 48 to 72 h after transfection. EVs were recovered through differential centrifugations by centrifuging supernatants at 500 × g for 10 min, and then at 10,000 × g for 30 min. Supernatants were harvested, filtered with 0.22 μm pore size filters, and ultracentrifuged at 70,000 × g for l h. Pelleted vesicles were resuspended in 1×PBS, and ultracentrifuged again at 70,000 × g for 1 h. Afterward, pellets containing EVs were resuspended in 1:100 of the initial volume.
Western blot analyses of both cell lysates and EVs were carried out as reported^{11 (link)}, and filters were revealed using 1:2000 diluted anti-flag M2 mAb from Merck (cat. H1029), 1:500-diluted anti-β-actin mAb (cat. 122625, Cell Signaling), 1:500 diluted anti-Alix Abs (PA5-52873 Invitrogen). Filters were analyzed by a Chemi-Doc apparatus (Bio-Rad) and relevant signals quantified by Image Lab software version 6.1.

Manfredi F., Chiozzini C., Ferrantelli F., Leone P., Pugliese K., Spada M., Di Virgilio A., Giovannelli A., Valeri M., Cara A., Michelini Z., Andreotti M, & Federico M. (2023). Antiviral effect of SARS-CoV-2 N-specific CD8+ T cells induced in lungs by engineered extracellular vesicles. NPJ Vaccines, 8, 83.

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Autophagy Induction Assay using DMSO

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Dimethyl sulfoxide (DMSO) was purchased from Wako Pure Chemical Industries Ltd. (Osaka, Japan). Doxorubicin and SP600125 were obtained from Sigma-Aldrich (St. Louis, MO, USA). Hydroxy-α-sanshool and hydroxy-β-sanshool were obtained from Tsumura (Tokyo, Japan). The following antibodies were used for Western blotting analyses: anti-LC3 pAb (PD014), anti-Atg5 mAb (M153-3) (Medical and Biological Laboratories Co. Ltd, Nagoya, Japan), anti-phospho-JNK pAb (Thr183/Tyr185) (#9251S), anti-JNK pAb (#9252S), anti-β-Actin mAb (#4970) (Cell Signaling, Danvers, MA, USA).

Nozaki R., Kono T., Bochimoto H., Watanabe T., Oketani K., Sakamaki Y., Okubo N., Nakagawa K, & Takeda H. (2016). Zanthoxylum fruit extract from Japanese pepper promotes autophagic cell death in cancer cells. Oncotarget, 7(43), 70437-70446.

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EXTL3 Protein Expression Analysis

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Protein lysates were obtained from fibroblasts from a healthy control and P1, P1 cells complemented with a lentivirus (LV) vector expressing wild-type EXTL3 cDNA (P1 LV), and PBMCs from a healthy donor and P3, upon lysing cells in SDS sample buffer. Protein lysates were separated by 4–12% gradient SDS-PAGE, transferred onto nitrocellulose using an iBlot2 system (Thermo Fisher Scientific), and immunoblotted with anti-EXTL3 rabbit polyclonal antibody (Ab113063; Abcam) and anti–β-actin mAb (Cell Signaling Technology), followed by staining with secondary donkey anti–rabbit IgG HRP-conjugated antibody and HRP-conjugated sheep anti–mouse IgG (both from GE Healthcare). The blot was developed with SuperSignal West Femto substrate for EXTL3 and SuperSignal West Dura substrate for β-actin (both from Thermo Fisher Scientific). Bands were visualized using Omega Lum C Imager and software (Aplegen).

Volpi S., Yamazaki Y., Brauer P.M., van Rooijen E., Hayashida A., Slavotinek A., Sun Kuehn H., Di Rocco M., Rivolta C., Bortolomai I., Du L., Felgentreff K., Ott de Bruin L., Hayashida K., Freedman G., Marcovecchio G.E., Capuder K., Rath P., Luche N., Hagedorn E.J., Buoncompagni A., Royer-Bertrand B., Giliani S., Poliani P.L., Imberti L., Dobbs K., Poulain F.E., Martini A., Manis J., Linhardt R.J., Bosticardo M., Rosenzweig S.D., Lee H., Puck J.M., Zúñiga-Pflücker J.C., Zon L., Park P.W., Superti-Furga A, & Notarangelo L.D. (2017). EXTL3 mutations cause skeletal dysplasia, immune deficiency, and developmental delay. The Journal of Experimental Medicine, 214(3), 623-637.

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Evaluating Anti-EGFR Antibody Efficacy

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All animal studies were conducted in accordance with protocols approved by the Animals Ethics Committee of Zhongshan Hospital, Fudan University. Eight-week-old male BALB/c nude mice (20–22 g) were from Charles River (Beijing, China). Anti-EGFR mAb (#ab52894) was from Abcam (Cambridge, UK). Horseradish peroxidase conjugated goat anti-rabbit IgG (H + L) (#GB23303), Cy3-conjugated goat anti-rabbit IgG (H + L) (#GB21303), and DAPI (#G1012) were from Servicebio (Wuhan, China). Anti-β-actin mAb (#4970) was from Cell Signaling Technologies (Boston, MA, USA). Cetuximab (#A2000) was from Selleck (Shanghai, China). Immunoglobulin G-degrading enzyme of Streptococcus pyogenes (IdeS) protease (#20412ES84) was from Yeasen (Shanghai, China).

Shi D., Zhang Y., Xu Z., Si Z., Cheng Y., Cheng D, & Liu G. (2022). Noninvasive Evaluation of EGFR Expression of Digestive Tumors Using 99mTc-MAG3-Cet-F(ab′)2-Based SPECT/CT Imaging. Molecular Imaging, 2022, 3748315.

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Validating Rab8a and Rab11a Knockdown

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To confirm the suppression of Rab8a and Rab11a in cells transfected with pGIP_Z vectors, lysates of HeLa cells were prepared 2 days after transfection using TNE buffer (10 mM Tris [pH 7.4], 150 mM NaCl, 0.5% NP-40, 1 mM EDTA). Proteins in the SDS-PAGE were electrotransferred onto PVDF membranes and probed with anti-Rab8 mAb (Abnova), anti-Rab11 rabbit serum (Invitrogen) or anti-β-actin mAb (Cell Signaling).

Stone R., Hayashi T., Bajimaya S., Hodges E, & Takimoto T. (2015). Critical role of Rab11a-mediated recycling endosomes in the assembly of type I parainfluenza viruses. Virology, 487, 11-18.

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Viral Protein Synthesis Quantification

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To determine viral protein synthesis, infected cells were lysed with TNE buffer and resolved by SDS-PAGE. After transferring to PVDF membranes, blots were reacted with anti-hPIV1 NP mAbs cocktail (P19, P27, P35) or anti-hPIV3 guinea pig serum. For the analysis of HMGCR or SQLE expression, anti-HMGCR (Atlas) or anti-SQLE (Santa Cruz) antibodies were used. For the detection of MX1 and MX2, rabbit anti-MX1 and anti-MX2 polyclonal antibodies were used. Anti-β-actin mAb (Cell Signaling) was used for a loading control. Band intensities were quantitated using BioRad Quantity One software.

Kurebayashi Y., Bajimaya S., Watanabe M., Lim N., Lutz M., Dunagan M, & Takimoto T. (2021). Human parainfluenza virus type 1 regulates cholesterol biosynthesis and establishes quiescent infection in human airway cells. PLoS Pathogens, 17(9), e1009908.

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