Anti β actin 13e5 rabbit mab

Manufactured by Cell Signaling Technology

Sourced in United Kingdom

Anti-β-actin (13E5) rabbit mAb is an antibody product that detects β-actin protein. It is a monoclonal antibody derived from rabbit. The core function of this product is to be used as a detection reagent for the identification and quantification of β-actin in various sample types.

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Lab products found in correlation

Compound c, by Selleck Chemicals (1 mentions) 2 deoxyglucose 2 dg, by Merck Group (1 mentions) Anti pim1, by Abcam (1 mentions) A769662, by Selleck Chemicals (1 mentions) Sc 21757, by Santa Cruz Biotechnology (1 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Es936, by Bio-Techne (1 mentions) Alexa fluor 488 goat anti rabbit igg, by Thermo Fisher Scientific (1 mentions) Bafilomycin a1, by Merck Group (1 mentions) Polyvinylidene fluoride (pvdf), by Bio-Rad (1 mentions) Anti egf receptor d38b1 xp rabbit mab, by Cell Signaling Technology (1 mentions) Ecl prime western blot detection system, by GE Healthcare (1 mentions) Ab205722, by Abcam (1 mentions) Mini protean tgx gel, by Bio-Rad (1 mentions) Trans blot turbo transfer pack membranes, by Bio-Rad (1 mentions) Imagequant tl software, by GE Healthcare (1 mentions)

Spelling variants of this product

Anti-β-actin (1878 citations) Rabbit anti-β-actin (244 citations) β-actin (13E5) (77 citations) β-actin rabbit mAb (29 citations) β-actin (13E5) rabbit mAb (22 citations) Anti-β-actin (13E5) (19 citations) Anti-β-actin mAb (16 citations) Anti-β-actin rabbit MAb (6 citations) Rabbit anti-β-actin (13E5) (5 citations) β-actin mAb (5 citations)

6 protocols using anti β actin 13e5 rabbit mab

Western Blot Antibodies and Inhibitors

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The following antibodies were used in this study: anti‐Pim1 (Abcam, Cambridge, UK); anti‐β‐actin (13E5) rabbit mAb (4970; Cell Signaling Technology, Danvers, MA, USA); anti‐AMPKα (D63G4) rabbit mAb (5832S; Cell Signaling Technology); anti‐phospho‐AMPKα (Thr172) (40H9) rabbit mAb (2535S; Cell Signaling Technology); anti‐LDHA (C4B5) rabbit mAb (3582; Cell Signaling Technology); and anti‐HK2 (C64G5) rabbit mAb (2867; Cell Signaling Technology).
Pim1 siRNAs (si1: sense 5′‐GGAACAACAUUUACAACUCdTdT‐3′, antisense 5′‐GAGUUGUAAAUGUUGUUCCdTdT‐3′; si2: sense 5′‐GAUAUGGUGUGUGGAGAUA‐3′, antisense 5′‐ UAU‐CUCCACACACCAUAUC‐3′), and a negative control siRNA (Scramble: sense 5′‐CUUACGCUGAGUACUUCGAdTdT‐3′, antisense 5′‐ UCGAAGUACUCAGCGUAAGdTdT‐3′) were purchased from GenePharma (Shanghai, China). 2‐Deoxyglucose (2‐DG, Sigma Chemical Co., St Louis, MO, USA), A769662 and Compound C (Selleck Chemicals, Houston, TX, USA) were added to the medium as indicated.

Zhang M., Liu T., Sun H., Weng W., Zhang Q., Liu C., Han Y, & Sheng W. (2018). Pim1 supports human colorectal cancer growth during glucose deprivation by enhancing the Warburg effect. Cancer Science, 109(5), 1468-1479.

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Quantitative Western Blot Analysis

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A Western blotting analysis was performed on 30 μg of whole-cell protein from liver tissues. After non-specific binding was blocked, the primary antibodies, anti-HO-1 (ab82585, Abcam, Cambridge, UK) and anti-β-actin (13E5) rabbit mAb (Cell Signaling Technology Inc., Danvers, MA, USA), were incubated. Thereafter, the proteins were visualized and analyzed using β-actin as the protein loading control.

Uto K., Sakamoto S., Que W., Shimata K., Hashimoto S., Sakisaka M., Narita Y., Yoshii D., Zhong L., Komohara Y., Li X.K., Inomata Y, & Hibi T. (2019). Hydrogen-rich solution attenuates cold ischemia-reperfusion injury in rat liver transplantation. BMC Gastroenterology, 19, 25.

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Western Blot Analysis of β-Globin

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The accumulation of the β-globin protein (16 kDa) was assessed by western blotting. For whole-cell extract preparation, the cells were lysed through three freeze-thaw cycles in dry ice and quantified by BCA assay (Pierce BCA Protein Assay Kit; Thermo Fisher Scientific). For each sample, 20 μg of ErPCs extracts was loaded on a 16% acrylamide SDS-PAGE gel (40% acrylamide/bis solution; Bio-Rad). After separation by an electrophoretic run, the proteins were transferred onto nitrocellulose paper and incubated with different primary antibodies: anti-β-globin chain antibody (monoclonal antibody [mAb], sc-21757; Santa Cruz), anti-α-globin chain antibody (mAb, TA307691; OriGene), and anti-β-actin (13E5 rabbit mAb; Cell Signaling Technology), a constitutive protein (45 kDa) expressed similarly in all treated and untreated samples, used as housekeeping to normalize the quantification of the target protein.

Cosenza L.C., Gasparello J., Romanini N., Zurlo M., Zuccato C., Gambari R, & Finotti A. (2021). Efficient CRISPR-Cas9-based genome editing of β-globin gene on erythroid cells from homozygous β039-thalassemia patients. Molecular Therapy. Methods & Clinical Development, 21, 507-523.

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Immunoblotting and Immunofluorescence Assay

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The following Abs were used: mouse anti-NQO1 monoclonal Ab (mAb) (39–3700, Invitrogen), rabbit anti-LC3 polyclonal Ab (pAb, PM036, MBL International Corp.), anti- β-Actin (13E5) rabbit mAb (4970, Cell Signaling), peroxidase-conjugated- goat anti-mouse IgG(H + L) and mouse anti-rabbit IgG(H + L) (115-035-062, 211-035-109; Jackson ImmunoResearch Labs) and alexa fluor-488 goat anti-rabbit IgG (A11008, Invitrogen). Dicoumarol (287897) was from Calbiochem and rapamycin (tlrl-rap) from Invitrogen. ES936 (4022) was purchased from Tocris Bioscience. Nitazoxanide (NTZ, 2-acetyloxy-N-(5-nitro-2-thiazolyl)benzamide) and its active metabolite tizoxanide (TIZ) were kindly provided by Eli Lilly. Dimethyl sulfoxide (DMSO; W387509) and N,N-Dimethylformamide (DMF; 227056), used to dilute small molecule inhibitors and used in cell culture (0.05%) as solvent controls, were purchased from Sigma-Aldrich. All drugs were aliquoted and kept at −80 °C until use. Bafilomycin A1, (B1793) was obtained from Sigma-Aldrich. 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT; M-6494) was purchased from Life Technologies, Thermo Fisher Scientific.

Li Q., Karim A.F., Ding X., Das B., Dobrowolski C., Gibson R.M., Quiñones-Mateu M.E., Karn J, & Rojas R.E. (2016). Novel high throughput pooled shRNA screening identifies NQO1 as a potential drug target for host directed therapy for tuberculosis. Scientific Reports, 6, 27566.

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Western Blot Analysis of Immune Signaling Proteins

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The cells were washed with PBS and scraped using a cell scraper. The cells were transferred to 1.5 mL microtubes and centrifuged at 5000 g for 3 min. Cells were lysed in 100 μL of lysis buffer (50 mM Tris–HCl, pH 6.8, 2% SDS, 6% 2‐mercaptoethanol, 10% glycerol, 0.0125% bromothymol blue) and heated at 95°C for 5 min. Whole cell extracts were subjected to electrophoresis on 4%–20% Mini PROTEAN TGX gels (Bio‐Rad, 4561095) and then transferred to Trans‐Blot Turbo Transfer Pack membranes (0.2 μM PVDF, BIO‐RAD, 1704156). Membranes were blocked with 5% BSA in Tris‐Buffered Saline‐Tween, TBST 0.001% azide for 60 min and probed with primary anti‐STING (D2P2F) rabbit mAb (#13647, Cell Signaling Technology), anti‐cGAS (D1D3G) rabbit mAb (#15102, Cell Signaling Technology), anti‐EGF‐Receptor (D38B1) XP rabbit mAb (#4267), and anti‐β‐actin (13E5) rabbit mAb (#4970, Cell Signaling Technology). The membranes were then washed with TBST and incubated with a secondary donkey anti‐rabbit immunoglobulin antibody conjugated to horseradish peroxidase (HRP) (Abcam, ab205722) for 1 h. Proteins were detected using a chemiluminescence detection system (ECL Prime Western Blot Detection System; GE Healthcare, RPN2232) according to the manufacturer's instructions.

Nishida Y., Yagi H., Ota M., Tanaka A., Sato K., Inoue T., Yamada S., Arakawa N., Ishige T., Kobayashi Y., Arakawa H, & Takizawa T. (2023). Oxidative stress induces MUC5AC expression through mitochondrial damage‐dependent STING signaling in human bronchial epithelial cells. FASEB BioAdvances, 5(4), 171-181.

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PSMA Expression Analysis in LNCaP Tumors

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PSMA expression by LNCaP tumors used in imaging studies was assessed by immunoblotting. Tumor lysates were loaded on 10% Mini-PROTEAN TGX precast gels and fractionated by SDS-PAGE. Protein extracts were electro-transferred to PVDF membrane. The PVDF membrane was incubated with PSMA (E-18) goat anti-PSMA antibody (sc-10269; Santa Cruz Biotechnology) in a 1:250 dilution, and anti-β-Actin (13E5) rabbit mAb (4970; Cell Signaling Technology, Beverly, MA) in a 1:2000 dilution overnight at 4°C. The membrane was then washed and incubated with AP-Bovine anti-goat IgG (sc-2351; Santa Cruz Biotechnology) plus AP-Goat anti-rabbit IgG (H+L) (111055045, Jackson ImmunoResearch) in a 1:2000 dilution for 1 h at room temperature. Finally, the membrane was washed and incubated with a chemiluminescent reagent (ECF substrate, GE RPN5785) for 5 min and imaged using a STORM 840 imaging system (GMI Ltd.). Bands for PSMA and ß-actin were quantified using ImageQuant TL software (GE Healthcare Life Sciences).

Zlitni A., Yin M., Janzen N., Chatterjee S., Lisok A., Gabrielson K.L., Nimmagadda S., Pomper M.G., Foster F.S, & Valliant J.F. (2017). Development of prostate specific membrane antigen targeted ultrasound microbubbles using bioorthogonal chemistry. PLoS ONE, 12(5), e0176958.

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