Mouse anti actin

Manufactured by Abcam

Sourced in United States, United Kingdom

Mouse anti-actin is a primary antibody that recognizes the actin protein, a highly conserved cytoskeletal protein found in all eukaryotic cells. This antibody can be used to detect and quantify actin levels in various experimental applications.

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Lab products found in correlation

Mouse anti flag, by Merck Group (7 mentions) Horseradish peroxidase conjugated secondary antibody, by Rockland Immunochemicals (5 mentions) Photo imager, by Kodak (4 mentions) Horseradish peroxidase conjugated anti rabbit igg antibody, by Abcam (4 mentions) Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (4 mentions) Ecl kit, by GE Healthcare (3 mentions) Las 1000, by Fujifilm (3 mentions) Rat anti ha peroxidase, by Roche (3 mentions) Rabbit anti flag, by Merck Group (3 mentions) Alexa fluor secondary antibody, by Thermo Fisher Scientific (3 mentions) Phosphatase inhibitor, by Merck Group (2 mentions) Nupage reducing agent, by Thermo Fisher Scientific (2 mentions) Amersham hyperfilm ecl, by GE Healthcare (2 mentions) Nupage lds sample buffer, by Thermo Fisher Scientific (2 mentions) Amersham ecl prime western blotting detection system, by GE Healthcare (2 mentions) Mouse anti myc tag, by Cell Signaling Technology (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Complete protease inhibitor cocktail, by Roche (2 mentions) Mouse anti βiii tubulin, by Merck Group (2 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (2 mentions)

Spelling variants of this product

Anti-actin (210 citations) Mouse anti-β-actin (199 citations) Mouse monoclonal anti-actin antibody (5 citations) Mouse monoclonal anti-beta-actin (3 citations) Mouse anti-actin (ab3280) (3 citations) Mouse anti (2 citations) Mouse anti β-actin (clone AC-15) (2 citations) Mouse monoclonal anti-β-actin (ab1906) (2 citations) Monoclonal mouse anti-human β-actin primary antibody (2 citations) Anti-β-actin mouse IgG (2 citations)

56 protocols using mouse anti actin

Antibody Panel for Protein Detection

Cited 1 time

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The following primary antibodies were used in this study: mouse anti-alpha-synuclein (Bio Legend, 4B12/Synuclein, 807801), mouse anti-alpha-synuclein (Invitrogen, AHB0261), mouse anti-GFP (Roche, 11814460001), mouse anti-HA (Sigma, HA-7, H9658), rabbit anti-HA (Sigma, H6908), rabbit anti-N-WASP (Cell Signaling, 30D10, #4848), rabbit anti-N-WASP (polyclonal raised against peptide 385–401) [65 (link)], rabbit anti-N-WASP (Invitrogen, PA5-52198), mouse anti-synaptophysin 1 (SySy, 7.2, 101 0011), mouse anti-actin (Abcam, ab14128). Secondary antibodies used in this study were: HRP-conjugated anti-mouse secondary (Thermo Fisher Scientific), HRP-conjugated anti-rabbit secondary (Promega, W4011), Alexa Fluor™ 488-conjugated goat anti-mouse IgG (Invitrogen, A-11001), Alexa Fluor™ 568-conjugated goat anti-rabbit IgG (Invitrogen, A-11011) and Abberior STAR 488-conjugated goat anti-rabbit IgG (Abberior).

Jackson J., Hoffmann C., Scifo E., Wang H., Wischhof L., Piazzesi A., Mondal M., Shields H., Zhou X., Mondin M., Ryan E.B., Döring H., Prehn J.H., Rottner K., Giannone G., Nicotera P., Ehninger D., Milovanovic D, & Bano D. (2024). Actin-nucleation promoting factor N-WASP influences alpha-synuclein condensates and pathology. Cell Death & Disease, 15(4), 304.

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Antibody Characterization for Mitochondrial Studies

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Antibodies and other reagents used were as follows: anti‐USP30 (Sigma HPA016952, 1:500 for WB), anti‐USP30 (gift from Baris Bingol, Genentech 10, 1:100 for IF), anti‐PMP70 (Sigma SAB4200181, 1:1,000), anti‐PEX19 (Life technologies, PA522129, 1:1,000), anti‐catalase (AbCam, ab1877, 1:2,000), anti‐PINK1 (Novus Biologicals, BC100‐494,) anti‐PINK1 (Fig 1E; D8G3, Cell Signalling, 6946S), anti‐GFP (gift from Ian Prior, University of Liverpool, Liverpool, UK; 1:5,000), anti‐VPS35 (AbCam ab10099, 1:1,000), anti‐p62 (BD Transduction, 610833, 1:1,000), anti‐LC3 (Nanotools, 5F10, 1:500), anti TOMM20 (Sigma HPA011562, 1:1,000), anti‐ACOX1 (gift from T. Hashimoto, Shinshu University, Nagano 390‐8621, Japan, 1:10,000), anti‐ACOX1 [EPR19038] (Abcam, ab184032, 1:1,000), anti‐VDAC1 (AbCam, ab15895, 1:1,000), anti‐GSTK1 (SantaCruz, Sc‐515580, 1:200), anti ATG7 (Cell Signalling, 12994), mouse anti‐actin (AbCam ab6276, 1:10,000), rabbit anti‐actin (Sigma A2266, 1:10,000), mouse anti‐αtubulin (Sigma T5168, 1:10,000). anti‐Myc (Millipore clone 4A6), oligomycin A (SIGMA 75351), antimycin A (SIGMA A8674), epoxomicin (Millipore 324800) and folimycin (Millipore 344085).

Marcassa E., Kallinos A., Jardine J., Rusilowicz‐Jones E.V., Martinez A., Kuehl S., Islinger M., Clague M.J, & Urbé S. (2018). Dual role of USP30 in controlling basal pexophagy and mitophagy. EMBO Reports, 19(7), e45595.

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Western Blot Protein Expression Analysis

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Protein lysate from one million cells were extracted on ice using Golden Lysis Buffer (10 mM Tris pH 8.0, 400 mM NaCl, 1% Triton X-100, 10% Glycerol+Complete protease inhibitor cocktail (Roche), phosphatase inhibitor (Sigma)). Protein concentration was measured using Pierce’s BCA Protein Assay Kit and analyzed on the Versamax spectrophotometer at a wavelength of 560nm. Appropriate volumes containing 20ug of protein lysates combined with NuPage LDS Sample Buffer and NuPage Reducing Agent (Invitrogen) were run on 4–12% (or otherwise indicated) NuPage Bis-Tris gels in MOPS buffer. Proteins were transferred onto a PVDF membrane (Millipore), blocked in 5% milk (TBST + dry milk) for one hour and incubated in the primary antibody (in 5% milk) overnight at 4°C. Membranes were washed with 0.05% TBST (TBS + 5% Tween) and secondary antibody incubations were done at room temperature for one hour. Proteins were visualized using Amersham ECL Prime Western Blotting Detection System and Amersham Hyperfilm ECL (GE Healthcare).
The following primary antibodies were used: mouse anti-Actin (1:10,000; Abcam), mouse anti-myc-tag (1:1000; Cell Signaling). Secondary antibodies goat anti-rabbit (Santa Cruz) and goat-anti-mouse (GE Healthcare) were used at concentrations of 1:10,000.

Ha N.H., Long J., Cai Q., Shu X.O, & Hunter K.W. (2016). The Circadian Rhythm Gene Arntl2 Is a Metastasis Susceptibility Gene for Estrogen Receptor-Negative Breast Cancer. PLoS Genetics, 12(9), e1006267.

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Cortical Brain Tissue Analysis of APP-KI Mice

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The brain cortical tissues were collected from APP-KI mice with or without SR9009 injection. The brain lysates were prepared as described previously [23 (link)]. The following primary antibodies were used: rabbit anti-Iba1 (1:1000; WAKO), mouse anti-NOS2 (1:1000; Abcam), mouse anti-IL-1β (1:1000, Santa Cruz Biotechnology), mouse anti-actin (1:5000; Abcam), mouse anti-phospho-IκBα (1:1000, Santa Cruz Biotechnology), rabbit anti-IκBα (1:1000, Santa Cruz Biotechnology), and mouse anti-Aβ (6E10, 1:1000, Covance). The following were used as secondary antibodies: horseradish peroxidase (HRP)-labeled anti-rabbit (1:2000; GE Healthcare) and anti-mouse (1:2000; R&D Systems). The HRP-labeled antibodies were detected using an enhanced chemiluminescence detection system (ECL Kit; GE Healthcare) with an image analyzer (LAS-1000; Fuji Photo Film).

Ni J., Wu Z., Meng J., Saito T., Saido T.C., Qing H, & Nakanishi H. (2019). An impaired intrinsic microglial clock system induces neuroinflammatory alterations in the early stage of amyloid precursor protein knock-in mouse brain. Journal of Neuroinflammation, 16, 173.

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Western Blot Analysis of STAT3 in Lung

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Whole-lung extracts and nuclear fractions were run on 12.5% SDS-polyacrylamide gels, with detailed protocol for sample processing as described in our previous publications(18 (link), 19 (link)). Polyvinylidene difluoride membranes were probed sequentially with rabbit anti-STAT3 or anti-phospho-STAT3 (1:2000); followed by horseradish peroxidase-conjugated anti-rabbit IgG antibodies (1:3000) (AbCAM, Cambridge, MA, USA). We detected actin as a loading control using mouse anti-actin (1:2000) (AbCAM) followed by secondary as described above. Proteins were visualized by chemiluminiscense (Super Signal West Pico chemiluminescent substrate, Pierce, Rockford, IL, USA) using a Kodak photo imager. In our previous report(13 (link)) we found that the peak of transgene expression of FER by EP delivery was at 24 h weaning off by 72 h, thus we performed lung sample collection using these time points for our Western Blot analysis.

Dolgachev V., Panicker S., Balijepalli S., McCandless L.K., Yin Y., Swamy S., Suresh M., Delano M.J., Hemmila M.R., Raghavendran K, & Machado-Aranda D. (2018). Electroporation-mediated Delivery of FER Gene Enhances Innate Immune Response and Improves Survival in a Murine Model of Pneumonia. Gene therapy, 25(5), 359-375.

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Antibody Validation for Protein Analysis

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The following primary antibodies were used in our study: mouse anti-CValpha (Abcam, 14748; 1:5000), rabbit anti-Hsp60 (Abcam, 46798; 1:500), rabbit anti-ROCK2 (Abcam, 125025; 1:5000), mouse anti-actin (Abcam, 8226; 1:1000), mouse anti-HK2 (Abcam, 3740910; 1:1000), mouse anti-Mfn2 (Abcam, 56889; 1:1000), rabbit anti-TOM20 (Santa Cruz, 191883; 1:1000), mouse anti-VDAC1 (Abcam, 14734; 1:1000), mouse anti-TOM70 (Santa Cruz, 390545; 1:1000), mouse anti-UQCRC2 (Abcam, 14745, 1:1000), rabbit anti-COXIV (Novus, NB110-39115; 1:500) and mouse anti-Flag (Sigma, F1804; 1:1000). Rabbit and mouse horseradish peroxidase-conjugated secondary antibodies (Jackson Immunoresearch; 1:5000) were used for secondary incubation.
The following primary antibodies were used in our study for immunofluorescence: mousen anti-CValpha (Abcam, 14748; 1:500), rabbit anti-Hsp60 (Abcam, 46798; 1:500), rabbit anti-LC3B (Cell Signaling, 2775) and mouse anti-Flag (Sigma, F1804; 1:1000). All antibodies were diluted in 1% goat serum.

Moskal N., Riccio V., Bashkurov M., Taddese R., Datti A., Lewis P.N, & Angus McQuibban G. (2020). ROCK inhibitors upregulate the neuroprotective Parkin-mediated mitophagy pathway. Nature Communications, 11, 88.

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Proximity Ligation Assay for Neuron Interactions

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The proximity ligation assay was performed according to the manufacturer’s instructions (Sigma-Aldrich). Briefly, fixed neurons were incubated with primary antibodies (SNPH-actin interaction: rabbit anti-SNPH, 1:250 and mouse anti-actin, 1:100, Abcam; SNPH-microtubules interaction: rabbit anti-SNPH, 1:100, Abcam and mouse anti-βIII-tubulin, 1:2000, Sigma-Aldrich) diluted in Duolink antibody diluent at 4°C overnight, then washed three times with Buffer A (0.01 M Tris, 0.15 M NaCl, 0.05% Tween 20) at RT for 5 min each, incubated with Duolink PLA Probe at 37°C for 1 hr, rewashed with PBS three times at RT for 5 min each, then incubated in Duolink PLA ligation solution at 37°C for 30 min, rewashed with PBS three times at RT for 5 min each, then incubated with Duolink PLA amplification solution at 37°C for 100 min, washed with 1x Buffer B (0.2 M Tris, 0.1 M NaCl pH 7.5) two times at RT for 10 min each and PBS at RT for 5 min. To counterstain for a neuronal marker, neurons were post-fixed with 4% paraformaldehyde and 4% sucrose for 10 min at RT and processed for immunocytochemistry.

Li S., Xiong G.J., Huang N, & Sheng Z.H. (2020). The crosstalk of energy sensing and mitochondrial anchoring sustains synaptic efficacy by maintaining presynaptic metabolism. Nature metabolism, 2(10), 1077-1095.

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C. elegans Developmental Proteome Analysis

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C. elegans were synchronized at 20 °C by bleaching gravid adult animals and maintaining starved L1 larvae for at least 24 h before plating on OP50. For sample collection, animals were harvested after 2 h (L1), 12 h (L2), 32 h (L3), 50 h (L4), and 72 h (gravid adult) on OP50. Number of animals loaded per lane was normalized for actin—~1000 L1s, 800 L2s, 600 L3s, 400 L4s, and 200 gravid adults. Proteins were resolved on 4–12% Bis-Tris polyacrylamide gels (Thermo Fisher), transferred to nitrocellulose membranes (Thermo Fisher), and probed with rat anti-HA-peroxidase 1:1000 (Roche 12013819001), mouse anti-FLAG 1:1000 (Sigma, F1804), mouse anti-actin 1:10,000 (Abcam ab3280), or rabbit anti-CSR-1 1:2000 antibodies^{8 (link)}. Secondary HRP antibodies were purchased from Thermo Fisher. Unedited western blots provided in the Source Data File.

Nguyen D.A, & Phillips C.M. (2021). Arginine methylation promotes siRNA-binding specificity for a spermatogenesis-specific isoform of the Argonaute protein CSR-1. Nature Communications, 12, 4212.

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Western Blot Procedure for KCNA1 and GPC1

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Proteins were prepared using radioimmunoprecipitation assay buffer (RIPA) as previously reported^{23 (link)}. Briefly, lysate protein concentrations were measured by BCA Assay (Thermo Fisher, USA). Protein extracts were separated by 10% SDS-PAGE and subsequently electro-transferred to the nitrocellulose membranes (GE Lifescience, USA). The membranes were blocked and then incubated with primary antibodies rabbit anti-KCNA1 (Sigma, Shanghai, China), rabbit anti-GPC1 (Abcam, Shanghai, China) and mouse anti-actin (Abcam, USA) overnight at 4 °C after 5% BSA block, and HRP-conjugated secondary antibodies (Invitrogen, CA, USA) were incubated at room temperature for 2 h at following day. Specific signals were examined using a Pierce Enhanced Chemiluminescence Plus kit (Life Technology, USA) and recorded with FluorChem Q (Proteinsimple, MD, USA). The band intensities were quantitated by Image J v1.50 (NIH, USA), relative densities of KCNA1 and GPC1 were normalized to actin of the same blot.

Li Q., Han Y., Xu P., Yin L., Si Y., Zhang C., Meng Y., Feng W., Pan Z., Gao Z., Li J, & Yang W. (2020). Elevated microRNA-125b inhibits cytotrophoblast invasion and impairs endothelial cell function in preeclampsia. Cell Death Discovery, 6, 35.

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Circadian Protein Rhythms in Drosophila

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Flies were synchronized for 3 days under LD (500 lux:0 lux) cycles, and collected every 3–4 h. Protein was extracted from 40–50 male heads at each time point. Frozen heads were homogenized in 150 ml ice-cold extraction buffer (20 mM HEPES, pH 7.5, 100 mM KCl, 5% glycerol, 10 mM EDTA, 0.1% Triton, 1 mM dithiothreitol, 0.5 mM phenylmethylsulfonyl fluoride) plus protease inhibitors (complete mini Roche), phosphatase inhibitors cocktails 1 (0.5%) and 2-mM b-glycerophosphate (1%; Sigma). For SDS–PAGE, 50 ug of protein extracts were separated on 8–10% Tris–acetate gels (Invitrogen) and transferred to NC membranes. Primary antibodies used were mouse anti-ACTIN (abcam;1∶2000) and rat ani-CRY and rat anti-TIM (from the laboratory of Dr. Rosbash Lab; anti-CRY 1∶500; anti-TIM 1∶1000). HRP-conjugated secondary antibodies (Zhongshan Goldenbridge Biotechnology Co., Ltd) were goat anti-mouse IgG (1∶1000) and goat anti rat IgG (1∶1000). All western blots were performed in triplicate. Band intensity was calculated and analyzed with the Gel-Pro Analyzer 4.0.

Liu Z, & Zhao Z. (2014). Effects of Light Interruption on Sleep and Viability of Drosophila melanogaster. PLoS ONE, 9(8), e105678.

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