Mouse anti actin antibody

Manufactured by Santa Cruz Biotechnology

Sourced in United States

The Mouse anti-actin antibody is a primary antibody that specifically recognizes and binds to the actin protein, a structural component found in the cytoskeleton of eukaryotic cells. This antibody can be used in various immunological techniques to detect and study the localization and expression of actin in biological samples.

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Anti-actin (514 citations) Anti-actin antibody (130 citations) Mouse anti-actin (75 citations) Mouse anti-actin monoclonal antibody (12 citations) Mouse anti-human β-actin antibody (5 citations) Mouse anti-β-actin antibody (sc-47778) (5 citations) Mouse anti-β-actin primary antibody (3 citations) Goat anti-mouse β-actin antibody (3 citations) Anti β-actin antibody produced in mouse (2 citations) Mouse anti-β-actin monoclonal antibody (sc-47778; (2 citations)

11 protocols using mouse anti actin antibody

Autophagy and Apoptosis Assays

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The following reagents were obtained commercially:
3‐[4,5‐dimethylthiazol‐2‐yl]2,5‐diphenyl tetrazolium bromide (MTT),
monodansylcadaverine (MDC), acridine orange were purchased from Sigma (St. Louis,
Missouri). 3‐Methyladenine (3‐MA, class III PI3K inhibitor) was obtained from
Calbiochem (La Jolla, California). Antibodies against the cleaved form of caspase‐3,
caspase‐8, Beclin‐1, and PARP were purchased from Cell Signaling Technology (Beverly,
MA). Antibodies against LC3 (Sigma) were also used. The p62/SQSTM1, caspase‐9,
ATG5‐ATG12 complex, GAPDH, mouse antiactin antibody, mouse antirabbit IgG antibody,
and rabbit antimouse IgG antibodies were purchased from Santa Cruz Biotechnology
(Santa Cruz, California). All other chemicals and reagents were purchased from Sigma
unless otherwise specified.

Lee Y., Park B., Park H., Yu S., Kang H, & Kim I. (2017). XIAP inhibitor embelin induces autophagic and apoptotic cell death in human oral squamous cell carcinoma cells. Environmental Toxicology, 32(11), 2371-2378.

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Comprehensive Cannabinoid Receptor Characterization

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Chemicals were of the purest analytical grade. MEM, glutamine, PES, DMSO, collagenase, DNase1, trypsin, BPA (Bisphenol A), ABTS (2,2′-azinobis [3-ethylbenzothiazoline-6-sulfonic acid]-diammonium salt), and hyaluronidase were purchased from Sigma (St. Louis, MO, USA). Rabbit anti-CB₁, anti-CB₂, anti-GPR55, anti-FAAH, anti-DAGL-α, anti-DAGL-β, anti-MAGL, anti-NAPE-PLD polyclonal antibodies, and KT109 were purchased from Cayman Chemicals (Ann Arbor, MI, USA). Mouse anti-actin antibody was obtained from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA), and rabbit anti-TRPV1 polyclonal antibody was from OriGene Technologies (Rockville, MD, USA). Rabbit anti-inhibin B polyclonal antibody was obtained from Elabscience Biotechnology (Houston, TX, USA), and rabbit anti-transferrin polyclonal antibody was from Proteintech Group (Chicago, IL, USA). Iodoresinferatoxin was obtained from Tocris Cookson (Bristol, UK), whereas SR144528 was a kind gift from Sanofi-Synthelabo (Montpellier, France).

Rossi G., Dufrusine B., Lizzi A.R., Luzi C., Piccoli A., Fezza F., Iorio R., D’Andrea G., Dainese E., Cecconi S, & Maccarrone M. (2020). Bisphenol A Deranges the Endocannabinoid System of Primary Sertoli Cells with an Impact on Inhibin B Production. International Journal of Molecular Sciences, 21(23), 8986.

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Western Blot Analysis of Mitochondrial Proteins

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Cell lysates were prepared after treatment with 60 μΜ of conjugates for 48 h. Total cellular proteins were isolated at 4 °C using RIPA buffer (ABCAM) and mixed with 4% SDS-containing loading buffer. Protein concentrations were determined using Bradford assay [24 (link)]. Lysates (100 mg protein/well) were reduced in Laemmli buffer containing 1 mM dithiothreitol, resolved by 10% SDS-PAGE and electrotransfered to Immobilon-P PVDF membranes (Millipore, Massachusetts, USA) according to standard procedures [25 (link)]. Blots were incubated at 4 °C overnight with rabbit monoclonal antibody against mitochondrial cytochrome c oxidase subunit II (COX2) (anti-mtCO2 antibody, ABCAM) at a 1:1000 dilution in blocking buffer. After washing with TBS-Tween and incubation with secondary antibody coupled to horse radish peroxidase, protein bands were visualized with ECL^TM chemiluminescence reagent (Amersham) and detected by autoradiography. The intensity of bands was quantified by Image Analysis, using the Image-Pro Plus 7 software (Media Cybernetics). Blots were re-probed with a mouse anti-actin antibody (Santa Cruz Biotechnology) to verify equal protein loading.

Giannopoulou P.C., Missiri D.A., Kournoutou G.G., Sazakli E., Papadopoulos G.E., Papaioannou D., Dinos G.P., Athanassopoulos C.M, & Kalpaxis D.L. (2019). New Chloramphenicol Derivatives from the Viewpoint of Anticancer and Antimicrobial Activity. Antibiotics, 8(1), 9.

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Quantifying Lung PPARγ Protein Levels

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Western blot (WB) analysis of lung homogenates was carried out as described previously (18 (link), 21 (link)). Briefly, tissue samples were homogenized in RIPA buffer and the protein content of the extracts was determined by the BCA Protein Assay Kit (Pierce, Rockford, IL). The homogenates were run on SDS-PAGE on 10% precast polyacrylamide gels (Bio Rad Lab, Hercules CA). The gels were transferred electrophoretically to nitrocellulose membranes (Bio Rad Lab). The blots were incubated with anti-PPARγ antibody (Cat#: sc-7273, Santa Cruz Biotech). The mouse anti-actin antibody (Santa Cruz Biotech) was used as a control for a house-keeping protein. After incubating with secondary antibody, immuno-detection was performed using Amersham ECL Western Blotting Detection Reagent (GE Healthcare Bio-Science Corp. Piscataway, NJ) and the images were captured by Fujiform LAS-4000 luminescent image analyzer (FUJIFILM Corporation, Tokyo). Densitometry was used to quantitate the expression of specific proteins and the ratio of PPARγ to actin.

Singh S.P., Chand H.S., Langley R.J., Mishra N., Barrett T., Rudolph K., Tellez C., Filipczak P.T., Belinsky S., Saeed A.I., Sheybani A., Exil V., Agarwal H., Sidhaye V.K., Sussan T., Biswal S, & Sopori M. (2017). Gestational exposure to sidestream (secondhand) cigarette smoke promotes transgenerational epigenetic transmission of exacerbated allergic asthma and bronchopulmonary dysplasia. Journal of immunology (Baltimore, Md. : 1950), 198(10), 3815-3822.

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Western Blot Analysis of Bax and Bcl-2

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For the detection of Bax and Bcl-2 expression, we used Western blotting, as the method described before [20 (link),21 (link)]. After separating 40-µg protein on sodium dodecyl sulfate-polyacrylamide gels, protein was transferred onto a nitrocellulose membrane (Schleicher & Schuell GmbH, Dassel, Germany). For the primary antibodies, we used mouse anti-actin antibody (1:2,000; Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse anti-Bax antibody (1:1,000; Santa Cruz Biotechnology), and mouse antiBcl-2 antibody (1:1,000 Santa Cruz Biotechnology). As the secondary antibodies, we used mouse horseradish peroxidase-conjugated antibody (1:2,000; Santa Cruz Biotechnology) for actin, Bax, and Bcl-2. We used enhanced chemiluminescence detection system (Amersham Pharmacia Biotechnology GmbH, Freiburg, Germany) for the band detection. By Image-Pro Plus software (Media Cybernetics Inc.), the detected bands were densitometrically analyzed.

Lee J.M., Kim T.W., Park S.S., Han J.H., Shin M.S., Lim B.V., Kim S.H., Baek S.S., Cho Y.S, & Kim K.H. (2018). Treadmill Exercise Improves Motor Function by Suppressing Purkinje Cell Loss in Parkinson Disease Rats. International Neurourology Journal, 22(Suppl 3), S147-155.

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Polyglutamylation Analysis in Mice Ovaries

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Ovaries from pcd^3J+/+ and pcd^3J-/- mice were ground and homogenized in tissue lysis buffer [0.32 M sucrose, 0.01 M Tris (PH 7.4)] with protease cocktail inhibitor (Sigma-Aldrich, Missouri, USA) and 1 mM PMSF. Total proteins were extracted from the supernatant and quantified using a Bradford Assay [29 (link)]. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes (GE Healthcare, Buckinghamshire, United Kingdom). Membranes were probed with a rabbit anti-polyglutamylation antibody (1:1000) [30 (link)] and a mouse anti-actin antibody (1:2000, Santa Cruz Biotechnology, Texas, USA), and blots were visualized using peroxidase-conjugated anti-rabbit and anti-mouse IgG antibodies (1:2000, Santa Cruz Biotechnology, Texas, USA), respectively.

Song N., Kim N., Xiao R., Choi H., Chun H.I., Kang M.H., Kim J.H., Seo K., Soundrarajan N., Do J.T., Song H., Ge Z.J, & Park C. (2015). Lack of Cytosolic Carboxypeptidase 1 Leads to Subfertility due to the Reduced Number of Antral Follicles in pcd3J-/- Females. PLoS ONE, 10(10), e0139557.

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Western Blot Analysis of Intestinal Proteins

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The freshly removed intestines were meshed and lysed with RIPA lysis buffer (Thermo Fisher Scientific, Waltham, MA, United States) on ice. The protein concentrations were measured with Bradford assay (Bio-Rad, Hercules, CA, United States), and 20 µg of protein per sample was subjected to 10% SDS-acrylamide gels for electrophoresis. The proteins were separated by electrophoresis at 80–120 V in an electrophoresis unit (Invitrogen, Waltham, MA, United States) with NuPAGE™ MOPS SDS as a running buffer. The separated proteins were transferred onto Immobilon PVDF membranes (Invitrogen, Waltham, MA, United States) with NuPAGE™ Transfer buffer using the Invitrogen blotting system and a BIO-RAD power supply constantly held at 125 mA and a maximum voltage of 10 V. After blocking in 5% skimmed milk/TBS–Tween 20, the membrane was incubated with a primary antibody and then with horseradish-peroxidase (HRP)-conjugated secondary antibodies. Enhanced chemiluminescence (Thermo Fisher Scientific, Waltham, MA, United States) signals were recorded using a 440-CF imaging system (Kodak, Rochester, NY, United States). Primary antibodies included mouse antiactin antibody (Santa Cruz Biotechnology Cat# sc-8432, RRID: AB_626630) and rabbit anti-YY1 antibody (Abcam, Cambridge, Cat# ab245365).

Lu C., Zhang X., Luo Y., Huang J, & Yu M. (2022). Identification of CXCL10 and CXCL11 as the candidate genes involving the development of colitis-associated colorectal cancer. Frontiers in Genetics, 13, 945414.

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Western Blotting for AQP4 Expression

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Western blotting using 30 μg of total proteins was carried out as described by Siddiqui et al. [20 (link)]. Membrane was probed with rabbit anti-AQP4 antibody (Abcam) at a concentration of 1 μg/ml in 4% blocking solution. Mouse anti-actin antibody (Santa Cruz Biotechnology) was used as a loading control. The membranes were visualized via enhanced chemiluminescence (Super Signal West, Thermo Scientific).

Rizwan Siddiqui M., Attar F., Mohanty V., Kim K.S., Shekhar Mayanil C, & Tomita T. (2018). Erythropoietin-mediated activation of aquaporin-4 channel for the treatment of experimental hydrocephalus. Child's Nervous System, 34(11), 2195-2202.

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Oxidative Stress Regulation in Diabetes

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MG (cat. no. M0252), GSH (cat. no. G4251), NAC (cat. no. A7250), streptozotocin (STZ; cat. no. S0130), the GSH synthesis inhibitor buthionine sulfoximine (BSO; cat. no. B2640) and guanidine hydrochloride (cat. no. G7294) were purchased from Sigma-Aldrich (Merck KGaA). Rabbit anti-glutathione peroxidase-1 (GPX-1; cat. no. ab22604), rabbit anti-superoxide dismutase-1 (SOD-1; cat. no. ab51254), rabbit anti-endothelial nitric oxide synthase (eNOS; cat. no. ab5589), anti-phosphorylated (p)-eNOS (cat. no. ab215717) and HRP-conjugated goat-anti-rabbit IgG (cat. no. ab150077) were purchased from Abcam. Rabbit anti-Akt (cat. no. sc-8312) and anti-p-Akt (cat. no. sc-7985 R) were obtained from Santa Cruz Biotechnology, Inc. Mouse anti-actin antibody (cat. no. 612656) was obtained from BD Biosciences. HRP-conjugated sheep-anti-mouse IgG (cat. no. NA931) was purchased from Amersham (Cytiva). Enhanced chemiluminescence (ECL) reagent (cat. no. 1705060) was acquired from Bio-Rad Laboratories, Inc. Nitric oxide (NO; cat. no. A012), which was used for the nitrate reductase method according to the instructions of the NO assay kit, and the malondialdehyde (MDA) assay kit (cat. no. A003) were obtained from Nanjing Jiancheng Bioengineering Institute.

Fang X., Liu L., Zhou S., Zhu M, & Wang B. (2021). N-acetylcysteine inhibits atherosclerosis by correcting glutathione-dependent methylglyoxal elimination and dicarbonyl/oxidative stress in the aorta of diabetic mice. Molecular Medicine Reports, 23(3), 201.

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Western Blot Analysis of GFP and Actin

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Protein samples were subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to polyvinylidene difluoride (PVDF) membrane. The membrane was incubated with blocking buffer (5% dried milk in TBS-Tween (10 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.1% v/v Tween-20)) for 1 h at RT and then incubated with a mouse anti-GFP antibody (Santa Cruz Biotechnology, SC-9996) or a mouse anti-actin antibody (Santa Cruz Biotechnology, SC-47778) (1:2000) in blocking buffer for 12 h at 4 °C overnight, washed with TBS-T, and incubated with a goat anti-mouse secondary antibody conjugated to horseradish peroxidase (HRP) (Thermo Scientific, 31,430) (1:15,000) for 1 h at RT. The membrane was washed with TBS-Tween and incubated with GE Healthcare ECL Western blotting detection solution and imaged with a BIO-RAD ChemiDoc Touch imaging system. Cells expressing GST-CpnA were also used in the native membrane binding assay and the GST was detected with an HRP-conjugated anti-GST antibody (1:5000) (GE Healthcare Life Services, RPN 1236 V).

Ilacqua A.N., Price J.E., Graham B.N., Buccilli M.J., McKellar D.R, & Damer C.K. (2018). Cyclic AMP signaling in Dictyostelium promotes the translocation of the copine family of calcium-binding proteins to the plasma membrane. BMC Cell Biology, 19, 13.

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