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Anti actin ab

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Anti-actin Ab is a laboratory reagent used for the detection and quantification of actin, a ubiquitous cytoskeletal protein, in various biological samples. It functions as a specific antibody that binds to actin, allowing researchers to analyze the expression, localization, and dynamics of this essential cellular component.

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Lab products found in correlation

Polyclonal rabbit abs to traf3 h122, by Santa Cruz Biotechnology (2 mentions) Hrp labeled secondary abs, by Jackson ImmunoResearch (2 mentions) L glutamine, by Thermo Fisher Scientific (2 mentions) Non essential amino acids (neaa), by Thermo Fisher Scientific (2 mentions) Hepes, by Thermo Fisher Scientific (2 mentions) Fitc conjugated secondary ab, by Jackson ImmunoResearch (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Merck Group (1 mentions) Pcmv cgas, by OriGene (1 mentions) Pcmv sting, by OriGene (1 mentions) Ripa buffer, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Ecl plus western blotting substrate, by Thermo Fisher Scientific (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Anti mouse igg1 microbeads, by Miltenyi Biotec (1 mentions) Igg1 rpe, by Jackson ImmunoResearch (1 mentions) Macs ms column, by Miltenyi Biotec (1 mentions) Sodium pyruvate, by Thermo Fisher Scientific (1 mentions) Nf κb2, by Cell Signaling Technology (1 mentions) C rel, by Cell Signaling Technology (1 mentions) Dna oligonucleotide primers, by Integrated DNA Technologies (1 mentions)

Spelling variants of this product

Anti-actin (1282 citations) Anti-β-actin Ab (26 citations) Mouse anti-β-actin Ab (9 citations) Mouse monoclonal anti-β-actin Ab (7 citations) Anti-mouse actin Ab (4 citations) Anti-β-Actin Ab (AC-15) (2 citations) Anti-β-actin antibody (Ab) (2 citations) Anti-beta actin Ab (2 citations) Anti-actin monoclonal Ab (2 citations)

8 protocols using anti actin ab

1

Immunofluorescence Analysis of Endometriotic Cells

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Human primary endometriotic stromal cells that were previously transfected with either the control vector or the shOCT4 plasmids were treated with or without TGF-βI (1 ng/mL). The cells were then fixed with 0.05% glutaraldehyde at room temperature for 15 minutes and blocked in 50 mg/mL of bovine serum albumin and 0.5% Triton X-100 in phosphate-buffered saline (pH 7) for 1 hour at room temperature. The blocked cells were incubated with an anti-Actin Ab (Sigma-Aldrich), and the bound primary Ab was detected with a FITC-conjugated secondary Ab (Jackson ImmunoResearch). The nuclei of the cells were counterstained with 4',6-diamidino-2-phenylindole (DAPI) (Sigma-Aldrich, St. Louis, MO, USA), and the cells were covered with an antifading reagent (Vector Laboratories, Burlingame, CA, USA) before examining them under a confocal-imaging fluorescence microscope (Leica, Buffalo Grove, IL, USA).
Au H.K., Chang J.H., Wu Y.C., Kuo Y.C., Chen Y.H., Lee W.C., Chang T.S., Lan P.C., Kuo H.C., Lee K.L., Lee M.T., Tzeng C.R, & Huang Y.H. (2015). TGF-βI Regulates Cell Migration through Pluripotent Transcription Factor OCT4 in Endometriosis. PLoS ONE, 10(12), e0145256.
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2

Quantifying cGAS and STING Activation

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HEK293T cells were transfected with pCMV-cGAS (Origene), pCMV-STING (Origene) or pcDNA3.1 vector (60 ng DNA). Cells were trypsinized 24 post transfection and re-plated individually or mixed at 1:1 ratio, such that each well contained a total of 4 × 105 cells/well in a 24 well dish. Cells were infected, or permeabilized with positive control ligands cGAMP (1µg/ml) or transfected with ISD (1µg), 6 hours after plating and harvested at indicated times and processed for RNA and qRT-PCR. Immunoblots for cGAS or STING protein in HEK293, HEK293T and HeLa cells were carried out using cell lysate prepared using RIPA buffer (Pierce-Thermo Scientific) and protease inhibitor cocktails (Sigma). Anti cGAS Ab (Cat# AP10510c, Abgent), anti-STING poly clonal Ab (Cat# PA5-26751, Thermo Scientific) and anti-actin Ab (Cat# A2228, Sigma) were used at the 1:500, 1:500 and 1:1000 concentration respectively.
Zhang Y., Yeruva L., Marinov A., Prantner D., Wyrick P., Lupashin V, & Nagarajan U.M. (2014). The DNA sensor, cyclic GMP-AMP synthase (cGAS) is essential for induction of IFN beta during Chlamydia trachomatis infection. Journal of immunology (Baltimore, Md. : 1950), 193(5), 2394-2404.
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3

Quantification of Protein Synthesis in NSC34 Cells

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Protein synthesis in NSC34 cells was determined using standard Western blotting with anti-myc Ab (Abcam, Cambridge, UK), anti-actin Ab, anti-mouse secondary Ab, and anti-rabbit secondary Ab (Sigma, St. Louis, MO, USA). An OXPHOS detection cocktail (Abcam) was used based on standard Western blotting. ECL plus Western blotting substrate (Thermo Scientific, Rockford, IL, USA) were used for detection of proteins.
Choi Y.R., Hong Y.B., Jung S.C., Lee J.H., Kim Y.J., Park H.J., Lee J., Koo H., Lee J.S., Jwa D.H., Jung N., Woo S.Y., Kim S.B., Chung K.W, & Choi B.O. (2015). A novel homozygous MPV17 mutation in two families with axonal sensorimotor polyneuropathy. BMC Neurology, 15, 179.
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4

Western Blot Analysis of SERCA2

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Proteins from CMs extracts were separated by SDS-polyacrylamide gel electrophoresis (4–12% Bis-Tris Criterion BIO-RAD gels), blotted for 1 h, incubated with polyclonal anti-SERCA2 primary antibody (N-19; Santa Cruz Biotechnology) at 4°C overnight, followed by incubation with a specific secondary antibody labeled with fluorescent markers (Alexa Fluor or IRDye) for 1 h. Signal intensity was quantified by Odyssey Infrared Imaging System (LI-COR). SERCA2 protein levels were normalized to actin levels, as measured using polyclonal anti-actin Ab (Sigma). Data are shown as percent changes vs. Ctrl.
Altomare C., Lodrini A.M., Milano G., Biemmi V., Lazzarini E., Bolis S., Pernigoni N., Torre E., Arici M., Ferrandi M., Barile L., Rocchetti M, & Vassalli G. (2021). Structural and Electrophysiological Changes in a Model of Cardiotoxicity Induced by Anthracycline Combined With Trastuzumab. Frontiers in Physiology, 12, 658790.
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5

Trout Immunoglobulin Profiling Protocol

Cited 1 time
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Phosphorothioate-modified B class CpG 2006 ODN (5′-T*CG T*CG T*TT T*GT C*GT T*TT G*TC G*T*T-3′, * indicates phosphothioate bonds) and non-CpG 2007 ODN, inverting all CGs to GCs, were purchased from Integrated DNA technologies. The monoclonal Abs IgF1-18 (6-1-18) anti-trout IgM38 (link) and anti-trout IgT13 (link) are described earlier. Isotype specific secondary Abs; IgG1-RPE (for IgM) and IgG2a-APC (for IgT) were both from Jackson ImmunoResearch. Fixable Viability Dye 780 (FVD780) was purchased from eBioscience. MACS MS columns and anti-Mouse IgG1 MicroBeads were purchased from Miltenyi Biotec. Anti-actin Ab was purchased from Sigma, while the preparation of MHCIIβ antiserum is described previously56 (link).
Jenberie S., Thim H.L., Sunyer J.O., Skjødt K., Jensen I, & Jørgensen J.B. (2018). Profiling Atlantic salmon B cell populations: CpG-mediated TLR-ligation enhances IgM secretion and modulates immune gene expression. Scientific Reports, 8, 3565.
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6

AMPA and NMDA receptor subunit analysis

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The AMPA receptor subunits were analysed by means of Western blotting as previously described [36] . For AMPA receptor subunit detection we used anti-GluA2-3 and anti-GluA1 antibodies (Abs) produced and characterised by us as described in [36] (see supplementary figure 2). For NMDA receptor subunit detection we used anti-GluN2A (clone A3-2D10, Life technologies, Waltham, MA, USA), anti-GluN2B (clone N59/20; Antibodies Incorporated, Davis, CA, USA), anti-NR1 subunit Ab produced by us and analysed in [37] ; We also used anti-PSD95 Ab (clone K28/43, Antibodies Incorporated, Davis, CA, USA) and anti-actin Ab (clone AC-40; Sigma-Aldrich, St. Louis, MO, USA).
For AMPA and NMDA receptor subunits and PSD the signal was normalised to the actin content and the values were normalised by taking the mean values of the AIR exposed mice as one.
Ponzoni L., Braida D., Carboni L., Moretti M., Viani P., Clementi F., Zoli M., Gotti C, & Sala M. (2020). Persistent cognitive and affective alterations at late withdrawal stages after long-term intermittent exposure to tobacco smoke or electronic cigarette vapour: Behavioural changes and their neurochemical correlates. Pharmacological research, 158.
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7

Choline Metabolism Regulation Assay

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Tissue culture supplements including stock solutions of sodium pyruvate, L-glutamine, non-essential amino acids, and HEPES (pH 7.55) were from Invitrogen (Carlsbad, CA). Trimethyl-D9-choline ([2H]9-Cho) was purchased from Cambridge Isotope Laboratories (Tewksbury, MA). MN58B and RSM932A were obtained from Aobious (Gloucester, MA). Antibodies (Abs) against Chkα were from Abcam (Cambridge, MA). Polyclonal rabbit Abs to TRAF3 (H122) were from Santa Cruz Biotechnology (Santa Cruz, CA). Anti-actin Ab was from Chemicon (Temecula, CA). HRP-labeled secondary Abs were from Jackson ImmunoResearch Laboratories, Inc. (West Grove, PA).
Gokhale S., Lu W., Zhu S., Liu Y., Hart R.P., Rabinowitz J.D, & Xie P. (2019). Elevated choline kinase α–mediated choline metabolism supports the prolonged survival of TRAF3-deficient B lymphocytes. Journal of immunology (Baltimore, Md. : 1950), 204(2), 459-471.
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8

Immunoblotting Reagents and Antibodies

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Tissue culture supplements including stock solutions of sodium pyruvate, L-glutamine, non-essential amino acids, and HEPES (pH 7.55) were from Invitrogen (Carlsbad, CA). IL-9 and IL-4 were purchased from Peprotech (Rocky Hill, NJ). Goat anti-mouse IgM F(ab′)2 was obtained from Jackson ImmunoResearch Laboratories (West Grove, PA). Agonistic anti-CD40 (HM40–3) was purchased from eBioscience (San Diego, CA). Peficitinib, baricitinib, decernotinib, stattic, and AS1517499 were purchased from Sigma-Aldrich Corp. (St. Louis, MO). EDTA-free Protease Inhibitor Cocktail Tablets were obtained from Roche Diagnostics Corp (Indianapolis, IN). Phosphatase Inhibitor Mini Tablets were purchased from Pierce (Rockford, IL). DNA oligonucleotide primers were obtained from Integrated DNA Technologies (Coralville, IA). Polyclonal or monoclonal rabbit Abs against total or phosphorylated STAT3, STAT6, STAT1, RelA, RelB, c-Rel, NF-κB1, NF-κB2, YY1, AID, Bcl6, and Blimp1 were from Cell Signaling Technology (Beverly, MA). Polyclonal rabbit Abs to TRAF3 (H122) were from Santa Cruz Biotechnology (Santa Cruz, CA). Anti-actin Ab was from Chemicon (Temecula, CA). HRP-labeled secondary Abs were from Jackson ImmunoResearch Laboratories, Inc. (West Grove, PA).
Gokhale S., Victor E., Tsai J., Spirollari E., Matracz B., Takatsuka S., Jung J., Kitamura D, & Xie P. (2023). Upregulated expression of the IL-9 receptor on TRAF3-deficient B lymphocytes confers the immunoglobulin isotype switching responsiveness to IL-9 in the presence of antigen receptor engagement and IL-4. Journal of immunology (Baltimore, Md. : 1950), 210(8), 1059-1073.
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