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Actin a2228

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Actin A2228 is a purified actin protein derived from rabbit skeletal muscle. It is a key structural component of the cytoskeleton in eukaryotic cells and is involved in various cellular processes such as cell motility, cell division, and intracellular transport.

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Lab products found in correlation

Chemiluminescent reagent, by Merck Group (1 mentions) Merlin sc 332, by Santa Cruz Biotechnology (1 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) E cadherin, by BD (1 mentions) Ne per extraction reagent, by Thermo Fisher Scientific (1 mentions) Nrf2 sc 722, by Santa Cruz Biotechnology (1 mentions) Criterion stain free gel, by Bio-Rad (1 mentions) Supersignal west pico plus chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) Tris glycine sds buffer, by Bio-Rad (1 mentions) Laemmli sample buffer, by Bio-Rad (1 mentions) Chemidoc mp imaging system, by Bio-Rad (1 mentions) Trans blot turbo transfer system, by Bio-Rad (1 mentions) C myc ab32072, by Abcam (1 mentions) Ezh2 5246, by Cell Signaling Technology (1 mentions) Slug 9585, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

A2228 (145 citations) β-actin (A2228) (34 citations) Anti-β-actin (A2228) (28 citations) Anti-β-actin antibody (A2228) (17 citations) β-actin antibody (A2228) (4 citations) Anti‐actin (A2228) (3 citations) Anti-actin mAb (A2228) (2 citations) Mouse monoclonal β-actin (A2228) (2 citations) Anti-beta-actin antibody (A2228) (2 citations) Anti-β-ACTIN (Catalog No. A2228, (2 citations)

6 protocols using actin a2228

1

LTβR Signaling Pathway Evaluation

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Stimulation: LIGHT (664-LI R&D systems), goat anti-human LTβR antibody (9 (link)). Detection antibodies: Cell Signaling Technology (EWS 11910, phospho-ERK-1/−2 9101, phospho-p38 9211), Santa Cruz Biotechnology (EWS sc-28327 AF647, TRAF3 sc-1828), Thermo (TRAF3 12H13L59), Abcam (p100 ab32859), and Sigma (Actin A2228).
Virgen-Slane R., Correa R.G., Ramezani-Rad P., Steen-Fuentes S., Detanico T., DiCandido M.J., Li J, & Ware C.F. (2020). The RNA-Binding Protein EWS is a Novel Modulator of Lymphotoxin-β Receptor Signaling. Journal of immunology (Baltimore, Md. : 1950), 204(5), 1085-1090.
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2

Immunoblotting for Protein Expression Analysis

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To analyze protein expression in cells, immunoblotting was performed according to standard methods [7 (link)]. The REDD1 primary antibody for immunoblotting (10638–1-AP) was obtained from Proteintech. Actin (A2228, Sigma Aldrich, US) was used as a loading control. Anti-rabbit (cs-7074) and anti-mouse (cs-7076) secondary antibodies bound to HRP were obtained from Cell Signaling Technology (Massachusetts, US). The protein bands were visualized with chemiluminescent reagents (Millipore, US).
Chang B., Meng J., Zhu H., Du X., Sun L., Wang L., Li S, & Yang G. (2018). Overexpression of the recently identified oncogene REDD1 correlates with tumor progression and is an independent unfavorable prognostic factor for ovarian carcinoma. Diagnostic Pathology, 13, 87.
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3

Analyzing FGFR4 Expression via Immunoblotting

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Cells were lysed by the addition of 50 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA, 1 mM dithiothreitol, 1 mM α-phenylmethylsulfonyl fluoride, 1 mM Na3VO4, 100 mM NaF, and 1% Triton X-100, pH 7.4. Following SDS-PAGE and transfer to nitrocellulose membrane, FGFR4 signal was detected via immunoblotting: Cell Signaling Technology (FGFR4: #8562) or Sigma Aldrich (Actin: A2228). Antibody specificity was verified via the molecular weight of FGFR4, a decrease in signal upon use of an siRNA against FGFR4 (not shown), and restored signal with transfection of an FGFR4 expression plasmid.
Phillips A.J., Lobl M.B., Hafeji Y.A., Safranek H.R., Mohr A.M, & Mott J.L. (2022). Glycosylation of FGFR4 in cholangiocarcinoma regulates receptor processing and cancer signaling. Journal of cellular biochemistry, 123(3), 568-580.
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4

Multiparametric Analysis of Cellular Signaling

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The following were used: Merlin (sc-332) and NEDD4 (sc-25508) from Santa Cruz, CA; phospho-histone H3 ser10 (H0412), AMOTL1 (HPA001196), and actin (A2228) from Sigma-Aldrich; YAP (#4912), p27 (#2552), AIP4 (#12117), and cleaved caspase 3 (#9661) from Cell Signaling Technology (Ozyme, France); E-cadherin (610182) from BD Biosciences; phospho-Src Y418 (44-660G) and phospho-FAK Y397 (44-624G) from Invitrogen; AMOTL1 p-S262 Covalab (pab0956-P, Lyon, France); and Tead2 Covalab (pab0961-P, Lyon, France).
Couderc C., Boin A., Fuhrmann L., Vincent-Salomon A., Mandati V., Kieffer Y., Mechta-Grigoriou F., Del Maestro L., Chavrier P., Vallerand D., Brito I., Dubois T., De Koning L., Bouvard D., Louvard D., Gautreau A, & Lallemand D. (2016). AMOTL1 Promotes Breast Cancer Progression and Is Antagonized by Merlin. Neoplasia (New York, N.Y.), 18(1), 10-24.
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5

Western Blot Analysis of Protein Fractions

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Nuclear and cytosplasmic fractions were separated with NE-PER extraction reagents, following the manufacturer’s instructions (Thermo Scientific). Protein yield was quantified via Coomassie Blue assay (Pierce), diluted in PBS, and combined with Laemmli sample buffer/2.5% β mercaptoethanol (1:1) (Bio Rad). Samples were heated to 95°C for 10 minutes and directly placed on ice. 10 ug protein were loaded to Criterion Stain-free gels and electrophoresed for 1 hour at 200v in 1X Tris/Glycine/SDS buffer (Bio Rad). Protein was transferred to PVDF membranes on a Trans-blot turbo transfer system following manufacturer’s instructions (Bio Rad) then blocked for 1 hour in 5% milk and TBST (0.1% tween). Membrane was incubated with primary antibody overnight at 4°C (1:200, Hmox 1: ab13243 (Abcam), actin: a2228 (Sigma) and Nrf2 sc-722 (Santa Cruz Biotechnology)) followed by secondary antibody at 1:10,000 concentration for one hour r.t. (HRP conjugated goat α rabbit, Invitrogen 31460). The membrane was developed with SuperSignal West Pico PLUS Chemiluminescent substrate (Thermo Scientific) and imaged for both total protein and HRP signal on a BioRad ChemiDoc MP imaging system.
Fulton R.E., Pearson-Smith J.N., Huynh C.Q., Fabisiak T., Liang L.P., Aivazidis S., High B.A., Buscaglia G., Corrigan T., Valdez R., Shimizu T, & Patel M.N. (2021). Neuron-specific mitochondrial oxidative stress results in epilepsy, glucose dysregulation and a striking astrocyte response. Neurobiology of disease, 158, 105470.
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6

Western Blot Analysis of Protein Markers

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Proteins were extracted as previously described. 30 Protein (20 µg of total protein lysate per sample) was subjected to western blot (WB) analysis using standard protocols. EZH2 (#5246) and SLUG (#9585) antibodies were purchased from Cell Signaling Technology (USA); YY1 (ab109237), integrinβ3 (ab75872) and c-myc (ab32072) antibodies were obtained from Abcam (USA). Actin (A2228), used to normalize protein expression, was purchased from Sigma Aldrich (Italy). The secondary antibodies anti-rabbit and anti-mouse were purchased from Santa Cruz Biotechnology (USA).
Dagrada G., Rupel K., Zacchigna S., Tamborini E., Pilotti S., Cavalleri A., Fechner L.E., Laurini E., Smith D.K., Brich S, & Pricl S. (2018). Self-Assembled Nanomicelles as Curcumin Drug Delivery Vehicles: Impact on Solitary Fibrous Tumor Cell Protein Expression and Viability. Molecular pharmaceutics, 15(10).
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