Anti α smooth muscle actin anti α sma

Manufactured by Merck Group

Sourced in United States

Anti-α-smooth muscle actin (anti-α-SMA) is a laboratory reagent used in research applications. It is a monoclonal antibody that specifically binds to the alpha-smooth muscle actin protein, which is a structural component of smooth muscle cells. This antibody is commonly used in immunohistochemistry and Western blot analyses to detect and visualize the presence of alpha-smooth muscle actin in various biological samples.

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Lab products found in correlation

Anti α tubulin, by Merck Group (2 mentions) Anti type 1 collagen, by Southern Biotech (2 mentions) Dab 3 3 diaminobenzidine, by Merck Group (1 mentions) Avidin biotin peroxidase system, by Vector Laboratories (1 mentions) Anti β actin, by Merck Group (1 mentions) Anti α tubulin, by Santa Cruz Biotechnology (1 mentions) Anti vimentin, by Merck Group (1 mentions) Anti p21, by Santa Cruz Biotechnology (1 mentions) Anti gapdh, by Thermo Fisher Scientific (1 mentions) Anti sirt1, by Santa Cruz Biotechnology (1 mentions) Anti β actin, by Santa Cruz Biotechnology (1 mentions) Anti phospho smad2, by Cell Signaling Technology (1 mentions) Anti p300, by Santa Cruz Biotechnology (1 mentions) Anti cd31, by Bio-Rad (1 mentions) Anti ki67, by Abcam (1 mentions) Anti pparδ, by Abcam (1 mentions)

Close spelling variants of this product

Anti-actin (1282 citations) α-SMA (473 citations) Anti-α-SMA (213 citations) α-actin (101 citations) α-smooth muscle actin (74 citations) α-smooth muscle actin (α-SMA, (38 citations) Anti-α-smooth muscle actin (36 citations) Anti-α-actin (34 citations) Anti-SMA (34 citations) Anti-α-smooth muscle actin (α-SMA) (16 citations)

5 protocols using anti α smooth muscle actin anti α sma

Immunohistochemical Analysis of Renal Tissue

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Renal tissue sections were deparaffinized and incubated with primary monoclonal antibodies anti-α-smooth muscle actin (anti-α-SMA) (1 : 1000 – Sigma-Aldrich, S. Louis, MO.) overnight at 4°C and anti-proliferating cell nuclear antigen (anti-PCNA) (1 : 1000 – Sigma-Aldrich, S. Louis, MO.) for 30 min at room temperature. The sections were then subjected to further incubation with a secondary mouse anti-IgG antibody (1 : 200 – monoclonal – Vector Laboratories; Burlingame, CA). Immunohistochemical staining was detected by an avidin-biotin-peroxidase system (Vector Laboratories; Burlingame, CA), stained with DAB (3,3 diaminobenzidine) (Sigma; Israel), and the sections were counterstained with methyl green.

França-Silva N., Oliveira N.D, & Balbi A.P. (2015). Morphofunctional renal alterations in rats induced by intrauterine hyperglycemic environment. Archives of Medical Science : AMS, 12(2), 243-251.

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Quantitative Analysis of Collagen and SMA

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At the end of the experiments, fibroblast cultures were harvested, and whole cell protein lysates were subjected to Western blot analysis. The following antibodies were used: anti–type I collagen (SouthernBiotech), anti–α-smooth muscle actin (anti–α-SMA) (Sigma), anti-GAPDH (Zymed), and anti–α-tubulin (Sigma). Bands were visualized using enhanced chemiluminescence reagents (Pierce), and images were captured using a Fujifilm (Fuji). In each sample, band intensities were quantified with ImageJ software and normalized to GAPDH.

Fang F., Marangoni R.G., Zhou X., Yang Y., Ye B., Shangguang A., Qin W., Wang W., Bhattacharyya S., Wei J., Tourtellotte W.G, & Varga J. (2016). Toll-like Receptor 9 Signaling Is Augmented in Systemic Sclerosis and Elicits Transforming Growth Factor β–Dependent Fibroblast Activation. Arthritis & rheumatology (Hoboken, N.J.), 68(8), 1989-2002.

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Western Blot Analysis of Cellular Markers

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Western blot analysis was performed as previously described37 (link) utilizing the following antibodies: anti-α-smooth muscle actin (anti-α-SMA) (1:20,000 dilution, Sigma-Aldrich Corporation, St Louis, MO, USA), anti-vimentin (1:1,000 dilution, Sigma-Aldrich Corporation, St Louis, MO, USA), anti-phosphorylated-chk2 (anti-p-chk2) (1:1,000 dilution, Cell Signaling Technology, Inc., Danvers, MA, USA), anti-p21 (1:1,000 dilution; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), anti-proliferating cell nuclear antigen (anti-PCNA) (1:20,000 dilution, DAKO, Carpinteria, CA, USA), anti-β-actin (1:20,000 dilution, Sigma-Aldrich Corporation, St Louis, MO, USA), anti-acetylated α-tubulin (anti-ac-α-tubulin) (1:10,000 dilution, Sigma-Aldrich Corporation, St Louis, MO, USA), anti-α-tubulin (1:10,000 dilution, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), anti-α-tubulin acetyltransferase 1 (anti-α-TAT1) (1:1,000 dilution, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), anti-histone deacetylase 6 (anti-HDAC6) (1:2,000 dilution, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), and anti-glyceraldehyde-3-phosphate dehydrogenase (anti-GAPDH) (1:20,000 dilution; Novus Biologicals LLC, Littleton, CO, USA).

Han S.J., Kim J.H., Kim J.I, & Park K.M. (2016). Inhibition of microtubule dynamics impedes repair of kidney ischemia/reperfusion injury and increases fibrosis. Scientific Reports, 6, 27775.

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Protein Expression Analysis in Cell Cultures

Cited 1 time

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At the end of the incubation periods, cultures were harvested, and equal amounts of whole-cell lysates (5–15 µg) were subjected to electrophoresis in Tris–glycine 4–15% gradient gels and transferred to PVDF membranes (15 (link)). Membranes were incubated with the primary antibodies anti–type I collagen (1:400; SouthernBiotech), anti–phospho-Smad2 (1:1,000; Cell Signaling Technology), anti-SIRT1, anti–histone H4, anti–β-actin, and anti-p300 (all 1:200; all from Santa Cruz Biotechnology), anti–α-smooth muscle actin (anti–α-SMA) and anti–α-tubulin (both 1:3,000; both from Sigma), and anti-GAPDH (1:3,000; Invitrogen), followed by appropriate secondary antibodies. Antigen–antibody complexes were visualized by enhanced chemiluminescence (Pierce). Protein levels were quantitated by determining band intensities normalized to loading controls in each lane using ImageJ software (http://rsb.info.nih.gov/ij/).

Wei J., Ghosh A.K., Chu H., Fang F., Hinchcliff M.E., Wang J., Marangoni R.G, & Varga J. (2015). The Histone Deacetylase Sirtuin 1 Is Reduced in Systemic Sclerosis and Abrogates Fibrotic Responses by Targeting Transforming Growth Factor β Signaling. Arthritis & rheumatology (Hoboken, N.J.), 67(5), 1323-1334.

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Protein Expression in Heart Tissues

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Heart tissues were suspended in a protein lysis buffer; then, the proteins were transferred to nitrocellulose membranes. Blots were probed using the following primary antibodies: polyclonal anti-transforming growth factor-beta 2 (TGF-β2), anti-collagen I (Calbiochem, Darmstadt, Germany), anti-PPAR-δ (Abcam, Cambridge, UK), anti-osteoblast cadherin (OB-cad) (Cell Signaling, Dallas, TX, USA), anti-α-smooth muscle actin (anti-α-SMA; Sigma-Aldrich, Saint Louis, MO, USA), anti-Ki67 (Abcam, Cambridge, UK), and anti-CD31 (AbD Serotec, Raleigh, NC, USA). The blots were visualized using secondary antibodies with an enhanced chemiluminescence kit. Northern blot analysis was employed for investigating TGF-β1 and -β2 mRNA expression.

Park J.R., Ahn J.H., Jung M.H., Koh J.S., Park Y., Hwang S.J., Jeong Y.H., Kwak C.H., Lee Y.S., Seo H.G., Kim J.H, & Hwang J.Y. (2016). Effects of Peroxisome Proliferator-Activated Receptor-δ Agonist on Cardiac Healing after Myocardial Infarction. PLoS ONE, 11(2), e0148510.

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