Sm22a

Manufactured by Proteintech

Sourced in United States

SM22a is a protein that is commonly used as a marker for smooth muscle cells. It is a 22 kDa protein that is involved in the regulation of actin cytoskeleton dynamics. The SM22a protein is expressed in vascular smooth muscle cells and plays a role in maintaining the contractile phenotype of these cells.

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Lab products found in correlation

Proliferating cell nuclear antigen (pcna), by Cell Signaling Technology (1 mentions) β actin, by Cell Signaling Technology (1 mentions) Geldoc go, by Bio-Rad (1 mentions) Calponin, by Bioss Antibodies (1 mentions) Actg2, by Bioss Antibodies (1 mentions) Mmp 9, by Abcam (1 mentions)

2 protocols using sm22a

Western Blot of Cell Signaling Proteins

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Protein extracted from cells was denatured at 95 °C, reduced with sample buffer (0.1 mol/L Tris, pH 6.8, 40% glycerol, 2% SDS, 2% beta-mercaptoethanol and 0.02% bromophenol blue) and separated by SDS-PAGE. Then, the proteins were blotted onto a nitrocellulose membrane, which was blocked in 5% BSA and incubated with primary antibodies against calponin (CNN1, Proteintech, 24844-1-AP, USA), transgelin (SM22a, Proteintech, 10493-1-AP, USA), osteopontin (OPN, Proteintech, 22952-1-AP, USA), proliferating cell nuclear antigen (PCNA, Cell Signaling Technology, 13110, USA) and β-actin (Cell Signaling Technology, 4970, USA) overnight. Subsequently, the membranes were treated with HRP-conjugated light chain-specific detection antibody (1:5000, Weiao Biotech, China) for 1 h. The membranes were developed using chemiluminescence (Millipore, WBLUF0500) on an Xograph processor (Bio-Rad Laboratories, GelDoc Go, Germany).

Wang R., Lu J., Yin J., Chen H., Liu H., Xu F., Zang T., Xu R., Li C., Wu Y., Wu Q., Fei X., Zhu M., Shen L, & Ge J. (2022). A TEMPOL and rapamycin loaded nanofiber-covered stent favors endothelialization and mitigates neointimal hyperplasia and local inflammation. Bioactive Materials, 19, 666-677.

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Protein Expression Profiling of Smooth Muscle Cells

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Total protein content of the cell was separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose membranes. Blots were blocked using 5% non-fat milk supplemented with 0.1% Tween 20. Subsequently, the blots were incubated with primary antibodies against ACTG2 (1:500, bioss), SM22a (1:500, Proteintech), SMA (1:800, bioss), calponin (1: 2,000, bioss), MYH (1:1,000, Proteintech), MMP-2 (1:500, abcam), and MMP-9 (1:500, abcam) followed by incubation with secondary antibodies. The images were analyzed using ImageJ.

Wang W., Wang Y., Piao H., Li B., Zhu Z., Li D., Wang T, & Liu K. (2021). Bioinformatics Analysis Reveals MicroRNA-193a-3p Regulates ACTG2 to Control Phenotype Switch in Human Vascular Smooth Muscle Cells. Frontiers in Genetics, 11, 572707.

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