Smurf2

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Smurf2 is a laboratory equipment product offered by Santa Cruz Biotechnology. It is a protein that plays a key role in the regulation of cellular processes. This product is designed to facilitate research and experimentation in the field of molecular biology.

Automatically generated - may contain errors

Lab products found in correlation

Smad7, by Santa Cruz Biotechnology (5 mentions) Smad3, by Santa Cruz Biotechnology (3 mentions) Phospho smad3, by Cell Signaling Technology (3 mentions) Phospho smad3, by Abcam (2 mentions) Collagen 1, by Southern Biotech (2 mentions) Irdye 800 conjugated secondary antibody, by Rockland Immunochemicals (2 mentions) β actin, by Santa Cruz Biotechnology (2 mentions) Smad3, by Thermo Fisher Scientific (2 mentions) Odyssey infrared imaging system, by LI COR (2 mentions) α sma, by Merck Group (2 mentions) Anti ha, by Abcam (1 mentions) Western blotting luminol reagent, by Santa Cruz Biotechnology (1 mentions) Smad2, by Santa Cruz Biotechnology (1 mentions) Anti tβri, by Abcam (1 mentions) Phospho smad2, by Santa Cruz Biotechnology (1 mentions) Anti flag, by Abcam (1 mentions) Anti β actin, by Merck Group (1 mentions) Nitrocellulose membrane, by Pall Corporation (1 mentions) Licor odyssey infrared image system, by LI COR (1 mentions) Total smad3, by Santa Cruz Biotechnology (1 mentions)

7 protocols using smurf2

Western Blot Analysis of SMAD Signaling

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Cells were lysed using protein extraction buffer at 48 h after transfection, and protein concentration was quantitated by BCA protein assay. Lysates (30 µg) were resolved by SDS/PAGE and transferred onto nitrocellulose membrane (Pall corporation, Port Washington, NY, USA). The following antibodies were purchased from Cell Signaling Technology (Danvers, MA, USA): SMAD2 (catalogue no. 5339); phospho‐SMAD2 (catalogue no. 3108); SMAD3 (catalogue no. 9523); p21 (catalogue no. 2947); Santa Cruz Biotechnology (Delaware, CA, USA): SMURF2 (catalogue no. sc‐25511); Na⁺/K⁺ ATPase α (catalogue no. sc‐48345), (AbFrontier, Seoul, Korea): anti‐β‐actin (catalogue no. LFPA0207), (Sigma‐Aldrich, St. Louis, MO, USA): anti‐HA (catalogue no. H6908); anti‐Flag (catalogue no. F1804), (Abcam, Cambridge, UK): anti‐TβRI (catalogue no. ab31013); phospho‐SMAD3 (catalogue no. ab52903). Western Blotting Luminol Reagent (Santa Cruz Biotechnology, Santa Cruz, CA, USA) was used to detect protein according to the manufacturer’s instructions. The membranes were visualized with an ATTO image analyzer (ATTO, Tokyo, Japan).

Chae D., Park J., Cho M., Ban E., Jang M., Yoo Y.S., Kim E.E., Baik J, & Song E.J. (2019). MiR‐195 and miR‐497 suppress tumorigenesis in lung cancer by inhibiting SMURF2‐induced TGF‐β receptor I ubiquitination. Molecular Oncology, 13(12), 2663-2678.

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Western Blot Analysis of Kidney Proteins

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Proteins from kidney tissues and cultured cells were extracted with RIPA lysis buffer, and western blot analysis was performed as described previously [10 (link)]. After blocking the nonspecific binding with 5% BSA (1h, room temperature), membranes were then incubated with the primary antibody against phospho-Smad3 (Cell Signaling Technology), collagen I (Southern Biotech), Smad7, Smurf2, total Smad3 (Santa Cruz Biotechnology), α-SMA, glyceraldehyde 3-phosphate dehydrogenase (Chemicon, Temecula, CA) overnight at 4°C, followed by the IRDye 800-conjugated secondary antibody (Rockland immunochemicals, Gilbertsville, PA). Signals were captured using the LiCor/Odyssey infrared image system (LI-COR Biosciences, Lincoln, NE) and the intensity of each band was quantified and analyzed by using the Image J software (NIH, Bethesda, MD, USA).

Meng X.M., Zhang Y., Huang X.R., Ren G.L., Li J, & Lan H.Y. (2015). Treatment of renal fibrosis by rebalancing TGF-β/Smad signaling with the combination of asiatic acid and naringenin. Oncotarget, 6(35), 36984-36997.

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Immunoprecipitation and Immunoblotting Assay

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Immunoprecipitation and immunoblotting were carried out as described previously [46 (link)]. The following antibodies were used: IRF3 (1:1000, Santa Cruz, sc-9082), p-IRF3 (1:1000, Cell Signaling, 4947S), OTUD1 (1:1000, Abcam, ab182511), Flag (1:5000, Sigma, F7425), β-actin (1:5000, Proteintech, 66009-1-Ig), Myc (1:5000, Abmart, m2002), MAVS (1:1000, Santa Cruz, sc-166583), TRAF3 (1:1000, Cell Signaling, 4729S), TRAF6 (1:1000, Abcam, ab94720), TBK1 (1:1000, Cell Signaling, 3013S), RIG-I (1:1000, Cell Signaling, 4200S), Smurf1 (1:1000, Santa Cruz, sc-100616), Smurf2 (1:1000, Santa Cruz, sc-25511), Ub (1:1000, Santa Cruz, sc-8017), HA (1:5000, Abcam, ab9110), K48-Ub (1:1000, Cell Signaling, 4289S), and VSVG (1:5,000, Santa Cruz, sc-66180).

Zhang L., Liu J., Qian L., Feng Q., Wang X., Yuan Y., Zuo Y., Cheng Q., Miao Y., Guo T., Zheng X, & Zheng H. (2018). Induction of OTUD1 by RNA viruses potently inhibits innate immune responses by promoting degradation of the MAVS/TRAF3/TRAF6 signalosome. PLoS Pathogens, 14(5), e1007067.

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Western Blot Analysis of Cardiac Proteins

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Total proteins from the left ventricle was isolated using RIPA lysis buffer, and Western blot was conducted as described before.⁶, ¹¹, ¹² Briefly, the membranes were blocked with 3% BSA, followed by incubation at 4°C for overnight with indicated primary antibodies including phospho‐NF‐κB/p65 (ser276), phospho‐IκBα (ser32), IκBα, phospho‐Smad3 (Cell Signaling Technology), Smad3, Smad7, Smurf2, NF‐κB/p65, β‐actin (Santa Cruz Biotechnology), collagen I and III (Southern Biotech), and α‐SMA (Sigma). Subsequently, the membranes were incubated with IRDye 800‐conjugated secondary antibody (Rockland Immunochemicals) and photographed with Odyssey infrared image system (LI‐COR Biosciences). Finally, the intensity of the bands was calculated by the Image J software and normalized against GAPDH.⁶, ¹¹, ¹²

Dong L., Li J., Hu Z., Huang X., Wang L., Wang H., Ma R.C., Lan H, & Yang S. (2021). Deletion of Smad3 protects against diabetic myocardiopathy in db/db mice. Journal of Cellular and Molecular Medicine, 25(10), 4860-4869.

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Protein Extraction and Western Blot Analysis from LV Tissues

Cited 1 time

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Protein from LV tissues was extracted with Radio-Immunoprecipitation Assay (RIPA) lysis buffer, and western blot analysis was performed as described previously.¹³ (link)^,¹⁶ (link)^,¹⁷ (link) In brief, after blocking nonspecific binding with 5% BSA, membranes were incubated overnight at 4°C with primary antibodies against collagen I (1310-01; Southern Biotech), collagen III (1330-01; Southern Biotech), α-smooth muscle actin (ab230458; Abcam), fibronectin (sc-6953; Santa Cruz Biotechnology), GAPDH (Chemicon; Merck), phospho-NF-κB/phospho-p65 (ab86299; Abcam), phospho-IkBα (#2859; Cell Signaling Technology), IkBα (sc-371; Santa Cruz Biotechnology), phospho-Smad3 (#9520; Cell Signaling Technology), Smad3 (51-1500; Invitrogen, Waltham, MA, USA), Smad7 (sc-11392; Santa Cruz Biotechnology), and Smurf2 (sc-393848; Santa Cruz Biotechnology). After being washed, the membranes were incubated with LI-COR IRDye 800-conjugated secondary antibodies, anti-mouse (#24849; Rockland Immunochemicals, Limerick, PA, USA) and anti-rabbit (#36595; Rockland Immunochemicals), in the dark for 1 h at room temperature. Signals were scanned and visualized by Odyssey Infrared Imaging System (Li-COR Biosciences, Lincoln, NE, USA). The ratio of the target protein was subjected to GAPDH and was quantified with ImageJ software (National Institutes of Health, Bethesda, MD, USA).

Meng J., Qin Y., Chen J., Wei L., Huang X.R., Yu X, & Lan H.Y. (2020). Treatment of Hypertensive Heart Disease by Targeting Smad3 Signaling in Mice. Molecular Therapy. Methods & Clinical Development, 18, 791-802.

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Renal Protein Quantification by Western Blot

Cited 5 times

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Total protein from renal cortical tissues were extracted by RIPA lysis buffe, and western blotting analysis was performed as previously described 15 (link)-18 (link), 20 (link)-22 (link), 24 (link). Antibodies used in this study included those against phospho-NF-κB/p65 (ser276) (Cell Signaling Technology, Berkeley, CA. cat# 3033), phospho-IκBα (ser32) (Cell Signaling Technology, cat# 2859), IκBα (Cell Signaling Technology, cat# 9242), phospho-Smad3 (Abcam, cat# ab52903), Smad3 (Invitrogen, cat# PA1-38613), Smad7 (Santa Cruz Biotechnology, cat# sc-9183), Smurf2 (Santa Cruz Biotechnology, cat# sc-2511), NF-κB/p65 (Cell Signaling Technology, cat# 8242), β-actin (Santa Cruz Biotechnology, cat# sc-47778), collagen I (Southern Biotech), FN (Abcam, cat# ab2413). After being incubated with the primary antibody at 4 °C overnight, the membrane was stained with the LI-COR IRDye 800-labeled secondary antibodies (1:3000, Rockland Immunochemicals, Gilbertsville PA, USA) for 1h. The signals were detected with Odyssey Infrared Imaging System (Li-COR Biosciences, Lincoln, NA, USA) and quantitated with Image J software (v1.48, NIH, USA). The intensity of the protein band was normalized against β-actin or total proteins as stated in the studies and expressed as the mean ± SEM.

He H., Wang H., Chen X., Zhong Y., Huang X.R., Ma R.C., Wang C, & Lan H.Y. (2024). Treatment for type 2 diabetes and diabetic nephropathy by targeting Smad3 signaling. International Journal of Biological Sciences, 20(1), 200-217.

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Molecular Mechanisms of Fibrosis Regulation

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SKI was purchased from Xi’an Century Shenkang Pharmaceutical Industry Co., Ltd. (Xi’an, China, 202102103). TGF-β1 (Santa Cruz, sc-130348), E-Cad (CST, #3195), P-Smad3 (Abclonal, A19115), P-Smad2/3 (Abclonal, A19115), Smurf2 (Santa Cruz, sc-518164), α-SMA (CST, #19245), collagen I (Abclonal, A5786), Smad7 (Santa Cruz, sc-365846), Smad2/3 (Santa Cruz, sc-133098), ubiquitin (Santa Cruz, sc-8017), TβR-I (Santa Cruz, sc-101574), TβR-II (Santa Cruz, sc-1700), Smad3 (Santa Cruz, sc-101154), serum creatinine (Scr), and blood urea nitrogen (BUN) assay kits were obtained from Nanjing Jiancheng Bioengineering Institute (Nanjing, China). Real-Time PCR Easy™- SYBR Green I (FOREGENE, QP-01014).

Zou J., Zhou X., Chen X., Ma Y, & Yu R. (2022). Shenkang Injection for Treating Renal Fibrosis-Metabonomics and Regulation of E3 Ubiquitin Ligase Smurfs on TGF-β/Smads Signal Transduction. Frontiers in Pharmacology, 13, 849832.

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