Snail1

Manufactured by Abcam

Sourced in United States, United Kingdom

Snail1 is a protein that plays a role in the regulation of cell-cell adhesion and the epithelial-mesenchymal transition (EMT) process. It functions as a transcriptional repressor of E-cadherin expression.

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Lab products found in correlation

Vimentin, by Abcam (7 mentions) E cadherin, by Abcam (6 mentions) N cadherin, by Abcam (6 mentions) Snail2, by Abcam (3 mentions) Twist1, by Abcam (3 mentions) P erk1 2, by Cell Signaling Technology (2 mentions) E cadherin, by BD (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions) Il20rb, by Abcam (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions) Cytochrome c, by Abcam (1 mentions) Histone h2b, by Abcam (1 mentions) P erk, by Santa Cruz Biotechnology (1 mentions) β actin, by Santa Cruz Biotechnology (1 mentions) Bcl 2, by Abcam (1 mentions) Twist2, by Abcam (1 mentions) Draq5tm, by Thermo Fisher Scientific (1 mentions) Cxcr4, by R&D Systems (1 mentions) Pdgfb, by Santa Cruz Biotechnology (1 mentions) Il 6r, by Abcam (1 mentions)

15 protocols using snail1

Protein Expression Analysis of IL20RB Knockdown

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Total protein was extracted from the cells 24 h after transfection with si-IL20RB, and
the concentration was measured by the BCA method. Twenty micrograms of protein from each
sample was subjected to SDS-PAGE and electrotransferred onto PVDF membranes. The membrane
was incubated with 5% skim milk powder for 1 h at room temperature and then incubated with
the primary antibodies, GAPDH (1:1,000, Cell Signaling Technology Inc., Beverly, MA, USA),
IL20RB, E-cadherin, N-cadherin, Vimentin, Snail1, and Snail2 (1:1,000, Abcam, Cambridge,
MA,USA) at 4°C overnight. The membrane was washed with PBS three times and then incubated
with the secondary antibodies (1:1,000, Cell Signaling Technology Inc.) for 1 h at room
temperature. The signal of the protein was visualized by ECL. Quantity One software was
used to measure the relative expression of the protein, and GAPDH was used as the internal
control.

Cui X.F., Cui X.G, & Leng N. (2019). Overexpression of interleukin-20 receptor subunit beta (IL20RB) correlates with cell proliferation, invasion and migration enhancement and poor prognosis in papillary renal cell carcinoma. Journal of Toxicologic Pathology, 32(4), 245-251.

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Protein Expression Analysis Protocol

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After transfer process, the primary antibodies against CHOP purchased from Cell Signaling Technology; Danvers, MA, USA, Bcl-2, cytochrome c, Snail1, Zeb1, and histone H2B purchased from Abcam; and PKC, MEK, p-ERK, ERK, and β-actin purchased from Santa Cruz Biotechnology, Santa Cruz, CA, USA were maintained overnight at 4 °C. As detailed in previous research [70 (link)].

Yun H.J., Kim M., Kim S.Y., Fang S., Kim Y., Chang H.S., Chang H.J, & Park K.C. (2022). Effects of Anti-Cancer Drug Sensitivity-Related Genetic Differences on Therapeutic Approaches in Refractory Papillary Thyroid Cancer. International Journal of Molecular Sciences, 23(2), 699.

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Quantitative Analysis of RNA-Protein Interactions

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RNA immunoprecipitation assay (RIP) assays were performed as described previously 15. RIP products were analyzed by qRT‐PCR. A total quantity of 5 μg Snail1 (Abcam), Snail2 (Abcam), ZEB1 (Abcam), ZEB2 (Abcam), Twist1 (Abcam), or Twist2 (Abcam) antibodies were used for RIP reaction.

Jia X., Wang Z., Qiu L., Yang Y., Wang Y., Chen Z., Liu Z, & Yu L. (2016). Upregulation of LncRNA‐HIT promotes migration and invasion of non‐small cell lung cancer cells by association with ZEB1. Cancer Medicine, 5(12), 3555-3563.

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Comprehensive Immunofluorescence Antibody Panel

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Hoechst 33342 and anti-β-actin and anti-SDF-1 antibodies were purchased from Sigma-Aldrich (Sigma-Aldrich, St. Louis, MO). Draq5^TM was purchased from eBioscience (San Diego, CA). Antibodies against ATR, Rad51, IL-6R, GP130, pATM (Ser1981), TWIST1, SNAIL1, N-cadherin and vimentin were from Abcam Inc. (Abcam, Cambridge, MA). Antibody against fibronectin was obtained from BD Pharmigen (BD Biosciences, San Diego, CA). ATM, AKT, pAKT (Ser 473), pATR (Ser428), ZEB1, SNAIL2 (SLUG), E-cadherin and β-catenin antibodies were purchased from Cell Signaling Technology Inc., (Danvers, MA). Antibodies against 53BP1 and γH2AX (Ser139) were obtained from EMD Millipore (Darmstadt, Germany). Rad51, PDGFB and ATR antibodies were from Santa Cruz biotechnology, (Dallas, TX). CXCR4, PDGFRα and PDGFRβ antibodies and human IL-6 ELIZA kit were from R&D (Minneapolis, MN). Secondary antibodies conjugated with Alexa^® −488, −546, and −680 were from Molecular Probes (Invitrogen, Carlsbad, CA).
HSP90 inhibitor ganetespib [3–(2,4–dihydroxy–5–isopropylphenyl)–4–(1–methyl–1H–indol–5–yl)–1H– 1,2,4–triazol–5(4H)–one] was generously provided by Synta Pharmaceuticals Corp. (Lexington, MA).

Gomez-Casal R., Epperly M.W., Wang H., Proia D.A., Greenberger J.S, & Levina V. (2015). Radioresistant human lung adenocarcinoma cells that survived multiple fractions of ionizing radiation are sensitive to HSP90 inhibition. Oncotarget, 6(42), 44306-44322.

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Protein Expression Analysis by Western Blot

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After digestion and centrifugation of the cells, protein concentration was determined by bicinchoninic acid kit (BCA, Beyotime Biotechnology, Beijing, China). 100 μg proteins were applied onto 12.5% SDS polyacrylamide gel (SDS-PAGE) for electrophoresis and then transferred onto nitrocellulose membrane, and probed with the primary antibodies (CSN6, 1: 2000, Enzo Life Sciences; Snail1, 1: 1500, ABCAm; β-actin, 1: 2000, Zhong-shan biotech). After incubating overnight at 4 °C with the primary antibody, membranes were washed with TBS/0.05% Tween-20 (TBST) and incubated with a secondary antibody (1:10000, VICMED) for 2 hours at room temperature. The membranes were then washed and scanned on the chemiluminescence imaging analysis system (Tanon, Biotechnology, Shanghai, China).

Mou J., Wei L., Liang J., Du W, & Pei D. (2020). CSN6 promotes the cell migration of breast cancer cells by positively regulating Snail1 stability. International Journal of Medical Sciences, 17(17), 2809-2818.

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Western Blot Analysis of EMT Markers

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Total protein was isolated from the cells with RIPA lysis buffer (Cat.No:KGP702, KeyGEN, Nanjing, China). Twenty micrograms of protein per well was electrophoresed in 10% SDS-PAGE gels and then transferred to polyvinylidene difluoride membranes (Cat.No:ISEQ00010, Millipore, Bedford, MA, U.S.A.). The membranes were incubated with different primary antibodies, including E-cadherin (dilution 1:3000, Cat.No:ab76055, Abcam, the U.K.), N-cadherin (dilution 1:3000, Cat.No:ab76057, Abcam, the U.K.), Vimentin (dilution 1:3000, Cat.No:ab92547, Abcam, the U.K.), Snail-1 (dilution 1:3000, Cat.No:ab53519, Abcam, the U.K.), Twist-1 (dilution 1:3000, Cat.No:ab175430, Abcam, the U.K.), Smad-3 (dilution 1:3000, Cat.No:ab40854, Abcam, the U.K.), MMP2 (dilution 1:3000, Cat.No:ab37150, Abcam, the U.K.), MMP9 (dilution 1:3000, Cat.No:ab58803, Abcam, the U.K.) and GAPDH (dilution 1:30000, Cat.No:ab181602, Abcam, the U.K.), at 4°C overnight and then incubated with secondary antibodies (dilution 1:30000, Cat.No:ab97051, Abcam, the U.K.). The bands were visualized with ECL reagent (Cat.No:32134, Thermo Fisher Scientific, U.S.A.) and GAPDH was used as the loading control.

Yuan Y., Wang J., Xu M., Zhang Y., Wang Z., Liang L, & Sun P. (2020). 20(S)-ginsenoside Rh2 as agent for the treatment of LMN-CRC via regulating epithelial–mesenchymal transition. Bioscience Reports, 40(3), BSR20191507.

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Western Blot Analysis of Cell Signaling Proteins

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Primary antibodies were obtained from the following companies: (1) TRIM66, PCNA, caspase7, caspase9, MMP2, MMP19, Twist11, CDH1, Snail1, Snail2, ZEB1 and TGF-β1, Abcam; (2) p-Smad4, Thermo Fisher; (3) p53, p-Smad2, Smad2, Smad4 and GAPDH, CST Biotech. Horseradish peroxidase-conjugated goat anti-mouse secondary antibody or goat anti-rabbit secondary antibody was purchased from Beyotime.
Treated and untreated cells were lysed in RIPA lysis buffer with fresh added protease inhibitor cocktail (Sigma). Protein concentration was assayed using BCA protein assay (Thermo Fisher). Equal amounts of protein were then subjected to SDS gel electrophoresis. Following SDS-PAGE, proteins were transferred to a nitrocellulose membrane and immunoblotted with the respective antibodies. Signals were developed by enhanced chemiluminescence (ECL, Millipore). Band intensities were measured using Image J (NIH) and normalized to GAPDH.

Chen Y., Guo Y., Yang H., Shi G., Xu G., Shi J., Na Y, & Chen D. (2015). TRIM66 overexpresssion contributes to osteosarcoma carcinogenesis and indicates poor survival outcome. Oncotarget, 6(27), 23708-23719.

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Agrin Signaling Pathway Analysis

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Agrin (D2) and rabbit (H-300), Lrp4, Cdc42, N-WASP (western blot (WB) dilution—1:100) and anti-GFP (WB dilution—1:1,000) antibodies were obtained from Santa Cruz Biotechnology Inc., Santa Cruz, CA), Antibodies against Na+/K+ ATPase, Rab5, integrin β1, cleaved caspase-3, total FAK, cortactin, pSrc, total Src, pPI3-K, total PI3-K, pAkt, total Akt, pERK1/2 and total ERK1/2 were obtained from Cell Signaling Technology (dilution for WB—1:1,000). Antibodies against pFAK pY397, caveolin-1, Ki67, E-cadherin, N-cadherin and Vimentin were purchased from BD Biosciences, San Jose, CA (WB dilution—1:500). PF-562271, glypican-3, flotillin-1, Arp2/3 subunit 1B, pFAK (pY397), Snail-1 and MuSK antibodies were obtained from Abcam (dilution for WB—1:500). Phospho-tyrosine monoclonal antibody 4G10, Agrin monoclonal antibody MAb5204, p34Arc, GFP and EGFP antibodies were obtained from Millipore, Billerica, MA (WB dilutions—1:1,000). Agrin polyclonal rabbit antibody, OKT-9 hybridoma cells producing anti-CD-71 antibody and fibronectin antibody were obtained from Sigma, St Louis, MO. Recombinant rat Agrin protein residues was obtained from R&D systems and My Biosource, Inc, San Diego, CA. Recombinant CTxB, Alexa 488 and 555 conjugated secondary antibodies were from purchased Molecular Probes, Invitrogen, Carlsbad, CA.

Chakraborty S., Lakshmanan M., Swa H.L., Chen J., Zhang X., Ong Y.S., Loo L.S., Akıncılar S.C., Gunaratne J., Tergaonkar V., Hui K.M, & Hong W. (2015). An oncogenic role of Agrin in regulating focal adhesion integrity in hepatocellular carcinoma. Nature Communications, 6, 6184.

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Evaluating CA4's Molecular Effects on EMT

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The cells were pre-treated with 5 concentrations of CA4 (0, 1, 2, 5, or 10 μM). CA4 with 0 μM acted as a control group. After 2-h treatment, the cells in each sample were lysed with lysis buffer (150 mM NaCl, 50 mM Tris-HCl [pH 8.0], 0.1% SDS, and 1% Triton X-100) for 30 min. The protein concentration was determined by using a Bicinchoninic Acid (BCA) assay kit (Thermo Scientific^®, Rockford, IL). Equivalent amounts of whole-cell extracts from each sample were resolved over sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to nitrocellulose membranes. The membranes were blocked within the blocking buffer (5% non-fat milk) for 2 h at room temperature and then incubated in primary antibody (N-Cadherin, ZEB1, p-PI3K, PI3K, p-Akt, Akt, and GAPDH were purchased from Santa Cruz Biotechnology, Santa Cruz, CA; E-cadherin, Vimentin, Snail1, Slug, and Twist1 were obtained from Abcam, Cambridge, MA) at 4°C overnight. The membranes were then incubated with the secondary antibody horseradish peroxidase (HRP) conjugate for 1 h. Blots were visualized by enhanced chemiluminescence (ECL) method.

Liang W., Lai Y., Zhu M., Huang S., Feng W, & Gu X. (2016). Combretastatin A4 Regulates Proliferation, Migration, Invasion, and Apoptosis of Thyroid Cancer Cells via PI3K/Akt Signaling Pathway. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 22, 4911-4917.

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Immunofluorescence Staining of Pancreatic Tumors

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OCT-embedded frozen pancreatic tumors from KPC and KPCA^−/− mice were sectioned and fixed in 4% paraformaldehyde for 10 min. The tumor sections were incubated in PBS containing 0.1% Triton X-100 for 5 min and then washed with PBS. Then, the tumor sections were blocked with 10% normal goat or donkey serum in PBS for 1 hour. Next, the tumor sections were incubated with antibodies against Sema3D (Abnova), PlxnD1 (Novus), Sema3A (Abcam), Snail1 (Abcam), NG2 (Chemicon), or AnxA2 (Cell Signaling) at a dilution of 1:25, 1:50 (Snail1), 1:300 (NG2), or 1:100 (AnxA2) in 10% normal goat or donkey serum overnight at 4°C. After the overnight incubation, the tumor sections were washed and were further incubated with FITC-conjugated goat antibodies against rabbit immunoglobulin G (IgG), FITC-conjugated goat antibodies against mouse IgG (Southern Biotechnology), or AF594-conjugated donkey antibodies against rabbit IgG (Life Technologies) at a 1:200 dilution or according to the manufacturer’s instructions (AF594) in 10% normal goat or donkey serum at room temperature for 1 hour. NG2 staining was performed according to a previously described protocol (42 (link)). The tumor sections were subsequently washed and mounted in medium containing DAPI (4′,6-diamidino-2-phenylindole) (Vector Labs) before being examined under a fluorescence microscope.

Foley K., Rucki A.A., Xiao Q., Zhou D., Leubner A., Mo G., Kleponis J., Wu A.A., Sharma R., Jiang Q., Anders R.A., Iacobuzio-Donahue C.A., Hajjar K.A., Maitra A., Jaffee E.M, & Zheng L. (2015). Semaphorin 3D autocrine signaling mediates the metastatic role of annexin A2 in pancreatic cancer. Science signaling, 8(388), ra77.

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