Sc 7210

Manufactured by Santa Cruz Biotechnology

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Sc-7210 is a laboratory equipment product manufactured by Santa Cruz Biotechnology. It is designed for general laboratory use.

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10 protocols using sc 7210

Protein Expression Analysis of Spinal Cord Tissue

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The collected 100 mg of spinal cord tissue from rats in all 7 groups was washed with phosphate-buffered saline (PBS). The total protein amount was extracted according to the procedural instructions provided by the tissue protein extraction kit (No. P060091; Shanghai Andi Biotechnology Co., Ltd, Shanghai, China) and separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Next, the total protein was electrically transferred onto a polyvinylidene fluoride (PVDF) membrane for detection. Antibodies were used at the following dilution ratios: rat anti-PTC1 (Santa Cruz; SC-6147; 1: 1000), rat anti-PTC2 (Proteintech; 55091-1-AP; 1: 1000), rat anti-Shh (Santa Cruz; SC-365112; 1: 1000), rat anti-Gli-1 (Santa Cruz; SC-515751; 1: 1000) and rat anti-β-actin (Santa Cruz; SC-7210; 1: 800) served as an internal reference. Membranes were incubated overnight at 4 °C and then added to horseradish peroxidase (HRP)-marked secondary antibodies (1: 200; #3999; cell signaling) for 2 h at room temperature. The gel imaging system (Gel Doc XR+, Bio-Rad Laboratories, Inc., Hercules, CA, USA) was used to obtain photographs, and ImageJ software was used to test gray levels.

Zhang Y.D., Zhu Z.S., Zhang D., Zhang Z., Ma B., Zhao S.C, & Xue F. (2017). Lentivirus-mediated silencing of the PTC1 and PTC2 genes promotes recovery from spinal cord injury by activating the Hedgehog signaling pathway in a rat model. Experimental & Molecular Medicine, 49(12), e412-.

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Ellagic Acid Modulates Liver Protein Expression

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Following treatment with ellagic acid, liver tissue samples were acquired and homogenized for 10 sec at 12,000 × g for 10 min at 4°C. Total protein was measured using a BCA assay reagent (Beyotime Institute of Biotechnology), and then 50 µg protein was subjected to 10–12% SDS-PAGE and electrotransferred onto a polyvinylidene difluoride membrane (BD Biosciences, San Jose, CA, USA). The membrane was blocked in 5% non-fat milk in phosphate-buffered saline (PBS; pH 7.4) for 2 h, and subsequently incubated overnight at 4°C with the following primary antibodies: Anti-inducible nitric oxide synthase (iNOS; 1:400; sc-649; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), anti-vascular endothelial growth factor (VEGF; 1:500; sc-13083; Santa Cruz Biotechnology, Inc.), anti-VEGF receptor 2 (VEGFR2; 1:3,000; ab11939; Abcam, Cambridge, UK) and β-actin (1:500; sc-7210; Santa Cruz Biotechnology, Inc.). Next, the membranes were washed with PBS and incubated with horseradish peroxidase-conjugated goat anti-mouse IgG secondary antibody (1:5,000; 7074; Cell Signaling Technology, Inc., Danvers, MA, USA) at room temperature for 2 h. Protein expression in the samples was detected by Amersham ECL Prime western blotting detection reagent (GE Healthcare Life Sciences, Piscataway, NJ, USA) and analyzed using AlphaEase FC (FluorChem FC2) software (Cell Biosciences Inc., Santa Clara, CA, USA).

Ding Y., Wang L., Song J, & Zhou S. (2017). Protective effects of ellagic acid against tetrachloride-induced cirrhosis in mice through the inhibition of reactive oxygen species formation and angiogenesis. Experimental and Therapeutic Medicine, 14(4), 3375-3380.

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Immunohistochemical Analysis of Soft Tissue Tumors

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The findings of different types of auxiliary examination, including computed tomography (CT), magnetic resonance imaging (MRI) scans and color Doppler ultrasound, were reviewed. A histopathological examination of paraffin-embedded surgical specimens was performed to confirm the diagnosis using standard hematoxylin and eosin staining and immunohistochemical techniques. Immunohistochemical staining was performed using a Dako EnVision System (Dako, Glostrup, Denmark), according to the manufacturer's instructions. The primary antibodies included rabbit polyclonal antibodies against vimentin (sc-5565; 1:200), cluster of differentiation (CD)34 (sc-9095; 1:100), actin (sc-7210; 1:200), desmin (sc-14026; 1:200), cytokeratin (CK; sc-134493; 1:100), S100 (sc-7849-R; 1:100), B-cell lymphoma 2 (bcl-2; sc-783; 1:200), CD99 (sc-241355; 1:200), CD117 (sc-3936; 1:200), epithelial membrane antigen (EMA; sc-6826; 1:200) and smooth muscle actin (SMA; sc-92040; 1:200; all Santa Cruz Biotechnology Inc., Dallas, TX, USA). 3,3′-diaminobenzidine was used as the chromogen.

Ge W., Yu D.C., Chen G, & Ding Y.T. (2016). Clinical analysis of 47 cases of solitary fibrous tumor. Oncology Letters, 12(4), 2475-2480.

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Protein Expression Analysis Protocol

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Cellular protein samples were isolated with a Protein Extraction Kit (Qiagen, GmbH, Hilden, Germany) according to the kit's manual and supplemented with a protease inhibitor cocktail (Abcam, Cambridge, UK). Protein samples were separated with 10% SDS-PAGE gel and were transferred to a polyvinylidene fluoride hydrophobic membrane (Millipore, Bedford, MA, USA). The membrane was blocked with 5% skimmed milk (Solarbio, Beijing, China) overnight at 4°C to cover the nonspecific binding sites. Then the membrane was inoculated with the rabbit anti-mouse KLF-4 (BM0485, Abzoom Biolabs, Dallas, TX, USA; 1 : 300), PAI-1 (sc-8979, Santa Cruz Biotechnology, Santa Cruz, CA, USA; 1 : 200), E-cadherin (sc-7870, Santa Cruz Biotechnology, Santa Cruz, CA, USA; 1 : 500), Collagen I (ab21286, Abcam, Cambridge, UK; 1 : 200), mouse anti-mouse α-Smooth Muscle Actin (α-SMA) (sc-53142, Santa Cruz Biotechnology, Santa Cruz, CA, USA; 1 : 200), or rabbit anti-mouse β-actin (sc-7210, Santa Cruz Biotechnology, Santa Cruz, CA, USA; 1 : 800) at room temperature for 2 hours. The specific binding to each protein marker was presented with the incubation with the peroxidase-conjugated secondary antibody (Promega, Madison, WI, USA) and the electrochemiluminescence (ECL) detection system (Amersham, Uppsala, Sweden). The protein level was presented as a ratio to β-actin.

Sun F, & Hu K. (2015). Krüppel-Like Factor 4 Inhibits the Transforming Growth Factor-β1-Promoted Epithelial-to-Mesenchymal Transition via Downregulating Plasminogen Activator Inhibitor-1 in Lung Epithelial Cells. Disease Markers, 2015, 473742.

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Liver Protein Analysis via Western Blot

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Frozen liver samples were homogenized in a buffer containing 10 mM Tris–HCl (pH 7.8), 2% SDS, 10 mM DTT, and proteinase inhibitors (Sigma) and centrifuged at 15,000× g for 20 min at 20 °C. Supernatants were collected, and the protein concentration was determined by Bradford assay. Tissue lysates containing 20 μg (liver) of total protein were separated by 10% SDS-PAGE and electroblotted onto Immobilon Transfer Membrane (Millipore Corporation, Billerica, MA, USA). The following antibodies were used: monoclonal antibody against HNF-1 (sc-393925, Santa Cruz Biotechnology, Inc. 10410 Finnell Street Dallas, TX, USA) and polyclonal antibody against Actin (sc-7210, Santa Cruz Biotechnology). HRP-conjugated secondary antibodies (sc-2030 and sc-2004) were obtained from Santa Cruz Biotechnology and the HAF019 from R&D Systems, Minneapolis, MN, USA) Immunodetection was accomplished with enhanced chemiluminescence using Western blotting Luminol Reagent (sc-2048, Santa Cruz Biotechnology add the location of company).

Sucajtys-Szulc E., Debska-Slizien A., Rutkowski B., Szolkiewicz M., Swierczynski J, & Smolenski R.T. (2022). Hepatocyte Nuclear Factor 1α Proinflammatory Effect Linked to the Overexpression of Liver Nuclear Factor–κB in Experimental Model of Chronic Kidney Disease. International Journal of Molecular Sciences, 23(16), 8883.

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Quantification of Autophagy Markers

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Cultured cells and fragments of the arterial wall were extracted by RIPA Lysis Buffer (Beyotime) containing protease and phosphatase inhibitors. Quantified samples with 30 μg total protein were separated on 12% SDS-ployacrylamide gel electrophoresis and transferred onto polyvinylidene difluoride membranes (Bio-Rad, Wattford, UK), which were blocked with 2% (wt/vol) bovine serum albumin in Tris-buffered saline solution containing 0.1% Tween-20 for 1 h. Membranes were incubated overnight at 4 °C with the primary antibodies for LC3 (1:1000 dilution; 2775 S) and SQSTM1/p62 monoclonal antibody (1:1000 dilution; 8025 S, both from Cell Signaling Technology), mouse monoclonal antibody against ACTIN (1:2000 dilution; sc-7210, Santa Cruz Biotechnology, Santa Cruz, CA, USA) and GAPDH, followed by peroxidase-conjugated secondary antibody (A0208, Beyotime) for 1 h at room temperature. After washing, signals were visualized using Super Signal West Pico Chemiluminescent Substrate (Pierce Biotechnology, Rockford, IL, USA). Western blots were prepared at least three times for each sample.

Dai S., Wang B., Li W., Wang L., Song X., Guo C., Li Y., Liu F., Zhu F., Wang Q., Wang X., Shi Y., Wang J., Zhao W, & Zhang L. (2016). Systemic application of 3-methyladenine markedly inhibited atherosclerotic lesion in ApoE−/− mice by modulating autophagy, foam cell formation and immune-negative molecules. Cell Death & Disease, 7(12), e2498-.

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Western Blotting of Cytosolic, Mitochondrial, and Membrane Proteins

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Western blotting was performed as previously described [41 (link)]. Briefly, protein samples (20 μg protein/lane) were separated by 12.5% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to a polyvinylidene difluoride membrane. Blots were separately probed with mouse monoclonal 3D5 anti-α-syn (1: 5000) and anti-Hb (1: 1000; ab77125, Abcam, MA, USA) primary antibodies, as well as rabbit polyclonal anti-actin (1: 1000; sc-7210, Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse monoclonal anti-voltage-dependent anion channel (1: 500; ab14734, Abcam, MA, USA), and rabbit polyclonal anti-calnexin (1: 1000; 2433s, Cell Signaling Technology, Danvers, MA, USA) antibodies as loading controls for cytosolic, mitochondrial, and membrane fractions, respectively. The blots were probed with appropriate secondary antibodies conjugated with horseradish peroxidase (1:5000; Vector Laboratories, Burlingame, CA, USA). Immunoreactivity was detected using enhanced chemiluminescence reagent (Promega, Madison, WI, USA).

Yang W., Li X., Li X., Li X, & Yu S. (2016). Neuronal hemoglobin in mitochondria is reduced by forming a complex with α-synuclein in aging monkey brains. Oncotarget, 7(7), 7441-7454.

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Liriodenine Modulates Cell Signaling in MCF-7 Cells

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In total, 1×10⁶ MCF-7 cells/well were seeded onto 6-well plates and treated with liriodenine (0, 0.1, 1 and 10 µM) for 48 h. According to the manufacturer's protocol, the cells were lysed using radioimmunoprecipitation assay buffer (Beyotime Institute of Biotechnology). The protein concentrations were determined using a bicinchoninic acid kit (Beyotime Institute of Biotechnology). Total protein (50 µg) was isolated with 10% SDS-PAGE and transferred to a nitrocellulose membrane. The nitrocellulose membrane was blocked with 5% skimmed milk powder in Tris-buffered saline with Tween-20 (TBST) for 1 h at room temperature, and incubated with antibodies against B-cell lymphoma-2 protein (dilution, 1:500; Bcl-2; sc-783), cyclin D1 (dilution, 1:500; sc-717), p53 (dilution, 1:500; sc-6243), vascular endothelial growth factor (dilution, 1:500; VEGF; sc-13083) and β-actin (dilution, 1:500; sc-7210; all Santa Cruz Biotechnology, Inc., Dallas, TX, USA) for 1 h at room temperature. The membrane was washed with TBST and incubated with secondary antibody mouse anti-rabbit IgG-HRP (sc-2357, dilution, 1:3,000; Santa Cruz Biotechnology, Inc.) at 37°C for 1 h, and then assessed by an BeyoECL Plus (P0018; Beyotime Institute of Biotechnology). The optical density was analyzed using Quantity One software (version 3.0; Bio-Rad Laboratories, Inc.).

Li Z.H., Gao J., Hu P.H, & Xiong J.P. (2017). Anticancer effects of liriodenine on the cell growth and apoptosis of human breast cancer MCF-7 cells through the upregulation of p53 expression. Oncology Letters, 14(2), 1979-1984.

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Quantifying HIF1α Protein Expression

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Protein samples were separated by sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDS−PAGE) and transferred to a nitrocellulose membrane. Western blots were performed with rabbit antibodies against HIF1α (NB100-479, Novus Biologicals, Inc., Littleton, CO) and β-actin (SC-7210, Santa Cruz Biotechnology, Inc., Dallas, TX). Proteins were visualized with horseradish peroxidase-conjugated goat anti-rabbit IgG (sc-2004, Santa Cruz Biotechnology, Inc.) and an ECL Western blot system (Pierce, Rockford, IL).

Hwang H.J., Lynn S.G., Vengellur A., Saini Y., Grier E.A., Ferguson-Miller S.M, & LaPres J.J. (2015). Hypoxia Inducible Factors Modulate Mitochondrial Oxygen Consumption and Transcriptional Regulation of Nuclear-Encoded Electron Transport Chain Genes. Biochemistry, 54(24), 3739-3748.

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Stroke-Induced APP Proteolysis Analysis

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The brain samples (penumbral and ischemic cortex) were collected at 6
and 24 h following stroke and were used for Western blot analysis according to a
previous study (Adegoke et al.2017). Blots were probed with an anti-BACE (1:1000, 5606S,
RRIDAB_1903900, Cell Signaling Technology), anti-Amyloid Precursor Protein
(C-terminal) (1:1000, A8717, RRIDAB_258409, Sigma-Aldrich), or anti-actin
(1:1000, sc-7210, RRID AB_2223518, Santa Cruz Biotechnology) antibody, or
appropriate secondary antibodies conjugated with fluorescent dyes (1:5000,
C-1003, LI-COR Inc., Lincoln, NE, USA). Protein band intensities were measured
using an Odyssey scanner (LI-COR) and quantified using UN-SCAN-IT gel6.1
software (Silk Scientific Inc., Orem, Utah, USA). The total APP level (APPtot)
was calculated as “APPtot = APPm + APPim” that
was normalized to actin, while the ratios of APPm/APPim and APP CTF/APPtot
normalized to actin were compared between each group.

Min J.W., Liu Y., Wang D., Qiao F, & Wang H. (2017). The non-peptidic δ-opioid receptor agonist Tan-67 mediates neuroprotection post-ischemically and is associated with altered amyloid precursor protein expression, maturation and processing in mice. Journal of neurochemistry, 144(3), 336-347.

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