C parp

Manufactured by Cell Signaling Technology

Sourced in United States

C-PARP is a laboratory reagent used for the detection of cleaved Poly(ADP-ribose) Polymerase (PARP). PARP is a protein involved in DNA repair, and its cleavage is a marker of apoptosis (programmed cell death). C-PARP is a specific antibody that recognizes the cleaved form of PARP, allowing researchers to monitor and quantify apoptosis in experimental systems.

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Cleaved PARP (c-PARP), (9 citations) Anti-c-PARP (6 citations)

63 protocols using c parp

Comprehensive Protein Extraction and Analysis

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Protein extraction was conducted using RIPA buffer (Sigma-Aldrich, USA) supplemented with protease inhibitor cocktail Tablets (Roche, Switzerland) and Pierce^TM phosphatase inhibitor (Thermo Scientific, USA). The antibodies against p53 (#2524), p-p53 ser315 (#2528), Forkhead box protein O3 (FoxO3) (#2497), CDK1(#9116), B-cell lymphoma-2 (Bcl-2) family proteins (#98322, #9941), poly (ADP-ribose) polymerase (PARP) (#9542), c-PARP (#5625) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:1000, Cell Signaling Technology, Beverly, MA, USA) were used.

Yuan Y., Zhang X., Du K., Zhu X., Chang S., Chen Y., Xu Y., Sun J., Luo X., Deng S., Qin Y., Feng X., Wei Y., Fan X., Liu Z., Zheng B., Ashktorab H., Smoot D., Li S., Xie X., Jin Z, & Peng Y. (2022). Circ_CEA promotes the interaction between the p53 and cyclin-dependent kinases 1 as a scaffold to inhibit the apoptosis of gastric cancer. Cell Death & Disease, 13(9), 827.

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Immunoblot Analysis of Cell Signaling

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HCT116 cells were harvested, lysed on ice in RIPA buffer (Beyotime Institute of Biotechnology, Shanghai, China) and boiled. Protein concentration was measured by BCA protein assay kit (Beyotime Institute of Biotechnology, Shanghai, China). The protein samples were separated by SDS-PAGE and transferred to the membrane (Pall, New York, NY, USA). Afterwards, the membrane was immunoblotted with the corresponding primary antibody (C-parp (#5625), C-cas9 (#9505), C-cas3 (#9661), Bcl-2 (#4223), Bax (#5023), SHP2 (#3752), P-Erk1/2 (#9101) and Erk1/2 (#9102), 1:1000, Cell Signaling Technology, Danvers, MA, USA; Tubulin (#ET1602-4), 1:5000, HUABIO, Hangzhou, China) and the appropriate HRP-conjugated secondary antibody, and determined with ECL detection reagent (Thermo Scientific, Waltham, MA, USA).

Dai J., Zhang Y., Gao Y., Bai X., Liu F., Li S., Yu Y., Hu W., Shi T., Shi D, & Li X. (2022). Toward a Treatment of Cancer: Design and In Vitro/In Vivo Evaluation of Uncharged Pyrazoline Derivatives as a Series of Novel SHP2 Inhibitors. International Journal of Molecular Sciences, 23(7), 3497.

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CYT997 Protocol for Cellular Assays

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CYT997 (MF: C₂₄H₃₀N₆O₂, MW: 434.53, purity: 99.46%) was purchased from Selleckchem (Houston, TX, USA) and dissolved in dimethyl sulfoxide (DMSO) to prepare a 40 mM stock solution, which was stored at − 80 °C. DMSO was obtained from Sigma-Aldrich (St. Louis, MO, USA). 2′,7′-Dichlorodihydrofluorescein diacetate (DCFH-DA), N-acetylcysteine (NAC), 3-methyladenine (3-MA), chloroquine (CQ) and GSK2606414 were purchased from Sigma-Aldrich. EN460 was purchased from MedchemExpress (Monmouth Junction, NJ, USA). Antibodies against PARP, C-PARP, CASPASE-4, LC3B-I/II, BECLIN-1, PERK, P-PERK, EIF2A, P-EIF2A, CHOP, ERO1-Lα, and GAPDH were purchased from Cell Signaling Technology (Beverly, MA, USA).

Wang Z., Yin F., Xu J., Zhang T., Wang G., Mao M., Wang Z., Sun W., Han J., Yang M., Jiang Y., Hua Y, & Cai Z. (2019). CYT997(Lexibulin) induces apoptosis and autophagy through the activation of mutually reinforced ER stress and ROS in osteosarcoma. Journal of Experimental & Clinical Cancer Research : CR, 38, 44.

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MEUB-Induced Apoptosis Activation

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Cells were treated with MEUB (48 h, 0 to 6 μg/mL or 0 to 48 h, 2 μg/mL). Detailed information of Western blotting was previously mentioned [25 (link)]. The primary apoptosis antibody against the cleaved form of poly (ADP-ribose) polymerase (c-PARP) (Cell Signaling Technology, Inc., Danvers, MA, USA) and internal control antibody against β-actin (Sigma-Aldrich, St. Louis, MO, USA) were applied.

Tang J.Y., Wu K.H., Wang Y.Y., Farooqi A.A., Huang H.W., Yuan S.S., Jian R.I., Tsao L.Y., Chen P.A., Chang F.R., Cheng Y.B., Hu H.C, & Chang H.W. (2020). Methanol Extract of Usnea barbata Induces Cell Killing, Apoptosis, and DNA Damage against Oral Cancer Cells through Oxidative Stress. Antioxidants, 9(8), 694.

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Quantifying Hippocampal Markers in Alzheimer's

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Seven (synaptophysin), 8 (GFAP), or 9 (Aβ_1–42, cPARP, BDNF, IL-1β, TNFα) days after Aβ_25–35 or Sc.Aβ injection, hippocampi were dissected out and rinsed in ice-cold PBS to remove excess blood, and weighed before nitrogen freezing and −80°C storage. Tissues were cut into small pieces, homogenised, sonicated and centrifuged. The supernatants were assayed immediately by ELISA for GFAP, synaptophysin, IL-1β (USCN, China), TNFα (Thermo Scientific, France), BDNF (Promega, France), cPARP (Cell Signalling, France) and Aβ_1–42 (Euromedex, France) following manufacturer's recommendations. All samples were assayed in duplicate and only samples for which the CV was <25% between replicates were included for analyses. Results were expressed in pg protein per mg of brain tissue, or as % of Sc. control. Protein concentration was determined in brain homogenates with the BCA protein assay kit (Pierce Perbio Science, France).

Chumakov I., Nabirotchkin S., Cholet N., Milet A., Boucard A., Toulorge D., Pereira Y., Graudens E., Traoré S., Foucquier J., Guedj M., Vial E., Callizot N., Steinschneider R., Maurice T., Bertrand V., Scart-Grès C., Hajj R, & Cohen D. (2015). Combining two repurposed drugs as a promising approach for Alzheimer's disease therapy. Scientific Reports, 5, 7608.

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Evaluation of Anticancer Compounds on Pancreatic and Cardiac Cells

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Human pancreatic cancer cells (L3.6pl, MIA PaCa-2) and cardiomyocyte cells (H9C2) were used in this study. L3.6pl cells were obtained from the University of Texas MD Anderson Cancer Center, Houston, TX. MIA PaCa-2 and H9C2 cells were purchased from ATCC (Manassas, VA). Cells were grown in DMEM media supplemented with fetal bovine serum and 1% antibiotic (Pen/Strep) and maintained at 37°C with 5% CO₂.
Antibodies were purchased from Santa Cruz Biotechnology, Santa Cruz, CA (Sp1, Sp3); R&D Systems, Minneapolis, MN (survivin); Cell Signaling Technology, Danvers, MA (c-PARP). Tolfenamic acid, Ibuprofen, Celebrex, dimethyl sulfoxide (DMSO), protease inhibitor, and β-actin were purchased from Sigma Chemical Co. (St. Louis, MO). Kits were purchased from BD Biosciences, San Jose, CA (Annexin-V/7-AAD); Pierce, Rockford, IL (BCA protein assay) and Promega, Madison, WI (CellTiter-Glo and Caspase-Glo 3/7). Reagents were obtained from Mediatech, Manassas, VA (PBS, DMEM); Invitrogen, Carlsbad, CA (cell lysis buffer) and Pierce, Rockford, IL (SuperSignal West Dura).

Basha R., Connelly S.F., Sankpal U.T., Nagaraju G.P., Patel H., Vishwanatha J.K., Shelake S., Tabor-Simecka L., Shoji M., Simecka J.W, & El-Rayes B. (2016). Small molecule tolfenamic acid and dietary spice curcumin treatment enhances anti-proliferative effect in pancreatic cancer cells via suppressing Sp1, disrupting NF-kB translocation to nucleus and cell cycle phase distribution. The Journal of nutritional biochemistry, 31, 77-87.

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Protein Expression Analysis via Western Blot

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Cells were seeded in 6-well plates, followed by treatments as indicated. Cells were lysed with RIPA buffer (150 mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris, pH 8.0), sonicated and centrifuged (14000 rpm, 10 min, 4°C). Supernatant protein content was measured using BCA Assay Kit (Pierce, Rockford, IL, USA). Proteins (50 μg/sample) were separated via reducing 10% SDS-PAGE and standard western blotting procedures [28 (link)] were used to detect proteins of interest with the following primary antibodies: c-PARP (Cell Signaling Technology, #9541), γ-H2AX (Cell Signaling Technology, #9718), MRP1 (Enzo Life Sciences, #106-80107), β-actin (Abcam, ab8227).

Shen H., Decollogne S., Dilda P.J., Hau E., Chung S.A., Luk P.P., Hogg P.J, & McDonald K.L. (2015). Dual-targeting of aberrant glucose metabolism in glioblastoma. Journal of Experimental & Clinical Cancer Research : CR, 34(1), 14.

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Signaling Pathway Protein Analysis

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The primary antibodies were as follows: anti-STAT3, p-STAT3 (Tyr705), IL6ST (Gp130), E-cadherin, Vimentin (R28), ZEB1, Snail, Axl, AKT, p-AKT (Ser473), p44/p42 mitogen-activated protein kinase (ERK), p-p44/p42 MAPK (p-ERK1/2), JAK1, p-JAK1, JAK2, p-JAK2, JAK3, Tyk2 (a JAK family menber), PARP, and c-PARP (Cell Signaling Technology) and IL6R, OSMR, and LIFR (Santa Cruz Biotechnology). Monoclonal anti-actin antibody, used as an equal loading control, was purchased from EMD Millipore. Secondary antibodies were goat anti-rabbit and goat anti-mouse horseradish peroxidase-conjugated immunoglobulin G (Santa Cruz Biotechnology). To detect specific signals, the membranes were examined by Western Lightning Plus-ECL (Perkin-Elmer).

Shien K., Papadimitrakopoulou V.A., Ruder D., Behrens C., Shen L., Kalhor N., Song J., Lee J.J., Wang J., Tang X., Herbst R.S., Toyooka S., Girard L., Minna J.D., Kurie J.M., Wistuba I.I, & Izzo J.G. (2017). JAK1/STAT3 activation through a proinflammatory cytokine pathway leads to resistance to molecularly targeted therapy in non-small cell lung cancer. Molecular cancer therapeutics, 16(10), 2234-2245.

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Immunoblotting for Protein Expression

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Immunoblotting was performed as described previously16 (link). Proteins were extracted from adherent cells with Radio Immunoprecipitation Assay (RIPA) lysis buffer. Cell lysates were electrophoresis in 10% Bis-Tris Gel, transferred to PVDF membranes, probed with HRP-linked secondary antibodies, and visualized with ECL reagent (Thermo Scientific).
Used antibodies were as follow: ELF5 (Santa Cruz Biotechnology, catalogue no. sc-376737), cPARP (Cell Signaling, catalogue no. 9541), BCL-xl (Cell Signaling, catalogue no. 2762), AR (Santa Cruz Biotechnology, catalogue no. sc-816), PSA (Dako, catalogue no. A0562) and FKBP5 (Abcam, catalogue no. ab2901).

Li K., Guo Y., Yang X., Zhang Z., Zhang C, & Xu Y. (2017). ELF5-Mediated AR Activation Regulates Prostate Cancer Progression. Scientific Reports, 7, 42759.

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Ruxolitinib and Calcitriol Impacts

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Ruxolitinib was purchased from Selleckchem (S1378, Houston, TX, USA), and calcitriol was purchased from Sigma-Aldrich (D1530, St. Louis, MO, USA). Ruxolitinib and calcitriol were dissolved in dimethyl sulfoxide (DMSO) to prepare the stock solutions, and the final concentrations were obtained by diluting the stock solutions with RPMI-1640 medium (Gibco; Thermo Fisher Scientific Inc., Waltham, MA, USA). All solutions were prepared immediately prior to use. Antibodies against c-Myc (#13987), cyclin B1 (#12231), cyclin D1 (#2922), CDK1 (#9116), CDK4 (#12790), CDK6 (#13331), p21 (#2947), p27 (#3686), BAD (#9239), Bcl-2 (#15071), Bcl-xL (#2764), c-caspase 3 (#9661), PARP (#9532), c-PARP (#5625), p-p53 (#2521), p-JAK2 (#3776), and β-actin (#4967) were purchased from Cell Signaling Technology Inc. (Danvers, MA, USA).

Schneider J., Jeon Y.W., Suh Y.J, & Lim S.T. (2022). Effects of Ruxolitinib and Calcitriol Combination Treatment on Various Molecular Subtypes of Breast Cancer. International Journal of Molecular Sciences, 23(5), 2535.

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