Anti parp 1

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-PARP-1 is a laboratory reagent designed for the detection and quantification of PARP-1 (Poly(ADP-ribose) Polymerase 1) protein in various biological samples. It is a critical enzyme involved in cellular processes such as DNA repair, genomic stability, and programmed cell death. This product can be used in techniques like Western blotting, immunoprecipitation, and ELISA to measure PARP-1 levels and activity.

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Mouse monoclonal anti-PARP-1 AF488-conjugated anti-PARP-1 Anti-PARP-1 (H-250, Rabbit anti-PARP-1 Anti-cleaved PARP-1 Mouse monoclonal anti-PARP-1 (F-2, Anti-PARP-1 (sc-7150) PARP-1 Anti-PARP

65 protocols using anti parp 1

Molecular Markers in Neurodegeneration

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The following antibodies were used in western blot and immunofluorescence studies: p-AMPK, AMPK p-CREB (Cell Signaling), anti-Nrf-2, anti-PSD-95, anti-Syntaxin, anti-synaptosomal-associated protein 23 (SNAP-23), anti-Caspase 3, anti- PARP-1, anti-Cleaved Caspase-3, Synaptophysin, anti-Bax, anti-Bcl2, anti-TNF-α, anti-IL-1β, anti-p-NF-κB, anti-Iba-1, anti-GFAP, and anti-β-actin, which were all obtained from Santa Cruz Biotechnology (Dallas, TX, USA). Primary antibodies were diluted in 1× TBST (Tris-buffered saline plus Tween) (1:1000), and secondary conjugated anti-mouse horseradish peroxidase (HRP) and conjugated anti-rabbit HRP were diluted 1:10,000 in 1× TBST, all purchased from Promega USA. For confocal microscopic studies, the secondary fluorescent antibodies used were goat anti-mouse and goat anti-rabbit diluted in 1 × 100 phosphate-buffered saline (PBS).

Rehman S.U., Ikram M., Ullah N., Alam S.I., Park H.Y., Badshah H., Choe K, & Ok Kim M. (2019). Neurological Enhancement Effects of Melatonin against Brain Injury-Induced Oxidative Stress, Neuroinflammation, and Neurodegeneration via AMPK/CREB Signaling. Cells, 8(7), 760.

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Comprehensive Western Blotting Procedure

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Western blotting was performed as described previously (Xie et al., 2017 (link)) with slight modifications. Cell pellets were resuspended in lysis buffer (50 mM Tris pH 7.4, 150 mM NaCl, 0.5% Triton X-100, 1mM EDTA pH 8.0, and protease cocktail inhibitor). Soluble extracts were prepared by centrifugation (14,000 × g for 20 min at 4°C). Cell lysates were separated by 6–15% SDS-PAGE and then transferred to nitrocellulose membranes (GE Healthcare). Membranes were blocked for 1 h with 3% dried skim milk in TBST (50 mM Tris pH 8.0, 150 mM NaCl, and 0.5% Tween 20) and incubated with the following primary antibodies, anti-HA (Santa Cruz, sc-805), anti-FLAG (Sigma Aldrich, F1804), anti-MYC (Cell Signaling, #2276), anti-BCL-xL (Cell Signaling, #2764), anti-MCL-1 (Santa Cruz, sc-819), anti-ACTIN (Santa Cruz, sc-47778), anti-GAPDH (Santa Cruz, sc-32233), anti-BCL2 (Santa Cruz, sc-7382), anti-BAX (Santa Cruz, sc-493), and anti-PARP1 (Santa Cruz, sc-7150). After incubation with primary antibodies, the membranes were incubated with the appropriate peroxidase-conjugated secondary antibodies (GeneDEPOT, USA). Protein expression was detected by enhanced chemiluminescence (ECL) reagents and LAS-3000 image analyzer (Fujifilm, Japan).

Jin Y., You L., Kim H.J, & Lee H.W. (2018). Telomerase Reverse Transcriptase Contains a BH3-Like Motif and Interacts with BCL-2 Family Members. Molecules and Cells, 41(7), 684-694.

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Comprehensive Protein Extraction and Analysis

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For protein extraction, all cell lines were lysed in RIPA buffer or in a less stringent buffer (20 mM Tris HCl pH 8, 137 mM NaCl, 1% NP-40, 2 mM ethylenediaminetetraacetic acid (EDTA)) for the SRSF3 ISO2 (SRSF3-TR) detection. The homogenates were subjected to western blot analyses as reported (26 (link)). Antibodies used were anti-SLU7 (Novus, 1:1000), anti-PARP1 (Santa Cruz SC-7150; 1:1000, CA, USA), anti-Actin (Sigma A2066; 1:6000, MO, USA), anti-Sororin (kindly provided by Dr JM Peters, Austria), anti-SRSF3 (Thermo Fisher 33-4200; 1:500 and MBL RN080PW; 1:500, MA, USA), anti-WAPL (Cell signaling 77428S; 1:1000, MA, USA), anti-H3S10P (Cell signaling #9701; 1:1000), anti-γ-H2AX (Cell signaling #2577S; 1:1000), anti-SRSF1 (Thermo Fisher 32-4600; 1:1000), anti-MAD2 (Bethyl laboratories a300-301A-M; 1:1000, TX, USA), anti-P21 (Santa Cruz SC-397; 1:1000), anti-RNaseH1 (Thermo Fisher PA5-30974; 1:1000) and anti-V5 (Invitrogene R960-25; 1:1000).

Jiménez M., Urtasun R., Elizalde M., Azkona M., Latasa M.U., Uriarte I., Arechederra M., Alignani D., Bárcena-Varela M., Álvarez-Sola G., Colyn L., Santamaría E., Sangro B., Rodriguez-Ortigosa C., Fernández-Barrena M.G., Ávila M.A, & Berasain C. (2019). Splicing events in the control of genome integrity: role of SLU7 and truncated SRSF3 proteins. Nucleic Acids Research, 47(7), 3450-3466.

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Protein Expression Analysis by Immunoblotting

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After treatment, the cells were harvested, lysed and their proteins subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) for immunoblotting with the respective antibodies. The protein bands were detected using an Amersham Imager 600 (GE Healthcare Life Sciences, Amersham, Buckinghamshire, UK). The following antibodies were used in this study: anti-p53 (sc-126, Santa Cruz, CA, USA), anti-FOXL2 [generated in our laboratory as previously described (29 (link))], anti-GAPDH (sc-47724, Santa Cruz), anti-Myc (#2276S, Cell Signaling Technology, Danvers, MA, USA), anti-FLAG (F1804, Sigma-Aldrich), anti-p21 (sc-397, Santa Cruz), anti-PARP1 (sc-74469, Santa Cruz), anti-BAX (sc-493, Santa Cruz) and anti-Caspase 3 (9662, Cell Signaling Technology).

Choi Y., Luo Y., Lee S., Jin H., Yoon H.J., Hahn Y., Bae J, & Lee H.H. (2022). FOXL2 and FOXA1 cooperatively assemble on the TP53 promoter in alternative dimer configurations. Nucleic Acids Research, 50(15), 8929-8946.

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Western Blot Analysis of MAPK Pathways

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Whole-cell protein extracts were isolated from primed hPSCs, hEPS, mES and mEPS cells using RIPA lysis buffer (Beyotime Technology Technology, P0013B) supplemented with protease inhibitor cocktail (Thermo Fisher Scientific, 78443) and phosphatase inhibitor cocktail (Thermo Fisher Scientific, 78428). Blots were incubated in 2% BSA/TBST at room temperature for 1 hr, and then, they were incubated with the following antibodies in 5% BSA or 5% skimmed milk powder/TBST at 4°C overnight. For detecting MAPK pathways, the same antibodies were used for human and mouse cells: anti-ERK1/2 (1:1,000; Beyotime Technology, AM076), anti-p-ERK1/2 (1:1,000; Beyotime Technology, AM071), anti-JNK (1:1,000; Beyotime Technology, AJ518), anti-p-JNK (1:1,000; Beyotime Technology, AM516), anti-p38 (1:1,000; Cell Signaling Technology, 9212), anti-p-p38 (1:1,000; Cell Signaling Technology, 9215) and anti-β-ACTIN (1:2,000; Sigma-Aldrich, A1978). For mouse cells, the anti-PARP1 (1:1,000; Santa Cruz, sc-7150) antibody was used. Secondary antibodies were anti-rabbit IgG, HRP-linked antibody (1:5,000; Cell Signaling Technology, 7074) and anti-mouse IgG, HRP-linked antibody (1:5,000; Cell Signaling Technology, 7076), which were incubated 1 hr at room temperature while shaking. The blots were developed using BeyoECL Plus (Beyotime Technology, P0018A).

Yang Y., Liu B., Xu J., Wang J., Wu J., Shi C., Xu Y., Dong J., Wang C., Lai W., Zhu J., Xiong L., Zhu D., Li X., Yang W., Yamauchi T., Sugawara A., Li Z., Sun F., Li X., Li C., He A., Du Y., Wang T., Zhao C., Li H., Chi X., Zhang H., Liu Y., Li C., Duo S., Yin M., Shen H., Belmonte J.C, & Deng H. (2017). Derivation of Pluripotent Stem Cells with In Vivo Embryonic and Extraembryonic Potency. Cell, 169(2), 243-257.e25.

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Antibody Sources for Protein Analysis

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DT and TMZ were obtained from Sigma Chemical Co. (St. Louis, MO, USA). The proteasome inhibitor MG132 was purchased from Calbiochem (San Diego, CA, USA). Monoclonal antibodies were purchased from the following companies: anti-CA9, anti-PARP-1, and anti-uPA antibodies from Santa Cruz Biotechnology (Santa Cruz, CA, USA); anti-HIF-1α and anti-HIF-1β antibodies from BD Biosciences (San Jose, CA, USA); anti-phospho-JNK and anti-JNK antibodies from Promega (Madison, WI, USA); anti-actin antibody from ICN (Costa Mesa, CA, USA); anti-CD133 and anti-VEGF antibodies from Abcam (USA); anti-β-Tubulin (Tuj1) antibody from Covance (USA); anti-Nestin antibody from Chemicon (USA); anti-SOX-2 antibody from R&D Systems (Minneapolis, MN, USA); and anti-Bmi1, anti-Musashi, anti-GFAP, anti-phospho-ERK, anti-ERK, anti-phospho-p38, anti-p38, anti-MMP-2, anti-MMP-9, and anti-phospho-Akt antibodies from Cell Signaling (Beverly, MA, USA).

Lee D.H., Oh S.C., Giles A.J., Jung J., Gilbert M.R, & Park D.M. (2017). Cardiac glycosides suppress the maintenance of stemness and malignancy via inhibiting HIF-1α in human glioma stem cells. Oncotarget, 8(25), 40233-40245.

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Western Blot Analysis of Apoptotic Markers

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For Western blot analysis, polypeptides in whole cell lysates were resolved by SDS-PAGE and transferred to NC or PVDF membrane filters. Proteins were detected with primary antibodies (1:1000 or 1:5000 dilution) using an enhanced chemiluminescence (ECL) system. Images were acquired using a Chemidoc-it 410 imaging system (UVP, Upland, CA) and an LAS4000 system (GE Healthcare, Uppsala, Sweden). The following primary antibodies were used: anti-LC3 (MBL International, Watertown, MA, USA), anti-p62 (MBL International), anti-caspase 3 (Cell Signaling Technology, Beverly, MA, USA), anti-cleaved caspase 3 (Cell Signaling Technology), anti-PARP-1 (Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-cleaved PARP (Genetex, San Antonio, TX, USA) and anti-actin (ABM, Richmond, BC, Canada).

Jang M., Kim H., Park R., Jo D., Lee E.J., Oh W.K, & Park J. (2017). 2,2′-Methylenebis (6-tert-butyl 4-methylphenol) enhances the antitumor efficacy of belotecan, a derivative of camptothecin, by inducing autophagy. Oncotarget, 8(70), 115068-115078.

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NFBD1 Knockdown Impacts DNA Repair

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CNE1, CNE2 and HNE1 were obtained from the Molecular Medicine and Cancer Research Center, Chongqing Medical University. The cells were grown in RMPI-1640 medium (HyClone, Logan City, Utah, USA) with 10% fetal bovine serum (HyClone, Logan City, Utah, USA) at 37 °C with 5% CO₂. The lentivirus-mediated shNFBD1 and shControl were purchased from Genechem, Shanghai,
China. PARP inhibitor Olaparib (AZD2281) was obtained from MedChemExpress (Princeton, NJ, USA). Hoechst 33342 were purchased from Beyotime Institute of Biotechnology (Nantong, China).The antibodies used in this study were anti-NFBD1 (Abcam, UK); anti-RAD51, anti-BRCA1, anti-BRCA2, and anti-PARP1 (Santa Cruz Biotechnology, USA); anti-γ-H2AX (Cell Signaling Technology, Danvers, MA, USA).

Wang Z., Zuo W., Zeng Q., Qian Y., Li Y., Liu C., Wang J., Zhong S., Bu Y, & Hu G. (2019). Loss of NFBD1/MDC1 disrupts homologous recombination repair and sensitizes nasopharyngeal carcinoma cells to PARP inhibitors. Journal of Biomedical Science, 26, 14.

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Western Blot Analysis of Cardiac Proteins

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Cardiac tissues and cardiomyocytes were homogenized in lysis buffer supplemented with the cOmplete™ Protease Inhibitor Cocktail. Next, we separated the proteins thus obtained using sodium dodecyl sulphate‐polyacrylamide gel electrophoresis on 10%‐12% gels. We transferred the separated proteins to nitrocellulose membranes, which were then blocked and incubated overnight at 4°C with the following primary antibodies: anti‐HIF‐1α, 1:500 (abcam); anti‐BAX, 1:1000 (Cell Signalling Technology); anti‐BCL‐2, 1:500 (abcam); anti‐BNIP3, 1:1000 (abcam); anti‐caspase‐3, 1:1000 (Cell Signalling Technology); anti‐PARP1, 1:500 (Santa Cruz Technology); and anti‐β‐tubulin, 1:1000 (Cell Signalling Technology). After this, the membranes were incubated for 1 hour at room temperature with rat anti‐mouse or goat anti‐rabbit secondary antibodies. Three replicates were tested for each sample. Finally, we visualized the blots by using chemiluminescence and a luminescent imaging workstation (Tanon 5200).

Peng K., Chen W., Xia F., Liu H., Meng X., Zhang J., Liu H., Xia Z, & Ji F. (2019). Dexmedetomidine post‐treatment attenuates cardiac ischaemia/reperfusion injury by inhibiting apoptosis through HIF‐1α signalling. Journal of Cellular and Molecular Medicine, 24(1), 850-861.

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Mitochondrial Dysfunction and Apoptosis Assay

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HepG2 cells were exposed to an IC₅₀ concentration of MBE (180 µg/mL) for 3, 6, and 24 h and then harvested and washed twice with ice-cold PBS. Mitochondria enrichment was obtained as previously described [12 (link)]. The membranes were incubated overnight at 4 °C with the specific primary antibody (anti-cytochrome c, 1:2000 Abcam). Moreover, whole lysate was blotted onto a nitrocellulose membrane and the nonspecific binding sites were blocked with TBST buffer containing 5% nonfat dry milk. The membranes were incubated with anti-PARP-1 or anti-Bcl-2, both diluted 1:200 (Santa Cruz Biotech, Dallas, TX, USA). After incubation with appropriate secondary antibodies, detection was performed using the enhanced chemiluminescence (ECL) kit (GE).

Russo D., Miglionico R., Carmosino M., Bisaccia F., Andrade P.B., Valentão P., Milella L, & Armentano M.F. (2018). A Comparative Study on Phytochemical Profiles and Biological Activities of Sclerocarya birrea (A.Rich.) Hochst Leaf and Bark Extracts. International Journal of Molecular Sciences, 19(1), 186.

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