Anti parp

Manufactured by Cell Signaling Technology

Sourced in United States, United Kingdom, China, Canada, Italy

Anti-PARP is a laboratory reagent produced by Cell Signaling Technology. It is a monoclonal antibody that binds to the Poly (ADP-ribose) Polymerase (PARP) protein. PARP is an enzyme involved in various cellular processes, including DNA repair, programmed cell death, and chromatin modification.

Automatically generated - may contain errors

Lab products found in correlation

Close spelling variants of this product

Anti-cleaved PARP (Asp214) (D64E10) Anti-poly(ADP-ribose) polymerase-1 (PARP-1; Anti-cleaved PARP (9664S Rabbit polyclonal anti-PARP (9542) Anti-cleaved poly(ADP-ribose) polymerase (PARP) antibody Anti-c-PARP Rabbit monoclonal anti-PARP Anti-cleaved PARP (D64E10; Anti-PARP rabbit polyclonal antibody Anti-cleaved PARP rabbit monoclonal antibody

500 protocols using anti parp

Protein Expression Analysis via Western Blot

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cells were lysed in RIPA-SDS buffer, after which the proteins were resolved by
SDS-PAGE, transferred onto PVDF membranes, and probed with the relevant
antibodies as previously described9 (link). The following antibodies
were used for the experiments: anti-actin (Sigma); anti-SESN2 (Proteintech),
anti-NRF2, anti-CHOP and anti-p53 (Santa Cruz); and anti-phospho(T389)-p70S6K,
anti-phospho(S235/236)-S6, anti-phospho(S65)-4E-BP1, anti-phospho
IF2α(S51), anti-phospho(T172)-AMPKα,
anti-phospho(S79)-acetyl-CoA carboxylase, anti-phospho(S9)-GSK3β,
anti-phospho(T1462), anti-4E-BP1, anti-S6, anti-TSC2, anti-AMPKα,
anti-ATF4, anti-Bip, anti-p62, anti-LC3, anti-PARP, anti-PARP(cleaved),
anti-caspase3, and anti-caspase3(cleaved) (Cell Signaling Inc). Sesn1 antibodies
were previously described11 (link).

Ding B., Parmigiani A., Divakaruni A.S., Archer K., Murphy A.N, & Budanov A.V. (2016). Sestrin2 is induced by glucose starvation via the unfolded protein response and protects cells from non-canonical necroptotic cell death. Scientific Reports, 6, 22538.

+ Open protocol

+ Expand

Apoptosis Induction by Targeted Doxorubicin

Check if the same lab product or an alternative is used in the 5 most similar protocols

MCF-7/Adr cells were cultured for 12 h and then treated with free DOX, DOX nanoparticles, targeted DOX nanoparticles or functional DOX nanoparticles. Controls were performed by adding blank medium. The final concentration of DOX was 2 μM. After 12 h of incubation, the cells were harvested, lysed, and analyzed by western blotting. The following antibodies were used: anti-caspase-8, anti-caspase-9, anti-caspase-3, and anti-PARP (all from Cell Signaling, Beverly, MA, USA) [27 (link)].

Wang H., Yin H., Yan F., Sun M., Du L., Peng W., Li Q., Feng Y, & Zhou Y. (2014). Folate-mediated mitochondrial targeting with doxorubicin-polyrotaxane nanoparticles overcomes multidrug resistance. Oncotarget, 6(5), 2827-2842.

+ Open protocol

+ Expand

Isolation and Characterization of Primary Muscle Cells

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Primary muscle cultures (pp6) were isolated as described (Qu et al., 1998 (link)) from the indicated mouse lines. FoxO3-depleted (FoxO-KO) pp6 cells were prepared from foxO3^+/− mice as previously described (Dentice et al., 2010 (link)). C2C12 cells were obtained from ATCC. In some experiments, endogenous T3 and T4 were removed from the FBS by charcoal absorption (Larsen, 1972 (link)). Transient transfections were performed using Lipofectamine 2000 (Life Technologies) according to the manufacturer’s instructions. Single myofibers were prepared from the extensor digitorumlongus and gastrocnemius muscles of 6- to 12-week-old mice as previously described (Rosenblatt et al., 1995 (link)). Pax7^Hi-Lo isolation by FACS has been described elsewhere (Rocheteau et al., 2012 (link)). Anti-MyoD (sc-304), myogenin (sc-12732), tubulin (sc-8035), and anti-FoxO3 antibodies were purchased from Santa Cruz Biotechnology. Polyclonal anti-MHC antibody (MF-20a) and anti-Pax7 antibody were from Developmental Studies Hybridoma Bank. Anti-D3 antibody is described elsewhere (Huang et al., 2003 (link)). Anti-Desmin antibody was from MP Biomedicals (#10519). Anti-total Akt was from Upstate, and anti-pAkt and anti-PARP were from Cell Signaling Technology. TUNEL assay was performed using the ApopTag kit from Millipore. Caspase-3/Caspase-7 activity was measured by using the CaspaseGlo kit from Promega.

Dentice M., Ambrosio R., Damiano V., Sibilio A., Luongo C., Guardiola O., Yennek S., Zordan P., Minchiotti G., Colao A., Marsili A., Brunelli S., Del Vecchio L., Larsen P.R., Tajbakhsh S, & Salvatore D. (2014). Intracellular Inactivation of Thyroid Hormone Is a Survival Mechanism for Muscle Stem Cell Proliferation and Lineage Progression. Cell Metabolism, 20(6), 1038-1048.

+ Open protocol

+ Expand

Apoptosis and Autophagy Regulation in PBDE-47 Exposure

Check if the same lab product or an alternative is used in the 5 most similar protocols

The following antibodies were used: anti-PARP (Cell Signaling Technology, 9542), anti-caspase-3 (9661, Cell Signaling Technology, USA), anti-autophagy-related protein 7 (ATG7) (ab133528, Abcam, USA), anti-LC3 (14600-1-AP, Proteintech, USA), anti-p62 (ab56416, Abcam, USA), anti-GAPDH (60004-1-Ig, Proteintech, USA). The following chemical regents were used: PBDE-47 (purity 99.5%, GC/MS) (BDE-047N-3G, AccuStandard Corp, USA), Wortmannin (WM) (S2758, Selleck Chemicals, USA), Rapamycin (RAP) (R5000, Shanghai Haoran, China), Ac-DEVD-CHO (DEVD) (C1206-10 mM, Beyotime Institute of Biotechnology, China). All other chemical regents were analytical grade purchased from credible supplier or as described in the relevant methods.

Li P., Ma R., Dong L., Liu L., Zhou G., Tian Z., Zhao Q., Xia T., Zhang S, & Wang A. (2019). Autophagy impairment contributes to PBDE-47-induced developmental neurotoxicity and its relationship with apoptosis. Theranostics, 9(15), 4375-4390.

+ Open protocol

+ Expand

Western Blot Analysis of Neurodegeneration

Check if the same lab product or an alternative is used in the 5 most similar protocols

Whole protein lysates were prepared using the PRO-PREP protein extraction solution (Intron Biotechnology, Seongnam, Korea), and mitochondrial and cytoplasmic fractions were performed with a mitochondria isolation kit (Thermo Fisher Scientific, Waltham, MA, USA). Equal amounts of proteins were separated by electrophoresis on 8–12% SDS-PAGE gels and transferred onto nitrocellulose membranes (BD Biosciences, San Jose, NJ, USA). The membranes were blocked by incubation in blocking buffer (BD Biosciences) and probed with the following antibodies overnight at 4°C: anti-NeuN, anti-AT8, anti-Tau-5, anti-β-actin (Sigma–Adrich, St. Louis, MO, USA), anti-PSD95, anti-phospho(p)-Tau(T181), anti-p-Tau(S396; Abcam, MA, USA), anti-Drp1, anti-p-Drp1(S616), anti-COXIV, anti-GAPDH, anti-PARP, anti-cleaved caspase-3, p-Tau(S262), anti-CDK5, anti-ERK, anti-p-ERK, anti-GSK3β, anti-p-GSK3β(S9; Cell Signaling, MA, USA), and anti-p35 (Thermo Fisher Scientific, Waltham, MA, USA). The membranes were washed with TBS with 0.1% Tween-20 (TBST) and incubated with horseradish peroxidase-conjugated secondary antibodies (Cell Signaling) for 1 h at room temperature. After washing with TBST, specific binding was detected using a chemiluminescence detection system (Thermo Fisher Scientific, Waltham, MA, USA).

Park J., Won J., Seo J., Yeo H.G., Kim K., Kim Y.G., Jeon C.Y., Kam M.K., Kim Y.H., Huh J.W., Lee S.R., Lee D.S, & Lee Y. (2020). Streptozotocin Induces Alzheimer’s Disease-Like Pathology in Hippocampal Neuronal Cells via CDK5/Drp1-Mediated Mitochondrial Fragmentation. Frontiers in Cellular Neuroscience, 14, 235.

+ Open protocol

+ Expand

Western Blot Analysis of Cell Cycle and Apoptosis

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

30 μg of whole cell lysate was separated on 7.5–12% SDS-PAGE and Western blotting as previously described [12 (link)]. Cyclin-B was detected using anti-cyclin B (Sigma). Apoptotic markers including, caspase-3 and poly (ADP-ribose) polymerase (PARP) were detected using anti-caspase-3 (Cell Signaling) and anti-PARP (Cell Signaling) antibodies, respectively. Anti-β-actin antibody (Sigma), was used as the loading control.

Rattanapornsompong K., Khattiya J., Phannasil P., Phaonakrop N., Roytrakul S., Jitrapakdee S, & Akekawatchai C. (2021). Impaired G2/M cell cycle arrest induces apoptosis in pyruvate carboxylase knockdown MDA-MB-231 cells. Biochemistry and Biophysics Reports, 25, 100903.

+ Open protocol

+ Expand

Western Blot Analysis Methodology

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Western blot analysis was carried out as described by Misiura et al. [30 (link)]. The membranes were incubated with primary antibodies diluted 1000 times in 5% bovine serum albumin (Sigma Aldrich, Saint Louis, MO, USA) in TBS-T (20 mM Tris, 150 mM NaCl, 0.1% Tween-20, pH 7.6). Anti-PARP, anti-AMPK and anti-caspase-7 and anti-GAPDH, were purchased from Cell Signaling Technology, Danvers, MA, USA; anti-PRODH/POX from St John’s Laboratory, London, UK), followed by incubation with alkaline phosphatase-linked goat anti-rabbit or anti-mouse antibodies (dilution: 1:10,000 in 5% non-fat dried milk (Santa Cruz Biotechnology, Dallas, TX, USA) in TBS-T; Sigma Aldrich, Saint Louis, MO, USA). The bands’ intensities were semi-quantitatively measured in ImageJ software (https://imagej.nih.gov/ij/, accessed on 27 October 2021). All experiments were run at least in triplicates.

Huynh T.Y., Oscilowska I., Sáiz J., Nizioł M., Baszanowska W., Barbas C, & Palka J. (2021). Metformin Treatment or PRODH/POX-Knock out Similarly Induces Apoptosis by Reprograming of Amino Acid Metabolism, TCA, Urea Cycle and Pentose Phosphate Pathway in MCF-7 Breast Cancer Cells. Biomolecules, 11(12), 1888.

+ Open protocol

+ Expand

Western Blot Analysis of Protein Modifications

Check if the same lab product or an alternative is used in the 5 most similar protocols

Cell lysates were harvested in NP-40 lysis buffer containing Complete Mini protease inhibitor cocktail (Roche Diagnostics). A small portion of each solid tumor (from NSG mice) or mouse spleen (from HIS mice) was collected in NP-40 lysis buffer containing Complete Mini protease inhibitor cocktail and homogenized using a BioMasher® II Micro Tissue Homogenizer (VWR). Protein quantification was carried out using the Pierce™ BCA Protein Assay Kit (Thermo Fisher) and a FilterMax F5 Multi-Mode Microplate Reader (San Jose, CA, United SA). Equal concentrations of protein were separated in Mini-PROTEAN® TGX™ Precast 4–20% Gels (Bio-Rad, Hercules, CA, USA) and transferred to nitrocellulose membranes. Membranes were blocked in PBS containing 5% milk and 0.1% Tween-20 and incubated with primary antibody overnight at 4°C. The following antibodies were used: anti-Symmetric Di-Methyl Arginine Motif [sdme-RG] (1:1000, Cell Signaling, Danvers, MA, USA), anti-PARP (1:1000, Cell Signaling), anti-β-actin (1:5000, Sigma, St. Louis, MO, USA), and anti-α-tubulin (1:250, Santa Cruz Biotechnology). Secondary antibodies used include IgG HRP anti-rabbit and anti-mouse (1:5000, Promega). Blots were developed using Pierce™ ECL Western chemiluminescence substrate (Thermo Scientific). Images were captured using the Amersham Imager 600 (GE Healthcare Life Sciences).

Ernzen K., Melvin C., Yu L., Phelps C., Niewiesk S., Green P.L, & Panfil A.R. (2023). The PRMT5 inhibitor EPZ015666 is effective against HTLV-1-transformed T-cell lines in vitro and in vivo. Frontiers in Microbiology, 14, 1101544.

+ Open protocol

+ Expand

Western Blot Analysis of Signaling Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols

Western blot was performed as previously described.3 (link) The anti-PARP, anti-p-β-catenin (S33/37/T41), anti-β-catenin, anti-c-Myc, anti-AKT1, anti-p-AKT1 (S473), anti-p-mTOR (S2448), anti-mTOR and anti-LC3B antibodies were purchased from Cell Signaling Technology (Beverly, MA). The anti-β-actin antibody was purchased from Santa Cruz Biotechnology (Santa Cruz, CA). The anti-SQSTM1/p62 antibody was from Abcam (Cambridge, UK). The densitometry of the immunoblots was performed with Image J software (NIH, Bethesda, MD)

Ma Y., Yuwen D., Chen J., Zheng B., Gao J., Fan M., Xue W., Wang Y., Li W., Shu Y., Xu Q, & Shen Y. (2019). Exosomal Transfer Of Cisplatin-Induced miR-425-3p Confers Cisplatin Resistance In NSCLC Through Activating Autophagy. International Journal of Nanomedicine, 14, 8121-8132.

+ Open protocol

+ Expand

Western Blot Detection of Apoptosis Markers

Check if the same lab product or an alternative is used in the 5 most similar protocols

Proteins were resolved by SDS-PAGE, transferred to PVDF membranes, blocked with 5% non-fat dry milk in TBST (0.1% Tween-20) and probed with the indicated antibodies. The primary antibodies were used as follows: anti-GADPH (Cell Signaling 2118, 1:2000), anti-PARP (Cell Signaling 9542, 1:1000), anti-pro/caspase-3 (Cell Signaling 9668, 1:1000), anti-pro/caspase-6 (Cell Signaling 9762 1:1000), anti-pro/caspase-7 (Cell Signaling 9492, 1:1000), anti-pro/caspase-8 (Cell Signaling 9746, 1:1000), anti-pro/caspase-9 (Cell Signaling 9502, 1:1000). Blots were incubated with primary antibodies (4 °C, overnight) , washed (rt, 3 × 5 min, TBST) and incubated with secondary antibodies (LICOR IR800CDW or IR680RD, 1: 10,000) for 1 h at ambient temperature. Blots were further washed (3 × 5 minutes, TBST) and visualized on a LICOR Odyssey Scanner.

Solania A., González-Páez G.E, & Wolan D.W. (2019). A selective and rapid cell-permeable inhibitor of human caspase-3. ACS chemical biology, 14(11), 2463-2470.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!