Product Details
| Alternative Name: | Poly(ADP-ribose) polymerase-1 |
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| Host: | Rabbit |
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| Immunogen: | Recombinant human PARP-1 (poly(ADP-ribose) polymerase-1) (aa 1-1014). |
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| UniProt ID: | P09874 |
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| Species reactivity: | Human, Mouse
Bovine, Monkey
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| Crossreactivity: | Does not cross-react with PARP-2. |
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| Applications: | ELISA, ICC, IHC (FS), IHC (PS), IP, WB
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| Recommended Dilutions/Conditions: | Immunocytochemistry (1:4,000)
Immunoprecipitation (1:400)
Western Blot (1:4,000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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| Application Notes: | Detects bands of ~116kDa (PARP-1) and ~85kDa (apoptosis-induced cleavage fragment) by Western blot. |
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| Formulation: | Liquid. Neat serum containing 0.02% sodium azide. |
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| Use/Stability: | Stable for at least one year when stored at +4°C. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | +4°C |
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| Regulatory Status: | RUO - Research Use Only |
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Figure: Western blot using rabbit polyclonal anti PARP-1.
Lane 1: recombinant human PARP-1 (ALX-201-053, 5 ng).
Lane 2: Total HeLa cell extract.
Lane 3: Total MEF PARP1+/+ cell extract.
Lane 4: Total MEF PARP1-/- cell extract.
Lane 5: Lysate (50 μg) from HeLa cells.
Lane 6: Lysate (50 μg) from HeLa PARP-1sh cells.
Lane 7: Lysate (50 μg) from HeLa cells treated for 8 hours with Doxorubicin 5 μg/ml.
Lane 8: Lysate (50 μg) from HEK293 cells.
Lane 9: Lysate (50 μg) from HEK293 cells.
Lane 10: Lysate (50 μg) from HEK293 cells transfected with PARP-1 siRNA.
Lane 11: Lysate (50 μg) from HEK293 cells transfected with control siRNA.
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Product Literature References
Cytidine deaminase deficiency in mice enhances genetic instability but limits the number of chemically induced colon tumors: R.O. Delic, et al.; Cancer Lett.
555, 216030 (2023),
Abstract;
Cytidine deaminase deficiency in tumor cells is associated with sensitivity to a naphthol derivative and a decrease in oncometabolite levels: H. Mameri, et al.; Cell. Mol. Life Sci.
79, 465 (2022),
Abstract;
MDM2 binds and ubiquitinates PARP1 to enhance DNA replication fork progression: C. Giansanti, et al.; Cell Rep.
39, 110879 (2022),
Abstract;
Differential data on the responsiveness of multiple cell types to cell death induced by non-thermal atmospheric pressure plasma-activated solutions: K. Eto, et al.; Data Brief
36, 106995 (2021),
Abstract;
Full Text
A decrease in NAMPT activity impairs basal PARP-1 activity in cytidine deaminase deficient-cells, independently of NAD+: S. Silveira, et al.; Sci. Rep.
10, 13907 (2020),
Abstract;
Full Text
Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation: H. Ali, et al.; Nat. Commun.
10, 926 (2019),
Abstract;
Full Text
Epigenetic Regulation of RIP3 Suppresses Necroptosis and Increases Resistance to Chemotherapy in NonSmall Cell Lung Cancer: Q. Wang, et al.; Transl. Oncol.
13, 372 (2019),
Abstract;
Full Text
Posttranscriptional Regulation of HIV-1 Gene Expression during Replication and Reactivation from Latency by Nuclear Matrix Protein MATR3: A. Sarracino, et al.; Mbio
9, e02158-18 (2018),
Abstract;
Full Text
Cytidine deaminase deficiency impairs sister chromatid disjunction by decreasing PARP-1 activity: S. Gemble, et al.; Cell Cycle
16, 1128 (2017),
Abstract;
Full Text
PARP1 promotes gene expression at the post-transcriptiona level by modulating the RNA-binding protein HuR: Y. Ke, et al.; Nat. Commun.
8, 14632 (2017),
Abstract;
Full Text
A balanced pyrimidine pool is required for optimal Chk1 activation to prevent ultrafine anaphase bridge formation: S. Gemble, et al.; J. Cell Sci.
129, 3167 (2016),
Abstract;
A PARP1-ERK2 synergism is required for the induction of LTP: L. Visochek, et al.; Sci. Rep.
6, 24950 (2016),
Application(s): Western blot,
Abstract;
Full Text
Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB: D.L. Medina, et al.; Nat. Cell. Biol.
17, 288 (2015),
Application(s): Western Blotting,
Abstract;
NF-κB transcriptional activation by TNFα requires phospholipase C, extracellular signal-regulated kinase 2 and poly(ADP-ribose) polymerase-1: B. Vuong, et al.; J. Neuroninflammation
12, 229 (2015),
Application(s): Western blot detecting PARP-1 expression,
Abstract;
Full Text
Pyrimidine Pool Disequilibrium Induced by a Cytidine Deaminase Deficiency Inhibits PARP-1 Activity, Leading to the Under Replication of DNA: S. Gemble, et al.; PLoS Genet.
11, 1005384 (2015),
Abstract;
Full Text
A JNK-mediated autophagy pathway that triggers c-IAP degradation and necroptosis for anticancer chemotherapy: W. He, et al.; Oncogene
33, 3004 (2014),
Abstract;
Full Text
Poly(ADP-Ribosyl)ation Is Required to Modulate Chromatin Changes at c-MYC Promoter during Emergence from Quiescence: C. Mostocotto, et al.; PLoS One
9, e102575 (2014),
Abstract;
Full Text
Receptor-interacting Protein 1 Increases Chemoresistance by Maintaining Inhibitor of Apoptosis Protein Levels and Reducing Reactive Oxygen Species through a microRNA-146a-mediated Catalase Pathway: Q. Wang, et al.; J. Biol. Chem.
289, 5654 (2014),
Abstract;
Full Text
Poly(ADP-ribose) Polymerase 1 (PARP-1) Binds to 8-Oxoguanine-DNA Glycosylase (OGG1): N. Noren Hooten, et al.; J. Biol. Chem.
286, 44679 (2011),
Abstract;
Full Text
RANKL up-regulates brain-type creatine kinase via poly(ADP-ribose) polymerase-1 during osteoclastogenesis: J. Chen, et al.; J. Biol. Chem.
285, 36315 (2010),
Abstract;
Full Text
The BRCT domain of PARP-1 is required for immunoglobulin gene conversion: M.N. Paddock, et al.; PLoS Biol.
8, e1000428 (2010),
Abstract;
Full Text
Mitochondrial localization of PARP-1 requires interaction with mitofilin and is involved in the maintenance of mitochondrial DNA integrity: M.N. Rossi, et al.; J. Biol. Chem.
284, 31616 (2009),
Abstract;
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Poly(adp-ribose) polymerase-1 regulates Tracp gene promoter activity during RANKL-induced osteoclastogenesis: G.E. Beranger, et al.; J. Bone Miner. Res.
23, 564 (2008),
Abstract;
The prevention of spontaneous apoptosis of follicular lymphoma B cells by a follicular dendritic cell line: involvement of caspase-3, caspase-8 and c-FLIP: J.J. Goval, et al.; Haematologica
93, 1169 (2008),
Application(s): WB using human follicular lymphoma lysate,
Abstract;
Full Text
