PARP1 monoclonal antibody, clone 194C1439
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More Files
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Specification
Product Description
Mouse monoclonal antibody raised against synthetic peptide of PARP1.
Immunogen
A synthetic peptide corresponding to amino acids near 214/215-cleavage site of human PARP1.
Host
Mouse
Reactivity
Human
Form
Liquid
Isotype
IgG
Recommend Usage
The optimal working dilution should be determined by the end user.
Storage Buffer
In PBS (0.05% BSA, 0.05% sodium azide)
Storage Instruction
Store at 4°C. For long term storage store at -20°C.
Aliquot to avoid repeated freezing and thawing.Note
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Applications
Western Blot (Cell lysate)
Western blot analysis of cleaved PARP1 in staurosporin-treated Jurkat cells at various time points, using PARP1 monoclonal antibody, clone 194C1439 (Cat # MAB0097) at 2 ug/mL . The band corresponding to cleaved PARP1 is only seen in the treated samples.Flow Cytometry
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Gene Info — PARP1
Entrez GeneID
142Gene Name
PARP1
Gene Alias
ADPRT, ADPRT1, PARP, PARP-1, PPOL, pADPRT-1
Gene Description
poly (ADP-ribose) polymerase 1
Omim ID
173870Gene Ontology
HyperlinkGene Summary
This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes. [provided by RefSeq
Other Designations
ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)|ADP-ribosyltransferase NAD(+)|OTTHUMP00000035663|poly (ADP-ribose) polymerase family, member 1|poly(ADP-ribose) polymerase|poly(ADP-ribose) synthetase|poly(ADP-ribosyl)transferase
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Interactome
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Pathway
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Disease
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Publication Reference
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Chemotherapeutic stress selectively activates NF-kappa B-dependent AKT and VEGF expression in liver cancer-derived endothelial cells.
Meng F, Henson R, Patel T.
American Journal of Physiology. Cell Physiology 2007 May; 293(2):C749.
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Expression of tumor endothelial marker 7 mRNA and protein in the dorsal root ganglion neurons of the rat.
Lee HK, Kang DS, Seo IA, Choi EJ, Park HT, Park JI.
Neuroscience Letters 2006 May; 402(1-2):71.
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Cloning, characterization and neuronal expression profiles of tumor endothelial marker 7 in the rat brain.
Lee HK, Bae HR, Park HK, Seo IA, Lee EY, Suh DJ, Park HT.
Brain Research. Molecular Brain Research 2005 May; 136(1-2):189.
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Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R.
Nanda A, Buckhaults P, Seaman S, Agrawal N, Boutin P, Shankara S, Nacht M, Teicher B, Stampfl J, Singh S, Vogelstein B, Kinzler KW, St Croix B.
Cancer Research 2004 Dec; 64(23):8507.
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Hydroxylation at C4' or C6 is essential for apoptosis-inducing activity of flavanone through activation of the caspase-3 cascade and production of reactive oxygen species.
Ko CH, Shen SC, Chen YC.
Free Radical Biology & Medicine 2004 Apr; 36(7):897.
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Rutinoside at C7 attenuates the apoptosis-inducing activity of flavonoids.
Yen-Chou Chen, Shing-Chuan Shen, Hui-Yi Lin.
Biochemical Pharmacology 2003 Oct; 66(7):1139.
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Emodin induces apoptosis in human promyeloleukemic HL-60 cells accompanied by activation of caspase 3 cascade but independent of reactive oxygen species production.
Yen-Chou Chen, Shing-Chuan Shen, Woan-Ruoh Lee, Foun-Lin Hsu, Hui-Yi Lin, Ching-Huai Ko, Shi-Wen Tseng.
Biochemical Pharmacology 2002 Dec; 64(12):1713.
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Chemotherapeutic stress selectively activates NF-kappa B-dependent AKT and VEGF expression in liver cancer-derived endothelial cells.
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