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Western blot analysis of PARP on Jurkat cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-PARP antibody.
Immunofluorescent staining on BC3H1 cells
BD Transduction Laboratories™ Purified Mouse Anti-PARP
BD Transduction Laboratories™ Purified Mouse Anti-PARP
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Poly(ADP-ribose) polymerase (PARP) is a constitutively expressed, abundant nuclear protein. It has been referred to as "a molecular nick sensor" due to its recognition of, and catalytic activation by, single or double strand DNA breaks. The most critical ad extensively studied role of PARP is its participation in DNA base excision repair. Following binding to damaged DNA, PARP uses NAD+ to synthesize branched polymers of poly(ADP-ribose) on nuclear target proteins, including itself. Such modification of PARP increases its negative charge and results in loss of interactionwith DNA due to electrostatic repulsion. This opens the damaged DNA to DNA repair proteins. The poly(ADP-ribose) molecule is quickly degraded by poly (ADP-ribose) glycohydrolase that is found in association with PARP. PARP contains N-terminal DNA-binding domain (DBD), a central automodification domain that accepts poly (ADP-ribose), and a C-terminal catalytic domain. PARP is one of the earliest proteins targeted by caspase-3 during apoptosis. Although this protein is central to DNA repair, it has additional DNA-related functions that remain to be investigated.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Cherney BW, McBride OW, Chen D, et al. cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. Proc Natl Acad Sci U S A. 1987; 84(23):8370-8374. (Biology). View Reference
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Duriez PJ, Shah GM. Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death. Biochem Cell Biol. 1997; 75(4):337-349. (Biology). View Reference
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Jaiswal AS, Marlow BP, Gupta N, Narayan S. Beta-catenin-mediated transactivation and cell-cell adhesion pathways are important in curcumin (diferuylmethane)-induced growth arrest and apoptosis in colon cancer cells . Oncogene. 2002; 21(55):8414-8427. (Clone-specific: Western blot). View Reference
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Liao AT, Chien MB, Shenoy N, et al. Inhibition of constitutively active forms of mutant kit by multitargeted indolinone tyrosine kinase inhibitors. Blood. 2002; 100(2):585-593. (Clone-specific: Western blot). View Reference
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Saitoh H, Pizzi MD, Wang J. Perturbation of SUMOlation enzyme Ubc9 by distinct domain within nucleoporin RanBP2/Nup358. J Biol Chem. 2002; 277(7):4755-4763. (Clone-specific: Immunofluorescence). View Reference
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