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Recombinant (partial), N-terminal 2/3 sequence of PARP
Formulation:
This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide. Final antibody concentration is 0.5 mg/ml.
Preparation:
The antibody was purified by affinity chromatography, and conjugated with biotin under optimal conditions. The solution is free of unconjugated biotin.
Concentration:
0.5 mg/ml
Storage & Handling:
The antibody solution should be stored undiluted at 4°C. Do not freeze.
Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 μg antibody per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Hela cell lysate was resolved by electrophoresis, transferred to nitrocellulose and probed with anti-PARP antibody. Proteins were visualized using a donkey anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Hela cells stained with PE-conjugated antibody against PARP
Hela cells stained with DAPI to indicate nuclei
Overlay of panels A and B, showing the nuclear localization of PARP
PARP (Poly (ADP-ribose) polymerase) is a 113 kD nuclear protein that can exist as a homo- or hetero-dimer. This protein acts as a molecular "nick sensor" and functions in base excision repair, poly(ADP-ribosyl)ation of acceptor proteins involved in chromatin architecture and DNA metabolism and participates in protein modification to enhance or repress transcription. PARP is ribosylated by PARP2 and is a target for caspase cleavage during apoptosis. PARP interacts with proteins in the base excision repair complex containing at least XRCC1, PARP2, POLB and LIG3. In addition PARP forms heterodimers with PARP2, and interacts with PARP3. The 5A5 monoclonal antibody recognizes the N-terminal region of human and mouse PARP and has been shown to be useful for Western blotting and immunofluorescence staining.
Other Names:
Poly (ADP-ribose) polymerase
Structure:
PARP family, BRCT domain, homo- or hetero-dimer; 113 kD
Distribution:
Nuclear
Function:
Molecular "nick sensor"; base excision repair, catalyzes poly(ADP-ribosyl)ation of acceptor proteins involved in chromatin architecture, DNA metabolism; protein modification may enhance or repress transcription
Component of a base excision repair complex containing at least XRCC1, PARP2, POLB and LIG3. Heterodimerizes with PARP2, interacts with PARP3, modifies TATA-BP, YY1, Sp1, NF-B, p53 and others
Antigen References:
1. Cherney B, et al. 1987. P. Natl. Acad. Sci. USA 84:8370. 2. Ikejima M, et al. 1990. J. Biol. Chem. 265:21907. 3. Ying W, et al. 2001. P. Natl. Acad. Sci. USA 98:12227. 4. Noel G, et al. 2003. BMC Cell Biol. 4:7.
*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/terms). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.
This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Purified anti-PARP
Hela cell lysate was resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-PARP antibody. Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Hela cells were stained with PE anti-PARP antibody and DAPI. The image shows nuclear localization of PARP.
Biotin anti-PARP
Hela cell lysate was resolved by electrophoresis, transferred to nitrocellulose and probed with anti-PARP antibody. Proteins were visualized using a donkey anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Hela cells stained with PE-conjugated antibody against PARP
Hela cells stained with DAPI to indicate nuclei
Overlay of panels A and B, showing the nuclear localization of PARP
