Technical Data
PARP Cleavage Site, p24, Asp214/Gly215 (Poly ADP-Ribose Polymerase)
Poly (ADP-ribose) polymerase (PARP) is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair (1). As a marker for apoptosis, PARP is cleaved in vitro by many caspases, and in vivo by Caspase-3 (2,3). Existing as a 116kD nuclear protein, PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments of 29kD and 85kD (2,4).

Suitable for use in Flow Cytometry, Western Blot, Immunoprecipitation, Immunohistochemistry, Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Flow Cytometry: 1:50
Western Blot: 1:10,000-50,000
Immunohistochemistry: 1:100
Immunocytochemistry: 1:250
Immunoprecipitation: 1:50

Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Freeze at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul -20°CBlue IceHumanRabbit
A synthetic peptide corresponding to residues before the cleavage site of human PARP-1
Supplied as a liquid.
Recognizes p25 cleaved-form of human PARP-1
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Ikejima, M, et al. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J. Biol. Chem. 265: 21907–13 (1990). 2. Lazebnik, Y.A., et al. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371: 346–347 (1994). 3. Tewari, M, et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801–9 (1995). 4. Kaufmann, S.H., et al. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53: 2976–3985 (1993).