Technical Data
P3113-02B
PARP Cleavage Site, p24, Asp214/Gly215 (Poly ADP-Ribose Polymerase)
Description:
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).

Applications:
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.
TypeIsotypeCloneGrade
MabIgG6k303Supernatant
SizeStorageShippingSourceHost
100ul -20°CBlue IceHumanRabbit
Concentration:
Immunogen:
A synthetic peptide corresponding to residues before the cleavage site of human PARP-1
Purity:
Supernatant
Form
Supplied as a liquid.
Specificity:
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).