Technical Data
PARP (Poly ADP-Ribose Polymerase)
PARP, a 116kD nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair predominantly in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates PARP's amino-terminal DNA binding domain (24kD) from its carboxy-terminal catalytic domain (89kD) (2,4). PARP is important for cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

Suitable for use in Western Blot, Immunoprecipitation and Immunofluorescence/Immunocytochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Immunoprecipitation: 1:200
Immunofluorescence/Immunocytochemistry: 1:800
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IceHumanRabbit
Not determined
Synthetic peptide corresponding to residues surrounding Gly623 of human PARP.
Supplied as a liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, <0.02% sodium azide, 50% glycerol.
Recognizes endogenous levels of total full-length human PARP at ~116kD and the large fragment (89kD) produced by caspase cleavage. Does not react with PARP2 or PARP3. Species Crossreactivity: monkey, mouse, rat
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
(1) Satoh, M.S. and Lindahl, T. (1992) Nature 356,
(2) Lazebnik, Y.A. et al. (1994) Nature 371, 346347.
(3) Cohen, G.M. (1997) Biochem. J. 326, 116.
(4) Nicholson, D.W. et al. (1995) Nature 376, 3743.
(5) Tewari, M. et al. (1995) Cell 81, 801809.
(6) Oliver, F.J. et al. (1998) J. Biol. Chem. 273,