Technical Data
P3113-07B
PARP, Cleavage Site (Asp214) (Poly ADP-Ribose Polymerase)
Description:
PARP, a 116kD nuclear poly (ADPribose) polymerase, appears to be involved in DNA repair predominantly in response to environmental stress (1). This protein can be cleaved by many ICElike 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 N-terminal DNA binding domain (24kD) from its C-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).

Recommended Dilution: Western Blot: 1:1000 Immunocytochemistry (ABC) 1:100 Immunocytochemistry (IF) 1:100

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, store 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
PabIgGAffinity Purified
SizeStorageShippingSourceHost
100ul-20°CBlue IceMouseRabbit
Concentration:
As reported
Immunogen:
Synthetic peptide (KLH coupled) corresponding to C-terminal residues adjacent to Asp214 in mouse PARP.
Purity:
Purified by Protein A affinity chromatography.
Form
Supplied as liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. No preservative added.
Specificity:
Detects endogenous levels of the large fragment (89kD) of mouse PARP produced by caspase cleavage. Does not react with full length PARP.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Satoh, M.S. and Lindahl, T. (1992) Nature 356, 356–358. 2. Lazebnik, Y.A. et al. (1994) Nature 371, 346–347. 3. Cohen, G.M. (1997) Biochem. J. 326, 1–16. 4. Nicholson, D.W. et al. (1995) Nature 376, 37–43. 5. Tewari, M. et al. (1995) Cell 81, 801–809. 6. Oliver, F.J. et al. (1998) J. Biol. Chem. 273, 33533–33539.