Technical Data
P3113-07
PARP (Poly ADP-Ribose Polymerase)
Description:
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 PARPs 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).

Applications:
Suitable for use in Western Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Immunohistochemistry (Paraffin): 1:50
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. 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
100ul4C (-20C Glycerol)Blue IceHumanRabbit
Concentration:
Not determined
Immunogen:
Synthetic peptide (KLH coupled) corresponding to the caspase cleavage site in PARP.
Purity:
Purified by Protein A and immunoaffinity 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 full length PARP (116kD), as well as the large fragment (89kD) and small fragment (24kD) of PARP resulting from caspase cleavage. Does not crossreact with related proteins. Species Crossreactivity: Human, mouse, rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Satoh, M.S. & Lindahl, T., Nature 356: 356-358 (1992). 2. Lazebnik, Y.A., et al., Nature 371: 346-347 (1994). 3. Cohen, G.M., Biochem. J. 326: 1-16 (1997). 4. Nicholson, D.W., et al., Nature 376: 37-43 (1995). 5. Tewari, M., et al., Cell 81: 801-809 (1995). 6. Oliver, F.J., et al., J. Biol. Chem. 273: 33,533-33,539 (1998). 7. Li, J., et al., J. Biol. Chem. 277: 388-394 (2002). 8. Soldatenkov, V.A., et al., J. Biol. Chem. 277: 665-670 (2002).