Description CONCENTRATION 10 units/µl SOURCE Purified from E.  coli containing a recombinant plasmid harboring human PARP1 gene. SUBSTRATE SPECIFICITY PARP1 uses NAD+ as a substrate to catalyze poly(ADP-ribosyl)ation of target proteins involved  in  chromatin  structure  and  DNA  metabolism. PARP1 is stimulated by DNA-strand breaks and capable of auto-ribosylation. STORAGE Store at -20°C in a manual defrost freezer. For long-term storage, freeze at -80°C in working aliquots. APPLICATIONS Identification of inhibitors of PARP1 activity Quantitation of DNA Damage Investigation of PARP1 inactivation during apoptosis Western Blot Analysis Catalog # 4668-02K-01 includes : Catalog Number Description Qty 4668-500-01 Human PARP 1 Enzyme, HSA 4 Poly(ADP-ribose) polymerase-dependent energy depletion occurs through inhibition of glycolysis Shaida A. Andrabi, George K. E. Umanah, Calvin Chang, Daniel A. Stevens, Senthilkumar S. Karuppagounder, Jean-Philippe Gagné, Guy G. Poirier, Valina L. Dawson, and Ted M. Dawson PNAS, Jul 2014; 111: 10209 – 10214. http://www.pnas.org/cgi/content/abstract/111/28/10209 The N-terminal Region of Chromodomain Helicase DNA-binding Protein 4 (CHD4) Is Essential for Activity and Contains a High Mobility Group (HMG) Box-like-domain That Can Bind Poly(ADP-ribose) Ana P. G. Silva, Daniel P. Ryan, Yaron Galanty, Jason K. K. Low, Marylene Vandevenne, Stephen P. Jackson, and Joel P. Mackay J. Biol. Chem., Jan 2016; 291: 924 – 938. http://www.jbc.org/cgi/content/abstract/291/2/924 Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor “Jasna Lalic, Melanija Posavec Marjanovic, Luca Palazzo, Dragutin Perina, Igor Sabljic, Roko Zaja, Thomas Colby, Bruna Plese, Mirna Halasz, Gytis Jankevicius, Giselda Bucca, Marijan Ahel, Ivan Matic, Helena Cetkovic, Marija Luic, Andreja Mikoc, and Ivan Ahel” J. Biol. Chem., Oct 2016; 291: 23175 – 23187 http://www.jbc.org/cgi/content/abstract/291/44/23175 Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro “Ibtissam Talhaoui, Natalia A. Lebedeva, Gabriella Zarkovic, Christine Saint-Pierre, Mikhail M. Kutuzov, Maria V. Sukhanova, Bakhyt T. Matkarimov, Didier Gasparutto, Murat K. Saparbaev, Olga I. Lavrik, and Alexander A. Ishchenko” Nucleic Acids Res., Nov 2016; 44: 9279 – 9295 http://nar.oxfordjournals.org/cgi/content/abstract/44/19/9279 PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair Khoury-Haddad, H., Guttmann-Raviv, N., Khoury-Haddad, H., Ipenberg, I., Guttmann-Raviv, N., Huggins, D., Ipenberg, I., Jeyasekharan, A.D., Huggins, D., Ayoub, N., Jeyasekharan, A.D., and Ayoub, N., PNAS, Feb 2014; 111: E728 – E737. http://www.pnas.org/cgi/content/abstract/111/7/E728 Differential and Concordant Roles for Poly(ADP-Ribose) Polymerase 1 and Poly(ADP-Ribose) in Regulating WRN and RECQL5 Activities Prabhat Khadka, Joseph K. Hsu, Sebastian Veith, Takashi Tadokoro, Raghavendra A. Shamanna, Aswin Mangerich, Deborah L. Croteau, and Vilhelm A. Bohr Mol. Cell. Biol., Dec 2015; 35: 3974 – 3989. http://mcb.asm.org/cgi/content/abstract/35/23/3974