Human PARP 1 Enzyme, High Specific Activity

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High specific activity PARP1 (PARP-HSA) is used in Trevigen’s PARP Assay Kits. The specific activity serves as a measure of enzyme purity, with greater than 95% purity for PARP-HSA. PARP1 is activated by 10X Activated DNA, which can be assayed using Trevigen’s Universal or PARP/Apoptosis Assay Kits.

Available Size(s): 1,000 units, 20,000 units, 5,000 units Catalog Number: 4668-02K-01 Category:


10 units/µl
Purified from E.  coli containing a recombinant plasmid harboring human PARP1 gene.
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.
Store at -20°C in a manual defrost freezer. For long-term storage, freeze at -80°C in working aliquots.
Identification of inhibitors of PARP1 activity
Quantitation of DNA Damage
Investigation of PARP1 inactivation during apoptosis
Western Blot Analysis





Material Safety Data Sheet(s)

msds_4668-100-01 PARP HSA Enzyme

msds_4668-500-01 PARP HSA Enzyme

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.

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.

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

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

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.

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.