PARP Enzyme High Specific Activity
PARP Enzyme High Specific Activity SummaryPurified from E. coli containing a recombinant plasmid harboring human PARP1 gene.
• Identification of inhibitors of PARP1 activity Quantitation of DNA Damage Investigation of PARP1 inactivation during apoptosis Western Blot Analysis
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.
For research use only. Not for diagnostic use.
Complete Your Research
Citations for PARP Enzyme High Specific Activity
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 8
Filter your results:
Molecular tweezers with varying anions: a comparative study.
Authors: Dutt S, Wilch C, Gersthagen T, Talbiersky P, Bravo-Rodriguez K, Hanni M, Sanchez-Garcia E, Ochsenfeld C, Klarner F, Schrader T
J Org Chem, 0;78(13):6721-34. 0
Poly-ADP ribosylation of PTEN by tankyrases promotes PTEN degradation and tumor growth.
Authors: Li N, Zhang Y, Han X, Liang K, Wang J, Feng L, Wang W, Songyang Z, Lin C, Yang L, Yu Y, Chen J
Genes Dev, 0;29(2):157-70. 0
Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination.
Authors: Wang Z, Michaud G, Cheng Z, Zhang Y, Hinds T, Fan E, Cong F, Xu W
Genes Dev, 0;26(3):235-40. 0
Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor.
Authors: Lalic J, Posavec Marjanovic M, Palazzo L, Perina D, Sabljic I, Zaja R, Colby T, Plese B, Halasz M, Jankevicius G, Bucca G, Ahel M, Matic I, Cetkovic H, Luic M, Mikoc A, Ahel I
J Biol Chem, 0;291(44):23175-23187. 0
2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation.
Authors: MacPherson L, Tamblyn L, Rajendra S, Bralha F, McPherson J, Matthews J
Nucleic Acids Res, 0;41(3):1604-21. 0
Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair.
Authors: King B, Cooper K, Liu K, Hudson L
J Biol Chem, 0;287(47):39824-33. 0
Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro.
Authors: Talhaoui I, Lebedeva N, Zarkovic G, Saint-Pierre C, Kutuzov M, Sukhanova M, Matkarimov B, Gasparutto D, Saparbaev M, Lavrik O, Ishchenko A
Nucleic Acids Res, 0;44(19):9279-9295. 0
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).
Authors: Silva A, Ryan D, Galanty Y, Low J, Vandevenne M, Jackson S, MacKay J
J Biol Chem, 0;291(2):924-38. 0
No product specific FAQs exist for this product, however you mayView all FAQs
Reviews for PARP Enzyme High Specific Activity
There are currently no reviews for this product. Be the first to review PARP Enzyme High Specific Activity and earn rewards!
Have you used PARP Enzyme High Specific Activity?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image