PARP Enzyme High Specific Activity

Newer Version Available: 4668-100-01
NEW

Discontinued Product

4668-500-01 has been discontinued and is replaced by 4668-100-01.

Product Details
Citations (8)
FAQs
Reviews

PARP Enzyme High Specific Activity Summary

Purified from E. coli containing a recombinant plasmid harboring human PARP1 gene.

Key Benefits

• Identification of inhibitors of PARP1 activity Quantitation of DNA Damage Investigation of PARP1 inactivation during apoptosis Western Blot Analysis

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.

Concentration

10 units/µl

Specifications

Shipping Conditions
The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended on the product label.
Storage
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Species
Human

Limitations

For research use only. Not for diagnostic use.

Product Datasheets

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.

8 Citations: Showing 1 - 8
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  1. 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
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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

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