P0996
PARP-1 human
recombinant, expressed in E. coli
Synonym(s):
NAD+ ADP-ribosyltransferase, Poly(ADP-ribose) Polymerase
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About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in E. coli
Quality Level
form
solution
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... PARP1(142)
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General description
Poly(ADP-ribose) polymerase 1 (PARP-1) is associated with the inflammation response during atherosclerosis.
Poly(ADP-ribose) polymerase 1 (PARP1) belongs to the PARP family which is highly conserved during evolution. PARP1 gene is localized at 1q42.12 in the human chromosome.
Application
PARP-1 human has been used in the GST-pull down assay for immunoprecipitation of Glutathione S-transferase (GST) or GST- cyclic GMP- AMP synthase (cGAS) (GST-cGAS). It has also been used in in vitro ribosylation assay.
PARP-1 is a nuclear enzyme that synthesizes ADP-ribose polymers from NAD+, specifically binds Zn2+ and DNA, and recognizes single-strand breaks in DNA. PARP1 has been used in a study to assess racial and tissue-specific cancer risk associated with polymorphism in the PARP1 gene. It has also been used in a study to investigate inhibitors of PARP-1 for potential cancer treatments.
Biochem/physiol Actions
PARP-1 is inactivated by cleavage into a 24kDA and 89kDA fragment by activated caspase-3 or caspase-7. This results in the decreased ability to repair DNA damage and an increase in apoptosis.
PARP-1, a nuclear enzyme that synthesizes ADP-ribose polymers from NAD, specifically binds Zn2+ and DNA, and recognizes single-strand breaks in DNA. It is involved in base excision repair, both short-patch and long-patch, rejoining DNA strand breaks and plays a role in p53 expression and activation. A high level of basal neuronal DNA damage and PARP activity has been reported in rat brain tissue. PARP-1 was shown to be required for HIV-1 integration into DNA. If PARP-1 is deficient there is no productive HIV-1 infection.
Poly(ADP-ribose) polymerase 1 (PARP1) is essential for diverse functions like DNA damage detection and repair, chromatin modification, cell differentiation, transcription and apoptotic cell death. It also plays a major role in spermatogenesis. Polymorphism in the gene PARP1 is associated with oligospermia and causes male infertility.
Unit Definition
One unit will incorporate 10 femptomole of poly(ADP-ribose) from NAD into 5 μg of immobilized histone proteins in 30 minutes at 22 °C in a 96 well plate.
Physical form
Supplied as a solution in 20 mM Tris-HCl, pH 8.0, 200 mM NaCl, 1 mM DTT, 0.1% Triton™-X 100, 50 % glycerol, and 0.1 mg/ml BSA.
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Nuclear cGAS suppresses DNA repair and promotes tumorigenesis
Liu H, et al.
Nature, 563(7729), 131-131 (2018)
S Muller et al.
Clinical immunology and immunopathology, 73(2), 187-196 (1994-11-01)
Poly(ADP-Ribose) polymerase (PARP) is a chromatin-associated enzyme that specifically binds to DNA strand breaks in a zinc-dependent manner. We describe here the presence of IgG antibodies reacting with recombinant human PARP in the serum of patients with systemic lupus erythematosus
PARP cleavage as a means of assessing apoptosis.
Peter Mullen
Methods in molecular medicine, 88, 171-181 (2003-11-25)
David Davidson et al.
Investigational new drugs, 31(2), 461-468 (2012-10-12)
Poly [ADP-ribose] polymerase-1 (PARP-1) localizes rapidly to sites of DNA damage and has been associated with various repair mechanisms including base excision repair (BER) and homologous recombination/non-homologous end joining (HRR/NHEJ). PARP-1 acts by adding poly-ADP ribose side chains to target
S Smith et al.
Science (New York, N.Y.), 282(5393), 1484-1487 (1998-11-20)
Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP), was identified and localized to human telomeres. Tankyrase binds to the telomeric protein TRF1 (telomeric repeat binding factor-1), a negative regulator of telomere
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