SRP0192
PARP1 Active human
recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)
Synonyme(s) :
ADPRT, NAD(+) ADP-ribosyltransferase 1, Poly (ADP-ribose) Polymerase 1
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
human
Produit recombinant
expressed in baculovirus infected insect cells
Pureté
≥80% (SDS-PAGE)
Forme
aqueous solution
Poids mol.
140 kDa
Conditionnement
pkg of 10 and 20 μg
Fabricant/nom de marque
Sigma-Aldrich
Conditions de stockage
avoid repeated freeze/thaw cycles
Concentration
>0.02 mg/mL
Technique(s)
inhibition assay: suitable
Numéro d'accès NCBI
Numéro d'accès UniProt
Application(s)
life science and biopharma
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... PARP1(142)
Description générale
Research area: Cell Signaling
Human PARP1 (GenBank Accession No. NM_001618), full length with N-terminal GST tag, MW = 140 kDa, expressed in a Baculovirus infected Sf9 cell expression system. Poly [ADP-ribose] polymerase 1 (PARP1) belongs to the DNA-dependent nuclear enzyme superfamily. Its structure includes an N-terminal with three zinc finger DNA-binding domains, an auto-modification domain with BRCT motif and a WGR domain having conserved tryptophan, glycine, and arginine residues, and a C-terminal catalytic domain with PARP signature sequence.
Human PARP1 (GenBank Accession No. NM_001618), full length with N-terminal GST tag, MW = 140 kDa, expressed in a Baculovirus infected Sf9 cell expression system. Poly [ADP-ribose] polymerase 1 (PARP1) belongs to the DNA-dependent nuclear enzyme superfamily. Its structure includes an N-terminal with three zinc finger DNA-binding domains, an auto-modification domain with BRCT motif and a WGR domain having conserved tryptophan, glycine, and arginine residues, and a C-terminal catalytic domain with PARP signature sequence.
Application
PARP1 Active human has been used in GST-PARP1 pulldown, to study the alterations in protein-protein interactions of sex determining region Y-box 2 (SOX2) upon O-GlcNAcylation. It has also been used in in vitro PARylation assay to investigate the effect of NR1D1 on DNA repair after damage induced by doxorubicin in breast cancer cells. It is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Actions biochimiques/physiologiques
PARPs comprise a set of enzymes that govern cellular processes such as DNA damage response, cell metabolism, chromatin remodeling, and transcriptional regulation. PARP1 detects and mends DNA breaks via base excision repair when DNA damage occurs. In the absence of PARP1 activity, damaged DNA accumulates, leading to impaired DNA replication.
Définition de l'unité
One unit of PARP incorporates 100 pmoles of poly(ADP) in 1 minute (room temperature) from NAD into acid-insoluble form.
Forme physique
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.
Notes préparatoires
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Fengxiao Zhang et al.
International journal of biological sciences, 16(15), 2868-2882 (2020-10-17)
Liver X receptor α (LXRα) controls a set of key genes involved in cholesterol metabolism. However, the molecular mechanism of this regulation remains unknown. The regulatory role of poly(ADP-ribose) polymerase 1 (PARP1) in cholesterol metabolism in the liver was examined.
SOX2 O-GlcNAcylation alters its protein-protein interactions and genomic occupancy to modulate gene expression in pluripotent cells
Myers SA, et al.
eLife, 5, e10647-e10647 (2016)
Caifeng Liu et al.
Journal of integrative plant biology, 59(7), 459-474 (2017-03-07)
Root organogenesis involves cell division, differentiation and expansion. The molecular mechanisms regulating root development are not fully understood. In this study, we identified poly(adenosine diphosphate (ADP)-ribose) polymerases (PARPs) as new players in root development. PARP catalyzes poly(ADP-ribosyl)ation of proteins by
NR1D1 Recruitment to Sites of DNA Damage Inhibits Repair and Is Associated with Chemosensitivity of Breast Cancer
Ka NL, et al.
Cancer Research, 77 (9), 2453?2463-2453?2463 (2017)
Anneli Andersson et al.
Nucleic acids research, 44(16), 7630-7645 (2016-05-21)
Harmful oxidation of proteins, lipids and nucleic acids is observed when reactive oxygen species (ROS) are produced excessively and/or the antioxidant capacity is reduced, causing 'oxidative stress'. Nuclear poly-ADP-ribose (PAR) formation is thought to be induced in response to oxidative
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