SRP0192
PARP1 Active human
recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)
Sinónimos:
ADPRT, NAD(+) ADP-ribosyltransferase 1, Poly (ADP-ribose) Polymerase 1
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Acerca de este artículo
NACRES:
NA.32
UNSPSC Code:
12352200
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Permítanos ayudarleNombre del producto
PARP1 Active human, recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)
biological source
human
recombinant
expressed in baculovirus infected insect cells
assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
140 kDa
packaging
pkg of 10 and 20 μg
manufacturer/tradename
Sigma-Aldrich
storage condition
avoid repeated freeze/thaw cycles
concentration
>0.02 mg/mL
technique(s)
inhibition assay: suitable
NCBI accession no.
UniProt accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PARP1(142)
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.
Biochem/physiol Actions
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.
General description
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.
Other Notes
One unit of PARP incorporates 100 pmoles of poly(ADP) in 1 minute (room temperature) from NAD into acid-insoluble form.
Physical form
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.
Preparation Note
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.
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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DNA repair, 96, 102977-102977 (2020-10-12)
The nucleoside analog 5-aza-2'-deoxycytidine (5-aza-dC) is used to treat some hematopoietic malignancies. The mechanism of cell killing depends upon DNMT1, but is otherwise not clearly defined. Here we show that PARP1 forms covalent DNA adducts in human lymphoblast or fibroblasts
Proteolysis-targeting chimeras: A promising technique in cancer therapy for gaining insights into tumor development
Lv M, et al.
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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
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.
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
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