SRP0192
PARP1 Active human
recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)
Sinônimo(s):
ADPRT, NAD(+) ADP-ribosyltransferase 1, Poly (ADP-ribose) Polymerase 1
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.32
Produtos recomendados
fonte biológica
human
recombinante
expressed in baculovirus infected insect cells
Ensaio
≥80% (SDS-PAGE)
forma
aqueous solution
peso molecular
140 kDa
embalagem
pkg of 10 and 20 μg
fabricante/nome comercial
Sigma-Aldrich
condição de armazenamento
avoid repeated freeze/thaw cycles
concentração
>0.02 mg/mL
técnica(s)
inhibition assay: suitable
nº de adesão NCBI
nº de adesão UniProt
aplicação(ões)
life science and biopharma
Condições de expedição
dry ice
temperatura de armazenamento
−70°C
Informações sobre genes
human ... PARP1(142)
Descrição geral
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.
Aplicação
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.
Ações bioquímicas/fisiológicas
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.
Definição da unidade
One unit of PARP incorporates 100 pmoles of poly(ADP) in 1 minute (room temperature) from NAD into acid-insoluble form.
forma física
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.
Nota de preparo
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.
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (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.
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
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)
Kostantin Kiianitsa et al.
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.
Cancer Letters, 539, 215716-215716 (2022)
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