SRP0193
PARP2 Active human
recombinant, expressed in baculovirus infected insect cells, ≥60% (SDS-PAGE)
別名:
ADPRT2, ADPRTL3, NAD(+) ADP-ribosyltransferase 2, Poly (ADP-ribose) Polymerase 2
製品名
PARP2 Active human, recombinant, expressed in baculovirus infected insect cells, ≥60% (SDS-PAGE)
biological source
human
recombinant
expressed in baculovirus infected insect cells
assay
≥60% (SDS-PAGE)
form
aqueous solution
mol wt
92 kDa
packaging
pkg of 10 μg
manufacturer/tradename
Sigma-Aldrich
concentration
>0.02 mg/mL
technique(s)
inhibition assay: suitable
solubility
water: soluble
NCBI accession no.
UniProt accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PARP2(10038)
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
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, 20% 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.
保管分類
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage.
Riccio AA
Nucleic Acids Research, 44(4), 1691-1702 (2016)
PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.
Ame JC
The Journal of Biological Chemistry, 274(25), 17860-17868 (1999)
PARP-2 regulates cell cycle-related genes through histone deacetylation and methylation independently of poly(ADP-ribosyl)ation.
Liang YC
Biochemical and Biophysical Research Communications, 431(1), 58-64 (2013)
Xiao-Nan Zhang et al.
Nature communications, 10(1), 4196-4196 (2019-09-15)
Nicotinamide adenine dinucleotide (NAD+)-dependent ADP-ribosylation plays important roles in physiology and pathophysiology. It has been challenging to study this key type of enzymatic post-translational modification in particular for protein poly-ADP-ribosylation (PARylation). Here we explore chemical and chemoenzymatic synthesis of NAD+
Sharon McGonigle et al.
Oncotarget, 6(38), 41307-41323 (2015-10-30)
Inhibition of Poly(ADP-ribose) Polymerase1 (PARP1) impairs DNA damage repair, and early generation PARP1/2 inhibitors (olaparib, niraparib, etc.) have demonstrated clinical proof of concept for cancer treatment. Here, we describe the development of the novel PARP inhibitor E7449, a potent PARP1/2
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