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SRP0193

Sigma-Aldrich

PARP2 Active human

recombinant, expressed in baculovirus infected insect cells, ≥60% (SDS-PAGE)

Synonym(s):

ADPRT2, ADPRTL3, NAD(+) ADP-ribosyltransferase 2, Poly (ADP-ribose) Polymerase 2

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

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.

NM_005484

UniProt accession no.

Q9UGN5

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.

Unit Definition

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.

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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 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 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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