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Key Documents

SRP0193

Sigma-Aldrich

PARP2 Active human

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

同義詞:

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

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About This Item

分類程式碼代碼:
12352200
NACRES:
NA.32

生物源

human

重組細胞

expressed in baculovirus infected insect cells

化驗

≥60% (SDS-PAGE)

形狀

aqueous solution

分子量

92 kDa

包裝

pkg of 10 μg

製造商/商標名

Sigma-Aldrich

濃度

>0.02 mg/mL

技術

inhibition assay: suitable

溶解度

water: soluble

NCBI登錄號

UniProt登錄號

應用

life science and biopharma

運輸包裝

dry ice

儲存溫度

−70°C

基因資訊

human ... PARP2(10038)

應用

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

單位定義

One unit of PARP incorporates 100 pmoles of poly(ADP) in 1 minute (room temperature) from NAD into acid-insoluble form.

外觀

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 20% glycerol and 3 mM DTT.

準備報告

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.

儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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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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