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Merck
모든 사진(1)

주요 문서

SRP0193

Sigma-Aldrich

PARP2 Active human

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

동의어(들):

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

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About This Item

UNSPSC 코드:
12352200
NACRES:
NA.32

생물학적 소스

human

재조합

expressed in baculovirus infected insect cells

분석

≥60% (SDS-PAGE)

양식

aqueous solution

분자량

92 kDa

포장

pkg of 10 μg

제조업체/상표

Sigma-Aldrich

농도

>0.02 mg/mL

기술

inhibition assay: suitable

solubility

water: soluble

NCBI 수납 번호

UniProt 수납 번호

응용 분야

life science and biopharma

배송 상태

dry ice

저장 온도

−70°C

유전자 정보

human ... PARP2(10038)

애플리케이션

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

단위 정의

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

물리적 형태

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

제조 메모

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

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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