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Merck
모든 사진(2)

주요 문서

P7605

Sigma-Aldrich

Anti-PARP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

동의어(들):

Anti-Poly[ADP-ribose] Polymerase

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

형태

buffered aqueous solution

분자량

antigen 116 kDa

종 반응성

human

기술

indirect immunofluorescence: 1:100 using cultured MCF7 cells
microarray: suitable
western blot: 1:200 using MCF7 human mammary adenocarcinoma cell extract

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... PARP1(142)

일반 설명

Poly (ADP-ribose) Polymerase (PARP, EC 2.4.2.30) is an abundant, zinc-dependent eukaryotic nuclear enzyme. PARP is composed of an N-terminal DNA binding domain, a central regulatory automodification domain that accepts poly (ADP-ribose) and a C-terminal catalytic domain. PARP contains a conserved proteinase recognition site (DEVD) a target for several caspases (e.g. Caspase 2, 3, 6, 7 and 9).

특이성

By immunoblotting, the antibody may also react with a cleavage product of 85 kDa in some preparations.

면역원

synthetic peptide corresponding to amino acids 2-20 of human or bovine PARP with a C-terminal added lysine, conjugated to KLH.

애플리케이션

Anti-PARP antibody produced in rabbit has been used in western blotting.

생화학적/생리학적 작용

Poly (ADP-ribose) Polymerase (PARP) specifically recognizes single or double strand DNA breaks produced by various genotoxic agents. Thus, it is a molecular nick sensor, that following binding to damaged DNA converts nicotinamide adenine dinucleotide (NAD) to nicotinamide and branched polymers of various poly (ADP-ribose)(PAR) on glutamate residues of a limited number of nuclear acceptor proteins, including PARP itself. The increased negative charge of modified PARP results in loss of interaction with DNA due to electrostatic repulsion. The poly (ADP-ribose) moiety is quickly degraded by a PARP-associated Poly (ADP-ribose) glycohydrolase. Also, PARP modification of nuclear proteins is involved in chromatin structure formation, the regulation of differentiation, proliferation, development, apoptosis, gene expression, response to heart and brain ischemia/reperfusion, and malignant transformation. Rapid activation of PARP may deplete NAD, slow glycolysis, electron transport and ATP formation and cause cell dysfunction and cell death. Cleavage of PARP into fragments of 24 kD and 89 kDa by caspase-3 is an early marker of apoptosis. Necrotic cleavage of PARP generates different fragments.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide

면책조항

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


시험 성적서(COA)

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문서 라이브러리 방문

The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger.
Eustermann S, et al.
Journal of molecular biology, 407(1), 149-170 (2011)
Role of poly (ADP-ribose) polymerase (PARP) cleavage in apoptosis Caspase 3-resistant PARP mutant increases rates of apoptosis in transfected cells.
Boulares AH, et al.
The Journal of biological chemistry, 274(33), 22932-22940 (1999)
PARP-1 activation requires local unfolding of an autoinhibitory domain.
Dawicki-McKenna JM, et al.
Molecular Cell, 60(5), 755-768 (2015)
Cytotoxicity of ORF3 proteins from a nonpathogenic and a pathogenic porcine circovirus.
Chaiyakul M, et al.
Journal of virology, 84(21), 11440-11447 (2010)
Yangke He et al.
Cell death & disease, 11(5), 358-358 (2020-05-14)
Emerging evidence has revealed that aberrantly expressed circular RNAs (circRNAs) play vital roles in tumorigenesis and progression of diverse human malignancies. Although an existing literature has elucidated the regulatory role of circZNF609 in breast cancer, the crucial function that circZNF609

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