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Key Documents

P7605

Sigma-Aldrich

Anti-PARP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Poly[ADP-ribose] Polymerase

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 116 kDa

Espèces réactives

human

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PARP1(142)

Description générale

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).

Spécificité

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

Immunogène

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

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
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)
Cytotoxicity of ORF3 proteins from a nonpathogenic and a pathogenic porcine circovirus.
Chaiyakul M, et al.
Journal of virology, 84(21), 11440-11447 (2010)
PARP-1 activation requires local unfolding of an autoinhibitory domain.
Dawicki-McKenna JM, et al.
Molecular Cell, 60(5), 755-768 (2015)
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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