P7605

Sigma-Aldrich

Anti-PARP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):
Anti-Poly[ADP-ribose] Polymerase
MDL number:
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 116 kDa

species reactivity

human

application(s)

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

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... PARP1(142)

General description

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).

Specificity

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

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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.

storage_class_code

12 - Non Combustible Liquids

WGK Germany

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

Certificate of Analysis

Certificate of Origin

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)
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)
Armel Nicolas et al.
Journal of virology, 84(17), 8871-8887 (2010-06-25)
Adeno-associated virus (AAV) is a human parvovirus that replicates only in cells coinfected with a helper virus, such as adenovirus or herpes simplex virus type 1 (HSV-1). We previously showed that nine HSV-1 factors are able to support AAV rep...

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