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P7605

Sigma-Aldrich

Anti-PARP antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 116 kDa

species reactivity

human

technique(s)

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PARP1(142)

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This Item
SAB4500487SAB5700016SAB1300765
antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

saturated ammonium sulfate (SAS) precipitated

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

conjugate

unconjugated

conjugate

unconjugated

conjugate

-

conjugate

unconjugated

Gene Information

human ... PARP1(142)

Gene Information

human ... PARP1(142)

Gene Information

human ... PARP1(142)

Gene Information

human ... PARP16(214424)

clone

polyclonal

clone

polyclonal

clone

polyclonal

clone

polyclonal

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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

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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)
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)
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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