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P248

Sigma-Aldrich

Monoclonal Anti-PARP antibody produced in mouse

clone C-2-10, ascites fluid

Synonym(s):

Monoclonal Anti-Poly[ADP-ribose] Polymerase

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About This Item

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

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

C-2-10, monoclonal

mol wt

antigen 116 kDa (PARP)
antigen 85 kDa (prICE/caspase-3 cleavage product)

species reactivity

hamster, rat, mouse, primate

should not react with

avian

technique(s)

ELISA: suitable (Assay Dependent)
immunocytochemistry: suitable (Assay Dependent)
immunofluorescence: suitable (Assay Dependent)
immunohistochemistry: 1:10-1:100
western blot: 1:500

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Monoclonal Anti-PARP (mouse IgG1) is produced by immunizing mice with purified calf thymus poly (ADPribose) polymerase as the antigen. This antibody recognizes a 116kDa protein which corresponds to PARP and the 85kDa apoptosis induced cleavage product of prICE (proteinase resembling interleukin 1b-converting enzyme) and CPP32 (cysteine protease). It also recognizes PARP from mouse, rat, hamster and primate sources, but fails to detect avian PARP.
Poly (ADP-ribose) polymerase 1 (PARP1)/PARP is encoded by the gene mapped to human chromosome 1q42. It is a nuclear protein with molecular mass of 113kDa and is characterized with three functional domains. It belongs to the PARP superfamily.
PARP1 poly(ADP-ribose) polymerase 1) is also termed as ARTD1. It is an abundant nuclear protein that belongs to the PARP family. This gene is located on human chromosome 1q42.

Specificity

The antibody reacts with PARP (116 kDa) and the 85 kDa apoptosis-induced cleavage product of prICE (proteinase resembling interleukin 1β-converting enzyme) and caspase-3 (CPP32 cysteine protease).

Immunogen

calf thymus PARP. The epitope is found between amino acids 216-375 in the DNA-binding domain of PARP.

Application

Monoclonal Anti-PARP (Cleaved-Asp214) antibody has been used in western blotting and immunohistochemical staining.

Biochem/physiol Actions

PARP1 poly(ADP-ribose) polymerase 1) and its enzymatic product PAR controls cellular processes like DNA repair, chromatin remodeling, transcription and cell death. PARP1 regulates transcription. PARP1 can induce or block homologous recombination (HR).
Poly (ADP-ribose) polymerase 1 (PARP1)/PARP participates in DNA repair. It facilitates homologous recombination. PARP controls transcription by regulating chromatin structure, altering DNA methylation patterns, acting as a co-regulator of transcription factors and interacting with chromatin insulators. It also plays an important role in the protection of cardiovascular system. PARP1 is also implicated in the maintenance of genomic stability.

Physical form

Solution in mouse ascites fluid containing 0.02% 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.

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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Deregulated expression of the polycomb-group protein SUZ12 target genes characterizes mantle cell lymphoma
Martin-Perez D, et al.
The American Journal of Pathology (2010)
PARP-1 protein expression in glioblastoma multiforme
A. Galia, et al.
European Journal of Histochemistry, 56 (2012)
Trapping of PARP1 and PARP2 by Clinical PARP Inhibitors
Murai J, et al.
Cancer Research, 72(21), 5588-5599 (2012)
PARP-1 protein expression in glioblastoma multiforme
Galia A, et al.
European Journal of Histochemistry (2012)
Kinetics of poly(ADP-ribosyl)ation, but not PARP1 itself, determines the cell fate in response to DNA damage in vitro and in vivo
Schuhwerk H, et al.
Nucleic Acids Research (2017)

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