P248

Sigma-Aldrich

Monoclonal Anti-PARP antibody produced in mouse

clone C-2-10, ascites fluid

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

Quality Level

biological source

mouse

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

primate, mouse, hamster, rat

should not react with

avian

application(s)

immunocytochemistry: 1:100-1:1,000
immunofluorescence: 1:100-1:1,000
immunohistochemistry: 1:10-1:100
western blot: 1:500-1:1,000

isotype

IgG1

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

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.

storage_class_code

12 - Non Combustible Liquids

WGK Germany

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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)
PARP inhibition: PARP1 and beyond.
Rouleau M, et al.
Nature Reviews. Cancer, 10, 293-301 (2010)
Effects of single, double or triple combinations of octreotide, galanin and serotonin on a human pancreatic cancer cell line Article (PDF Available) ?in?Histology and histopathology 20(2):537-41 ? May
lineV. Tjomsland and M. El-Salhy
Histology and Histopathology (2005)
PARP-1 protein expression in glioblastoma multiforme
Galia A, et al.
European Journal of Histochemistry (2012)
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)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service