Mouse Monoclonal Poly (ADP-Ribose) Polymer antibody. Suitable for IHC-Fr and reacts with Chemical samples. Cited in 62 publications.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 1% BSA, 0.87% Sodium chloride, 0.242% Tris
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Poly ADP ribose, pADPr
Mouse Monoclonal Poly (ADP-Ribose) Polymer antibody. Suitable for IHC-Fr and reacts with Chemical samples. Cited in 62 publications.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 1% BSA, 0.87% Sodium chloride, 0.242% Tris
This antibody reacts with poly (ADP-Ribose) Polymer synthesized by a variety of poly(ADP- ribose) polymerases (PARP)-related enzymes including PARP1, 2, 3, tankyrase, vPARP, sPARP and others.
The antibody does not cross-react with ADP-ribose, 5'-AMP, or yeast RNA as tested by ELISA.
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Poly (ADP-Ribose) Polymerase often abbreviated as PARP is an enzyme that plays an important role in cellular processes. PARP catalyzes the addition of ADP-ribose units from NAD+ to target proteins—a process known as poly(ADP-ribosyl)ation. This modification is important for modulating protein function. The enzyme has a molecular weight of approximately 116 kDa. PARP is located mainly in the nucleus of cells and shows high expression in tissues with elevated cellular proliferation and metabolism such as the brain and testis.
PARP is integral to the DNA damage response mechanism in eukaryotic cells. It detects and signals single-strand DNA breaks inducing repair by recruiting DNA repair complexes. PARP collaborates with XRCC1 to facilitate the base excision repair pathway. As a part of these complexes PARP’s activity ensures cell survival under stress conditions. In concert with other poly (ADP-ribose) molecules PARP also influences chromatin structure impacting gene expression.
PARP functions prominently within the signaling responses to DNA damage and apoptosis pathways. It associates closely with proteins like ATM and ATR as they coordinate cell cycle checkpoints. PARP’s enzymatic activity modulates the synthesis of poly (ADP-ribose) which interacts with other repair proteins to drive DNA strand repair. Furthermore the activity of PARP connects to the tumor suppressor protein p53 influencing cellular fate decisions between cell survival and apoptosis.
PARP is heavily studied in the context of cancer and neurodegenerative diseases. Elevated PARP activity is recognized in various cancers as it helps tumor cells survive DNA damage. PARP inhibitors have emerged as therapeutic agents targeting cancers with BRCA1/2 mutations. Moreover in neurodegenerative diseases like Parkinson’s PARP’s excessive activation can lead to cell death. The interaction of PARP with other proteins such as α-synuclein in Parkinson’s highlights its multifaceted role in disease pathogenesis.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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Immunohistochemistry of rat livers treated with diethylnitrosamine (200 mg/kg) and stained with ab14459 diluted 1/100. After treatment livers were removed and rapidly processed 10 hr later, at peak polymer induction. Left hand side image was from diethylnitrosamine untreated liver tissue and right one represents DEN treated sections.
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