MW 136.15 Da, Purity >99%. Poly(ADP-ribose) polymerase (PARP) inhibitor (Ki = 1.8 μM). Displays various biological actions including stimulation of angiogenesis. Additionally displays neuroprotective, anti-necrotic effects and shows free-radical scavenging ability.
(R)-limonene 6-monooxygenase, (S)-limonene 6-monooxygenase, (S)-limonene 7-monooxygenase, ADP ribosyltransferase, ADP ribosyltransferase (NAD+; poly (ADP ribose) polymerase), ADP ribosyltransferase NAD(+), ADP-ribosyltransferase diphtheria toxin-like 1, ADPRT, ADPRT 1, ARTD1, CP2C9_HUMAN, CPC9, CYP2C, CYP2C10, CYPIIC9, Cytochrome P-450MP, Cytochrome P450 2C9, Cytochrome P450 MP-4, Cytochrome P450 MP-8, Cytochrome P450 PB-1, Cytochrome P450, family 2, subfamily C, polypeptide 9, MGC149605, MGC88320, Microsomal monooxygenase, NAD(+) ADP-ribosyltransferase 1, OTTHUMP00000020135, P450 MP, P450 PB 1, P450IIC9, PARP, PARP1_HUMAN, PPOL, Poly (ADP ribose) synthetase, Poly (ADP-ribose) polymerase 1, Poly [ADP-ribose] polymerase 1, Poly(ADP ribose) polymerase, Poly(ADP-ribosyl)transferase, Poly[ADP ribose] synthetase 1, Poly[ADP-ribose] synthase 1, S-mephenytoin 4-hydroxylase, Xenobiotic monooxygenase, cytochrome P-450 S-mephenytoin 4-hydroxylase, flavoprotein-linked monooxygenase, msPARP, pADPRT-1, poly (ADP ribose) polymerase family, member 1, sPARP 1
MW 136.15 Da, Purity >99%. Poly(ADP-ribose) polymerase (PARP) inhibitor (Ki = 1.8 μM). Displays various biological actions including stimulation of angiogenesis. Additionally displays neuroprotective, anti-necrotic effects and shows free-radical scavenging ability.
Soluble in water to 100 mM.
Poly(ADP-ribose) polymerase (PARP) inhibitor (Ki = 1.8 μM). Displays various biological actions including stimulation of angiogenesis. Additionally displays neuroprotective, anti-necrotic effects and shows free-radical scavenging ability.
PARP1 also known as Poly (ADP-ribose) polymerase 1 is a protein with a molecular mass of approximately 113 kDa. This enzyme plays a mechanical role in the detection and repair of DNA damage through its ability to transfer ADP-ribose units onto acceptor proteins. It is expressed broadly in the nucleus of many cell types especially in tissues with high cellular turnover such as the bone marrow and intestinal epithelium. PARP1 is recognized for its interaction with NAD+ during DNA repair and is considered an important element in maintaining genomic stability.
This protein contributes to DNA repair pathways by sensing DNA strand breaks and recruiting repair enzymes. PARP1 operates as part of a repair complex that initiates the base excision repair process. It facilitates the binding of repair proteins like XRCC1 to damaged DNA sites promoting efficient repair. PARP inhibitors named after their ability to block PARP1 activity are a focus of significant research interest. These include compounds such as 2-aminobenzamide 3-aminobenzamide and other variants marketed for their therapeutic potential.
PARP1 functions prominently within the base excision repair (BER) and homologous recombination repair pathways. It interacts with proteins like DNA ligase III and DNA polymerase beta which are integral to BER. Additionally its role in the homologous recombination pathway connects it to proteins such as RAD51. These pathways are important for maintaining cellular integrity and preventing mutations making PARP1 a central player in the cell's defensive mechanisms against genomic instability.
PARP1 is heavily implicated in cancer especially breast and ovarian cancers. Both conditions often involve deficiencies in the BRCA1 and BRCA2 proteins. The dependency of cancer cells with BRCA mutations on PARP1 for DNA repair makes PARP inhibitors highly effective in treating these cancers. Additionally PARP1's involvement in apoptosis and inflammation ties it to neurodegenerative disorders like Parkinson's disease where disrupted DNA repair processes contribute to neuronal death. Effective targeting of PARP1 through pharmacological agents like those in the PARP inhibitor market shows promise in therapeutic strategies for these conditions.
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2D chemical structure image of ab141069, 3-Aminobenzamide (3-AB), PARP inhibitor
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