PARP Mouse, Unlabeled, Clone: 42, BD

Description

• Poly(ADP-ribose) polymerase (PARP) is a constitutively expressed, abundant nuclear protein
• It has been referred to as “a molecular nick sensor” due to its recognition of, and catalytic activation by, single or double strand DNA breaks
• The most critical ad extensively studied role of PARP is its participation in DNA base excision repair
• Following binding to damaged DNA, PARP uses NAD + to synthesize branched polymers of poly(ADP-ribose) on nuclear target proteins, including itself
• Such modification of PARP increases its negative charge and results in loss of interactionwith DNA due to electrostatic repulsion
• This opens the damaged DNA to DNA repair proteins
• The poly(ADP-ribose) molecule is quickly degraded by poly (ADP-ribose) glycohydrolase that is found in association with PARP
• PARP contains N-terminal DNA-binding domain (DBD), a central automodification domain that accepts poly (ADP-ribose), and a C-terminal catalytic domain
• PARP is one of the earliest proteins targeted by caspase-3 during apoptosis
• Although this protein is central to DNA repair, it has additional DNA-related functions that remain to be investigated
• Immunofluorescence, Western Blotting