PARP2 Antibody

Poly (ADP-Ribose) Polymerase 2 (PARP-2) is a member of the PARP family of proteins, which play a crucial role in various cellular processes, including DNA repair, transcription, and chromatin remodeling. PARP-2, along with PARP-1, is involved in the cellular response to DNA damage and is essential for maintaining genomic stability.

PARP-2 is a nuclear enzyme that catalyzes the transfer of ADP-ribose units from NAD+ to target proteins, forming poly (ADP-ribose) chains. This process, known as poly (ADP-ribosyl)ation, is a post-translational modification that regulates protein function and interactions. PARP-2 has a DNA-binding domain, an automodification domain, and a catalytic domain, which are essential for its activity .

PARP-2 is activated by DNA strand breaks and works in conjunction with PARP-1 to detect and repair DNA damage. Upon activation, PARP-2 synthesizes poly (ADP-ribose) chains that recruit DNA repair proteins to the site of damage. This process is critical for the repair of single-strand breaks and the maintenance of genomic integrity .

PARP-2 interacts with several proteins involved in the DNA damage response and cell cycle regulation. It has been shown to associate with centromeres in a cell-cycle-dependent manner, accumulating at centromeres during prometaphase and metaphase, and disassociating during anaphase . PARP-2 also interacts with PARP-1, Cenpa, Cenpb, and Bub3, but not with Cenpc .

PARP inhibitors (PARPi) have emerged as promising therapeutic agents for the treatment of cancers with deficiencies in homologous recombination repair, such as BRCA1/2-mutated tumors. PARP-2, along with PARP-1, is a target for these inhibitors, which block poly (ADP-ribosyl)ation and trap PARP proteins on damaged DNA, leading to cell death . However, resistance to PARPi remains a challenge, and ongoing research aims to develop combinatorial treatment strategies to overcome this resistance .