Recombinant Human Poly [Adp-Ribose] Polymerase 2 (PARP2) Protein (His)

• Purity: Greater than 85% as determined by SDS-PAGE.
• Host Species: Human
• Accession: Q9UGN5
• Gene: PARP2
• CAT.NO: B000004
• Product Name: Recombinant Human Poly [Adp-Ribose] Polymerase 2 (PARP2) Protein (His)
• Source: E.coli
• Protein Expression Range: 1-583aa
• Tag: N-6His
• Molecular Mass: 72.2 kDa
• Form: Liquid or Lyophilized powder
• Buffer: Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
• Storage: 1. Store at -20¡«C/-80¡«C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4¡«C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20¡«C/-80¡«C. Protein in lyophilized powder form is stable for up to 12 months at -20¡«C/-80¡«C.

Poly-ADP-ribosyltransferase PARP2 plays a pivotal role in DNA repair by mediating poly-ADP-ribosylation of proteins. It catalyzes the transfer of ADP-ribosyl groups from NAD+ to target residues, primarily serine, glutamate, and aspartate. The process forms polymers averaging 20-30 ADP-ribose units. Serine ADP-ribosylation, the predominant response to DNA damage, occurs upon interaction with HPF1, which modifies PARP2’s active site to confer serine specificity. Without HPF1, PARP2 targets glutamate and aspartate residues.
PARP2 recognizes double-strand DNA breaks, binding to damaged chromatin and recruiting HPF1 to promote serine ADP-ribosylation of proteins like histones. This activity decompacts chromatin, enabling the recruitment of repair factors to restore DNA integrity. While HPF1 facilitates serine-specific ADP-ribosylation, it also limits PARP2’s polymerase activity, ensuring controlled poly-ADP-ribose chain length.
PARP2 also forms branched poly-ADP-ribose chains, which are recognized by repair factors such as APLF, enhancing DNA repair efficiency. Beyond proteins, PARP2 can ADP-ribosylate DNA, preferentially targeting 5’-terminal phosphates at DNA strand breaks in nicked duplexes. This dual functionality underpins its critical role in maintaining genomic stability by facilitating chromatin remodeling and the precise repair of DNA strand breaks.