1. Signaling Pathways
  2. Cell Cycle/DNA Damage
  3. Poly(ADP-ribose) Glycohydrolase (PARG)

Poly(ADP-ribose) Glycohydrolase (PARG)

Poly (ADP-ribose) glycohydrolase (PARG) is the primary hydrolase involved in the degradation of poly(ADP-ribose) (PAR). PARG possesses both endo-glycohydrolase and exo-glycohydrolase activity, preferentially performing the latter by binding to the two most distal ADP-ribose residues within the PAR chain. These different modes of catalysis produce free PAR and mono ADP-ribose moieties, respectively. The free mono ADP-ribose is then metabolized into AMP and ribose 5′ phosphate by ADP-ribose pyrophosphohydrolases such as the NUDIX family. AMP is utilized in ATP reformation and different metabolic and cell signaling pathways while ribose 5′ phosphate is a precursor to many biomolecules including DNA, RNA and ATP. Endo-glycohydrolase activity is considered to occur primarily during hyper-PARP activation, the resulting free PAR chains produced are then implicated in apoptosis acting as a death signal.

Poly(ADP-ribose) Glycohydrolase (PARG) Related Products (2):

Cat. No. Product Name Effect Purity
  • HY-146248A
    TFMU-ADPr ammonium
    TFMU-ADPr ammonium is a general substrate for monitoring poly(ADP-ribose) glycohydrolase (PARG) activity. TFMU-ADPr ammonium can directly report on total PAR hydrolase activity via release of a fluorophore. TFMU-ADPr ammonium has excellent reactivity, generality, stability, and usability. TFMU-ADPr ammonium is a versatile tool for assessing small-molecule inhibitors in vitro and probing the regulation of ADP-ribosyl catabolic enzymes.
  • HY-146248
    TFMU-ADPr
    TFMU-ADPr is a general substrate for monitoring poly(ADP-ribose) glycohydrolase (PARG) activity. TFMU-ADPr can directly report on total PAR hydrolase activity via release of a fluorophore. TFMU-ADPr has excellent reactivity, generality, stability, and usability. TFMU-ADPr is a versatile tool for assessing small-molecule inhibitors in vitro and probing the regulation of ADP-ribosyl catabolic enzymes.