PARG (Poly ADP-ribose glycohydrolase) is a catabolic enzyme with molecular mass ranging from 60-74kDa. It has four isoforms namely G1, G2, G3 and G4 with high protease sensitivity.
Immunogen
PARG (NP_003622, 329-364) This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human Parg.
Application
Anti-PARG (N-term) antibody produced in rabbit is suitable for indirect ELISA (1:1000) and immunohistochemistry (1:50-1:100) applications.
Biochem/physiol Actions
PARG (Poly ADP-ribose glycohydrolase) is involved in several gene regulation processes such as maintenance of chromatin structure, transcription, DNA repair and apoptosis. It regulates retinoic acid receptor (RAR)-mediated transcription during chromatin remodeling. It catabolically separate ADP-ribose polymers synthesized by poly-(ADP-ribose) polymerases. A study shows that PARG plays a therapeutic role in various physiological conditions such as inflammation, ischemia, stroke, and cancer chemotherapy.
Physical form
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
Frontiers in bioscience (Landmark edition), 14, 1619-1626 (2009-03-11)
Poly (ADP-robose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers synthesized by members of the poly (ADP-ribose) polymerase (PARP) family of enzymes. The growing evidence supports the importance of a tight control of poly (ADP-ribose) metabolism by the
Poly-(ADP-ribose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers synthesized by poly-(ADP-ribose) polymerases. Here, transcriptome profiling and differentiation assay revealed a requirement of PARG for retinoic acid receptor (RAR)-mediated transcription. Mechanistically, PARG accumulates early at promoters of RAR-responsive
Cellular and molecular life sciences : CMLS, 62(7-8), 739-750 (2005-05-04)
Poly(ADP-ribose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers formed by members of the PARP family of enzymes. Despite its discovery and subsequent partial purification in the 1970s and the cloning of its single gene in the late
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