Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
基因功能參考文獻(xiàn):
Study results establish ARH3 as a serine mono-ADP-ribosylhydrolase and as an important regulator of the basal and stress-induced ADP-ribosylome. PMID: 29234005
By screening for the hydrolase that is responsible for the reversal of Ser-ADP ribosilation, the authors identified ARH3/ADPRHL2 as capable of efficiently and specifically removing Ser-ADP ribosilation of histones and other proteins. PMID: 28650317
ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). PMID: 22433848
ARH3 has poly(ADP-ribose) glycohydrolase activity but is structurally unrelated to poly(ADP-ribose) glycohydrolase PMID: 16278211
cloning, recombinant production, purification and crystallization of ARH3 consisting of 347 amino-acid residues PMID: 16511307
The molecular architecture of human ARH3 constitutes the archetype of an all-alpha-helical protein fold and suggests reversibility mechanisms of protein ADP-ribosylation. PMID: 17015823
poly(ADP-ribose) glycohydrolase ARH3 hydrolyzed O-acetyl-ADP-ribose to produce ADP-ribose in a time- and Mg(2+)-dependent reaction and thus could participate in two signaling pathways PMID: 17075046