Render Target: STATIC
Render Timestamp: 2024-10-09T09:41:21.330Z
Commit: f04ddd7fea9fb3592f59f61482fcb94610d25cbe
1% for the planet logo
PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

ARH3 (E8A6G) Rabbit mAb #32205

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 39
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    ARH3 (E8A6G) Rabbit mAb recognizes endogenous levels of total ARH3 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro241 of human ARH3 protein.

    Background

    ADP-ribosylation is a reversible post-translational modification (PTM) where a single unit or polymers of ADP-ribose (ADPr) groups from β-nicotinamide adenine dinucleotide (NAD+) are transferred onto specific residues of target proteins (1). In addition to proteins, DNA and RNA molecules have also been identified as targets of ADP-ribosylation (2,3). This modification is catalyzed by a diverse group of ADP-ribosyltransferases (ARTs), with the majority of them functioning to add a single ADPr unit (MARylation) while the deposition of multiple ADPrs are done by poly (ADP-ribose) polymerases (PARPs). Reversal of ADP-ribosylation is accomplished by the evolutionarily distinct macrodomain and ADP-ribosylhydrolase (ARH) protein families (4). Specifically, poly (ADP-ribose) glycohydrolase (PARG) or ADP-ribosylhydrolase 3 (ARH3) degrade PARylation down to single ADPr units and MacroD1, MacroD2, TARG1, or ARH1 fully remove them from target residues (5). ADP-ribosylation and the enzymes that regulate it are involved in a wide range of cellular processes, such as DNA repair, chromatin regulation, transcription, and cellular stress response (1,4). Moreover, ADP-ribosylation has been shown to be a therapeutically critical PTM in various cancers, neurodegenerative diseases, and inflammation (6).

    The ARH family of ADP-ribose hydrolases contains three proteins with similarities in amino acid sequence but differences in their enzymatic activities. ARH3, also known as ADPRHL2, is a ubiquitous protein that localizes to the nucleus, cytosol, and mitochondria in a cell-type specific manner (7-9). ARH3 exhibits partial redundancy with PARG in their preference for hydrolysis of DNA damage-induced serine ADP-ribosylation which underlies a key role for these enzymes in maintaining genomic stability. Arh3-KO mice have been shown to develop increased brain infarction in response to ischemia-reperfusion injury (10) and human ARH3-deficiency is a rare recessive autosomal disorder characterized by neurodegeneration and early death (11,12).
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