PARG Antibody (YA9960)
(Synonyms: PARG99)PARG Antibody (YA9960) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to PARG.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:1000-2000 |
Product Details
PARG Antibody (YA9960) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to PARG.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Calculated Molecular Weight Predicted band size: 110.9 kDa
Human recombinant protein fragment corresponding to amino acids 1-367 of human PARG produced in E.coli.
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
PARG is a Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). Mainly acts as an exo-glycohydrolase but can act as an endo-glycohydrolase at low efficiency, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming[1][2][3][4][5][6][7][8][9][10][11].
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Subcellular Localization
Nucleus
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Expression
Tissue_Specificity: Ubiquitously expressed. -
Isoforms & Post-Translational Modification
PARG has 5 isoforms, Q86W56-1: amino acid length is 976, molecular weight is 111110 Da (predicted); Q86W56-2: amino acid length is 894, molecular weight is 102312 Da (predicted); Q86W56-3: amino acid length is 868, molecular weight is 99432 Da (predicted); Q86W56-4: amino acid length is 527, molecular weight is 60873 Da (predicted); Q86W56-5: amino acid length is 475, molecular weight is 54794 Da (predicted).
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Subunit
Interacts with PCNA.
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SwissProt ID
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Synonyms
PARG99
Documentation
[1]. Putt KS, et al. A nonradiometric, high-throughput assay for poly(ADP-ribose) glycohydrolase (PARG): application to inhibitor identification and evaluation. Anal Biochem. 2004 Oct 15;333(2):256-64. [Content Brief]
[2]. Slade D, et al. The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. Nature. 2011 Sep 4;477(7366):616-20. [Content Brief]
[3]. Le May N, et al. Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression. Mol Cell. 2012 Dec 14;48(5):785-98. [Content Brief]
[4]. Rosenthal F, et al. Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases. Nat Struct Mol Biol. 2013 Apr;20(4):502-7. [Content Brief]
[5]. Bonfiglio JJ, et al. An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell. 2020 Nov 12;183(4):1086-1102.e23. [Content Brief]
[6]. Prokhorova E, et al. Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease. Mol Cell. 2021 Jun 17;81(12):2640-2655.e8. [Content Brief]
[7]. Rack JGM, et al. Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal. Nat Commun. 2021 Jul 28;12(1):4581. [Content Brief]
[8]. Sharifi R, et al. Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease. EMBO J. 2013 May 2;32(9):1225-37. [Content Brief]
[9]. Fontana P, et al. Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling. Nat Commun. 2023 Jun 2;14(1):3200. [Content Brief]
[10]. Illuzzi G, et al. PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress. Nucleic Acids Res. 2014 Jul;42(12):7776-92. [Content Brief]
[11]. Wright RH, et al. ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling. Science. 2016 Jun 3;352(6290):1221-5. [Content Brief]
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