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Key Documents

SRP8023

Sigma-Aldrich

PARG human

recombinant, expressed in Sf21 cells, His tagged, >95% (SDS-PAGE)

Synonym(s):

FNDC5 (cleaved), Poly(ADP-ribose) glycohydrolase

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About This Item

CAS Number:
9068-16-0
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in Sf21 cells

tag

His tagged

assay

>95% (SDS-PAGE)

form

liquid

mol wt

~110 kDa by SDS-PAGE

packaging

pkg of 2 μg

concentration

≥0.2 mg/mL

color

clear

UniProt accession no.

Q86W56

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PARG(8505)

General description

Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG hydrolyzes poly(ADP-ribose) at glycosidic (1′′-2′) linkage of ribose-ribose bond to produce free ADP-ribose.

Physical form

Solution in 50 mM TRIS-HCl, pH 7.5, containing 100 mM sodium chloride, 0.2% NP-40, 50 mM imidazole and 10% glycerol.

Other Notes

Human PARG is fused to a His-tag.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H360D

Hazard Classifications

Repr. 1B

Storage Class

6.1D - Non-combustible, acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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Sara C Larsen et al.
Cell reports, 24(9), 2493-2505 (2018-08-30)
ADP-ribosylation (ADPr) is a reversible posttranslational modification involved in a range of cellular processes. Here, we report system-wide identification of serine ADPr in human cells upon oxidative stress. High-resolution mass spectrometry and unrestricted data processing confirm that serine residues are
Jeannette Abplanalp et al.
Nature communications, 8(1), 2055-2055 (2017-12-14)
ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well investigated.
Sara C Buch-Larsen et al.
Cell reports, 32(12), 108176-108176 (2020-09-24)
ADP-ribosylation (ADPr) is a post-translational modification that plays pivotal roles in a wide range of cellular processes. Mass spectrometry (MS)-based analysis of ADPr under physiological conditions, without relying on genetic or chemical perturbation, has been hindered by technical limitations. Here
Xiao-Nan Zhang et al.
Nature communications, 10(1), 4196-4196 (2019-09-15)
Nicotinamide adenine dinucleotide (NAD+)-dependent ADP-ribosylation plays important roles in physiology and pathophysiology. It has been challenging to study this key type of enzymatic post-translational modification in particular for protein poly-ADP-ribosylation (PARylation). Here we explore chemical and chemoenzymatic synthesis of NAD+
Michelle Schacke et al.
International journal of molecular sciences, 20(3) (2019-01-30)
Poly- adenosine diphosphate (ADP)-ribose (PAR) is a polymer synthesized as a posttranslational modification by some poly (ADP-ribose) polymerases (PARPs), namely PARP-1, PARP-2, tankyrase-1, and tankyrase-2 (TNKS-1/2). PARP-1 is nuclear and has also been detected in extracellular vesicles. PARP-2 and TNKS-1/2

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