MABS61
Anti-PARG Antibody, clone D8B10
clone D8B10, from mouse
Synonym(s):
poly (ADP-ribose) glycohydrolase, poly(ADP-ribose) glycohydrolase 60 kDa isoform
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
D8B10, monoclonal
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... PARG(8505)
General description
Poly(ADP-ribose) glycohydrolase (PARG) is an enzyme possessing both endo- and exoglycosidase activity against poly (ADP-ribose) (PARP), rapidly degrading PARP to release large quantities of free ADP-ribose. PARG is involved in several cellular processes including; apoptosis, DNA repair, cell cycle progression, cell survival and cellular differentiation. During apoptosis, PARG is cleaved by caspase-3 suggesting that PARG activity is regulated during this process. Although encoded by one gene, PARG is present in different cellular localizations as different isoforms: Isoform 1 (111 kDa) is present in the nucleus, Isoform 2 (102 kDA) is in the cytoplasm and Isoform 3 (99 kDa) is mitochondrial. Studies have indicated a critical role for PARG isoform 1 in the quality of sperm chromatin, and subsequent embryonic survival.
Immunogen
Epitope: Unknown
Histidine-tagged recombinant protein corresponding to human PARG.
Application
Anti-PARG Antibody, clone D8B10 is an antibody against PARG for use in WB & IP.
Research Category
Signaling
Epigenetics & Nuclear Function
Signaling
Epigenetics & Nuclear Function
Research Sub Category
Hormones & Receptors
Chromatin Biology
Hormones & Receptors
Chromatin Biology
Quality
Evaluated by Western Blot in Jurkat cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected PARG on 10 µg of Jurkat cell lysate.
Western Blot Analysis: 0.5 µg/mL of this antibody detected PARG on 10 µg of Jurkat cell lysate.
Target description
~ 102 kDa observed. Other isoforms may be observed in some lysates at 111 and 99 kDa
Physical form
Format: Purified
Protein G
Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
Jurkat cell lysate
Jurkat cell lysate
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Jean-Christophe Amé et al.
Methods in molecular biology (Clifton, N.J.), 1608, 395-413 (2017-07-12)
The purification of Poly(ADP-ribose) glycohydrolase (PARG) from overexpressing bacteria Escherichia coli is described here to a fast and reproducible one chromatographic step protocol. After cell lysis, GST-PARG-fusion proteins from the crude extract are affinity purified by a Glutathione 4B Sepharose
Yajie Zhang et al.
Nature methods, 10(10), 981-984 (2013-08-21)
Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid- and glutamic acid-ADP-ribosylated proteome. We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wide array of nuclear
Sarah L Grady et al.
Journal of virology, 86(15), 8259-8268 (2012-05-25)
Herpes simplex virus 1 infection triggers multiple changes in the metabolism of host cells, including a dramatic decrease in the levels of NAD(+). In addition to its role as a cofactor in reduction-oxidation reactions, NAD(+) is required for certain posttranslational
Priyanka Verma et al.
Nature cell biology, 23(2), 160-171 (2021-01-20)
The response to poly(ADP-ribose) polymerase inhibitors (PARPi) is dictated by homologous recombination (HR) DNA repair and the abundance of lesions that trap PARP enzymes. It remains unclear, however, if the established role of PARP in promoting chromatin accessibility impacts viability
Evgeniia Prokhorova et al.
Molecular cell, 81(12), 2640-2655 (2021-05-22)
ARH3/ADPRHL2 and PARG are the primary enzymes reversing ADP-ribosylation in vertebrates, yet their functions in vivo remain unclear. ARH3 is the only hydrolase able to remove serine-linked mono(ADP-ribose) (MAR) but is much less efficient than PARG against poly(ADP-ribose) (PAR) chains in vitro.
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