MABC547
Anti-Poly ADP-ribose Antibody, clone 10H
clone 10H, from mouse
Sinónimos:
Anti-PAR antibody
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Productos recomendados
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
10H, monoclonal
species reactivity
human
technique(s)
immunofluorescence: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG3κ
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... PARP1(142)
General description
Poly(ADP-ribose) polymerase is an abundant nuclear enzyme that catalyses the synthesis of poly(ADP-ribose) from nicotinamide adenine dinucleotide (NAD+). Poly(ADP-ribose) has an N-terminal DNA-binding domain containing two zinc-fingers, which is linked to the C-terminal NAD+-binding domain by a short region containing several glutamic acid residues that are sites of auto-poly (ADP-ribosyl) ation. Production of poly(ADP-ribose) within the cell is initiated by agents that generate DNA strand interruptions. The branched homopolymer chains may reach a length of 200–300 residues but are rapidly degraded after synthesis. The function of poly(ADP-ribose) synthesis is not clear, although it seems to be required for DNA repair.
Immunogen
Corresponding to human Poly ADP-ribose chain.
Application
Detect PARP using this mouse monoclonal antibody, Anti-Poly ADP-ribose Antibody, clone 10H validated for use in western blotting, IP & Immunofluorescence.
Immunoprecipitation Analysis: A representative lot was used by an an independent laboratory to immunoprecipitate Poly ADP-ribose in cultured supernatents from mouse erythrocytes coated with Poly ADP-ribose (Kawamitsu, H., et al. (1984). American Chemical Society. 3771-3777).
Immunofluorescence Analysis: A representative lot was used by an an independent laboratory to detect Poly (ADP-ribose) synthesis on transfected CV-1 cells via indirect immunofluorescence (J.H. Kupper, et al. J. Biol. Chem. (1990) 265:18721).
Immunofluorescence Analysis: A representative lot was used by an an independent laboratory to detect Poly (ADP-ribose) synthesis on transfected CV-1 cells via indirect immunofluorescence (J.H. Kupper, et al. J. Biol. Chem. (1990) 265:18721).
Research Category
Apoptosis & Cancer
Apoptosis & Cancer
Research Sub Category
Apoptosis - Additional
Apoptosis - Additional
Quality
Evaluated by Western Blotting in untreated and UV treated HeLa cells.
Western Blotting Analysis: 1.0 µg/mL of this antibody detected UV treated HeLa cells. Little or no signal observed in untreated HeLa cells.
Western Blotting Analysis: 1.0 µg/mL of this antibody detected UV treated HeLa cells. Little or no signal observed in untreated HeLa cells.
Target description
Observed molecular weight is the result of poly(ADP-ribose) polymer on protein receptors (such as histones and transcription factors).
Linkage
Replaces: MAB3192
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG3κ 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.
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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Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Jing Xu et al.
Cancer chemotherapy and pharmacology, 89(5), 683-695 (2022-04-15)
Although the use of PARP inhibitor has received considerable amount of attention in ovarian cancer, PARP inhibitor resistance still emerges with disease progression. PI3K/AKT pathway inhibitors have been proposed to synergize with PARP inhibition to slow tumor growth, but the
Umeshkumar Vekariya et al.
Nature communications, 15(1), 5822-5822 (2024-07-11)
DNA polymerase theta (Polθ)-mediated end-joining (TMEJ) repairs DNA double-strand breaks and confers resistance to genotoxic agents. How Polθ is regulated at the molecular level to exert TMEJ remains poorly characterized. We find that Polθ interacts with and is PARylated by
Bingteng Xie et al.
Cell research, 28(4), 462-475 (2018-02-22)
Before fertilization, mammalian oocyte undergoes an asymmetric division which depends on eccentric positioning of the spindle at the oocyte cortex to form a polar body and an egg. Since the centriole is absent and, as a result, the polar array
Yousef M O Alhammad et al.
bioRxiv : the preprint server for biology (2020-06-09)
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other SARS-like-CoVs encode 3 tandem macrodomains within non-structural protein 3 (nsp3). The first macrodomain, Mac1, is conserved throughout CoVs, and binds to and hydrolyzes mono-ADP-ribose (MAR) from target proteins. Mac1 likely counters
Christina Andronikou et al.
The EMBO journal, 43(6), 1015-1042 (2024-02-16)
Targeting poly(ADP-ribose) glycohydrolase (PARG) is currently explored as a therapeutic approach to treat various cancer types, but we have a poor understanding of the specific genetic vulnerabilities that would make cancer cells susceptible to such a tailored therapy. Moreover, the
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