|Application ||FC, WB, IHC-P, E|
|Calculated MW||79917 Da|
|Antigen Region||312-344 aa|
|Other Names||Poly [ADP-ribose] polymerase 12, PARP-12, ADP-ribosyltransferase diphtheria toxin-like 12, ARTD12, Zinc finger CCCH domain-containing protein 1, Parp12, Zc3hdc1|
|Target/Specificity||This Parp12 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 312-344 amino acids from the N-terminal region of mouse Parp12.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Parp12 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Poly(ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. Poly(ADP-ribose) polymerases (PARPs) now constitute a large family of 18 proteins, encoded by different genes and displaying a conserved catalytic domain in which PARP-1 (113 kDa), the founding member, and PARP-2 (62 kDa) are so far the sole enzymes whose catalytic activity has been shown to be immediately stimulated by DNA strand breaks. A large repertoire of sequences encoding novel PARPs now extends considerably the field of poly(ADP-ribosyl)ation reactions to various aspects of the cell biology including cell proliferation and cell death. Some of these new members interact with each other, share common partners and common subcellular localizations suggesting possible fine tuning in the regulation of this post-translational modification of proteins.
Bailey,P.J., Exp. Cell Res. 312 (16), 3108-3119 (2006)
Katoh,M., Int. J. Oncol. 23 (2), 541-547 (2003)
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