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Parp12 Antibody (N-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q8BZ20
Other Accession NP_766481
Clone Names 71113051
Additional Information
Gene ID 243771
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 The synthetic peptide sequence used to generate the antibody AP6298a was selected from the N-term region of human Parp12. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name Parp12 {ECO:0000312|MGI:MGI:2143990}
Synonyms Zc3hdc1
Function Mono-ADP-ribosyltransferase that mediates mono-ADP- ribosylation of target proteins.
Cellular Location Nucleus.
Research Areas
Citations (0)
citation

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Background

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.

References

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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$ 277.78
Cat# BP6298a
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