Product nameRecombinant Human PARP1 (mutated E988 K) protein
See all PARP1 proteins and peptides
Protein lengthFull length protein
SourceBaculovirus infected Sf21 cells
Amino Acid Sequence
Amino acids1 to 1014
Additional sequence informationHuman full-length inactive mutant E988K of PARP1 fused to a His-tag.
Our Abpromise guarantee covers the use of ab157027 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity> 95 % SDS-PAGE.
Specific activity: 0.5% of wild type PARP1.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Preservative: 0.34% Imidazole
Constituents: 0.2% Tergitol-NP40, 0.79% Tris HCl, 10% Glycerol, 0.58% Sodium chloride
- ADP ribosyltransferase
- ADP ribosyltransferase (NAD+; poly (ADP ribose) polymerase)
- ADP ribosyltransferase diphtheria toxin like 1
FunctionInvolved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150.
Sequence similaritiesContains 1 BRCT domain.
Contains 1 PARP alpha-helical domain.
Contains 1 PARP catalytic domain.
Contains 2 PARP-type zinc fingers.
modificationsPhosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR.
Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
S-nitrosylated, leading to inhibit transcription regulation activity.
- Information by UniProt
ab157027 has not yet been referenced specifically in any publications.