HPF1 active protein
HPF1 protein, human
Synonyms
HPF1; HPF1 protein; human; Histone PARylation factor 1; C4orf27; HPF1 active protein
Form/Format
50ug HPF1 protein, human, lyophilized or 0.5mg (1mg/mL).
Western Blot (WB)
(ADP-ribosylation of PARP1 and HPF1. PARP1 is autoPARylated with the addition of 100uM NAD in the presence of activated DNA, lane B. When HPF1 is added, the autoPARylation profile shows lower MW staining, lane C. Also, HPF1 is ADP-ribosylated, lane C. The no NAD control shows no ADP-ribosylation, lane A. PARP1, HPF1, and autoPARylated PARP1 are indicated.)
SDS-Page
Related Product Information for HPF1 active protein
HPF1 protein, human, Cat. #2097, is highly purified and active recombinant full-length human HPF1, expressed in E. coli. The purified protein does not contain any expression tags. Please see the datasheet for additional information.
Mono- and poly-ADP-ribosylation are catalyzed by poly (ADP-ribose) polymerase (PARP) family proteins. PARP1/2 plays a critical role in the SSBR, and DSBR, the regulation of the stability of DNA replication forks, and maintenance of chromatin structures. Upon DNA damage, PARP1 rapidly recognizes and binds to a nicked or a gapped single-stranded DNA break which activates autoPARylation. Various PARP1-interacting regulatory factors play a role in the regulation of PARP1 activity. In response to DNA damage, histone PARylation factor 1 (HPF1 ; C4orf27) directly binds to the catalytic domain of PARP1/2 and promotes ADP-ribosylation at serine residues of PARP1, histone proteins, and other chromatin-associated factors. The serine-ADPr is a major and reversible post-translational modification in cells in response to DNA damage.
Mono- and poly-ADP-ribosylation are catalyzed by poly (ADP-ribose) polymerase (PARP) family proteins. PARP1/2 plays a critical role in the SSBR, and DSBR, the regulation of the stability of DNA replication forks, and maintenance of chromatin structures. Upon DNA damage, PARP1 rapidly recognizes and binds to a nicked or a gapped single-stranded DNA break which activates autoPARylation. Various PARP1-interacting regulatory factors play a role in the regulation of PARP1 activity. In response to DNA damage, histone PARylation factor 1 (HPF1 ; C4orf27) directly binds to the catalytic domain of PARP1/2 and promotes ADP-ribosylation at serine residues of PARP1, histone proteins, and other chromatin-associated factors. The serine-ADPr is a major and reversible post-translational modification in cells in response to DNA damage.
References
Gibbs-Seymour I, et al. (2016) Mol Cell. 62 432 doi.org/10.1016/j.molcel.2016.03.008
