HPF1 (E8B3W) Rabbit mAb #90876
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
HPF1 (E8B3W) Rabbit mAb recognizes endogenous levels of total HPF1 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu241 of human HPF1 protein.
Background
Poly (ADP-ribose) polymerases (PARPs) are a family of enzymes that catalyze ADP-ribosylation (ADPr), a reversible posttranslational modification of proteins that regulates various cellular processes. PARP-1 and PARP-2 are two well-characterized family members that catalyze ADPr on a wide range of substrates in response to DNA damage (1). Histone PARylation factor 1 (HPF1), also referred to as C4orf27, is an accessory protein to PARP1/2 that directly binds to these enzymes and alters their ADPr amino acid specificity from aspartate/glutamate to serine. (2). HPF1 is specifically required to carry out ADPr modifications on serine residues for both histone and non-histone substrates, as serine ADPr does not occur in cells lacking HPF1 (3). This is critically important, as serine has been shown to be the most abundant ADPr residue in cells affected by DNA damage (4). Mechanistically, PARP1/2 have been described as incomplete enzymes, and crystal structure analysis shows that HPF1-PARP1/2 binding confers a joint active site, which may explain the switch from aspartate/glutamate specificity to serine (2). Additionally, HPF1 knockout cells are more sensitive to PARP inhibitors, suggesting that drug manufacturers will need to take HPF1 binding into account when developing effective inhibitors for these enzymes (1).
Limited Uses
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