Description
Recombinant Human PARP-1 Protein (His Tag)(Active) | PKSH031294 | Gentaur US, UK & Europe Disrtribition
Synonyms: ADPRT;ADPRT1;ARTD1;pADPRT-1;PARP;PARP-1;PPOL
Active Protein: Active protein
Activity: The amino acids corresponding to the full length of human PARP1 (NP_001609.2) (Met 1-Trp 1014) was fused with a polyhistidine tag at the C-terminus.
Protein Construction: The amino acids corresponding to the full length of human PARP1 (NP_001609.2) (Met 1-Trp 1014) was fused with a polyhistidine tag at the C-terminus.
Fusion Tag: C-His
Species: Human
Expressed Host: Baculovirus-Insect Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 90 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 114.5 kDa
Formulation: Lyophilized from sterile PBS, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: Poly (ADP-ribose) polymerase 1(PRAP1), also known as NAD(+) ADP-ribosyltransferase 1(ADPRT), is a chromatin-associated enzyme which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. The poly(ADP-ribosyl)ation modification is critical for a wide range of processes, including DNA repair, regulation of chromosome structure, transcriptional regulation, mitosis and apoptosis. PARP1 is demonstrateed to mediate the poly(ADP-ribose) ation of APLF (aprataxin PNK-like factor) and CHFR (checkpoint protein with FHA and RING domains), two representative proteins involved in the DNA damage response and checkpoint regulation. Further, It has been suggested that DNA-dependent protein kinase (DNA-PK), another component of DNA repair, suppresses PARP activity, probably through direct binding and/or sequestration of DNA-ends which serve as an important stimulator for both enzymes. PARP1 inhibitors is thus proposed as a targeted cancer therapy for recombination deficient cancers, such as BRCA2 tumors.
Research Area: Cell biology, Cancer, epigenetics and nuclear signal, metabolism
