Recombinant Human PARP1

Cat.No. : PARP1-30787TH
Product Overview : Recombinant full length Human PARP with N terminal proprietary tag, expressed in a Baculovirus infected Sf9 cell expression system, 140 kDa.
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Species : Human
Tag : Non
Description : This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes.
Biological activity : Specific Activity: 9067.5 U/mg.
Form : Liquid
Storage buffer : Preservative: NoneConstituents: 50% Glycerol, 0.05% Tween 20, 3mM DTT, 25mM Tris HCl, 100mM Sodium chloride, pH 8.0
Storage : Aliquot and store at -80°C. Avoid repeated freeze / thaw cycles.
Sequence Similarities : Contains 1 BRCT domain.Contains 1 PARP alpha-helical domain.Contains 1 PARP catalytic domain.Contains 2 PARP-type zinc fingers.
Full Length : Full L.
Gene Name PARP1 poly (ADP-ribose) polymerase 1 [ Homo sapiens ]
Official Symbol PARP1
Synonyms PARP1; poly (ADP-ribose) polymerase 1; ADP ribosyltransferase (NAD+; poly (ADP ribose) polymerase) , ADPRT, poly (ADP ribose) polymerase family, member 1 , PPOL; poly [ADP-ribose] polymerase 1; PARP;
Gene ID 142
mRNA Refseq NM_001618
Protein Refseq NP_001609
MIM 173870
Uniprot ID P09874
Chromosome Location 1q41-q42
Pathway BER complex, organism-specific biosystem; BER complex, conserved biosystem; Base excision repair, organism-specific biosystem; Base excision repair, conserved biosystem; Caspase cascade in apoptosis, organism-specific biosystem;
Function DNA binding; NAD binding; NAD+ ADP-ribosyltransferase activity; metal ion binding; protein N-terminus binding;

Not For Human Consumption!

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