Human Poly ADP-Ribose Polymerase 1 (PARP1) Protein (Active)
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Description
Human PARP-1 Protein is a recombinant protein from Human produced in Baculovirus-Insect Cells. 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.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | PARP-1 |
| Host | Insect |
| Assay Type | Activity: Active Sequence Fragment: Met1-Trp1014 |
| Origin | Human |
| Observed MW | 114.5 kDa |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 50 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Buffer | Lyophilized from sterile PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Aliquot and store at -20 °C. Avoid repeated freeze/thaw cycles. Shelf Life: 6 months. |
| Dry Ice | No |
| NCBI Accession | NP_001609.2 |
| Background | Protein PARP1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. Endotoxin Level: < 1.0 EU per µg of the protein as determined by the LAL method. |
Descripción
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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.
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PARP1 (poly(ADP-ribose) polymerase 1) is a nuclear enzyme catalyzing the poly(ADP-ribosyl)ation of many key proteins in vivo. The normal function of PARP1 is the routine repair of DNA damage. Activated by DNA strand breaks, the PARP1 is cleaved into an 85 to 89-kDa COOH-terminal fragment and a 24-kDa NH2-terminal peptide by caspases during the apoptotic process. The appearance of PARP fragments is commonly considered as an important biomarker of apoptosis. In addition to caspases, other proteases like calpains, cathepsins, granzymes and matrix metalloproteinases (MMPs) have also been reported to cleave PARP1 and gave rise to fragments ranging from 42-89kD. This antibody was generated against the N-terminal region of human PARP1 and it recognizes the full-length as well as the cleavage of the PARP1.
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