Human PARP1 (Poly [ADP-ribose] polymerase 1) ELISA Kit
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Product specifications
| Category | ELISA Kits |
| Reactivity | Human |
| Detection Method | Colorimetric |
| Assay Data | 4 hours |
| Assay Type | Sandwich ELISA, Double Antibody |
| Test Range | 0.625-40ng/ml |
| Sensitivity | 0.375ng/ml |
| Size 1 | 96T |
| Tested Applications | ELISA |
| Sample Type | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Availability | Shipped within 10-14 working days. |
| Storage | 2-8 °C for 12 months |
| UniProt ID | P09874 |
| Alias | Poly [ADP-ribose] polymerase 1, PARP-1, ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1, DNA ADP-ribosyltransferase PARP1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1, Protein poly-ADP-ribosyltransferase PARP1, Poly [ADP-ribose] polymerase 1, processed C-terminus, Poly [ADP-ribose] polymerase 1, 89-kDa form, Poly [ADP-ribose] polymerase 1, processed N-terminus, NT-PARP-1, Poly [ADP-ribose] polymerase 1, 24-kDa form, Poly [ADP-ribose] polymerase 1, 28-kDa form, PARP1, ADPRT, PPOL |
| Background | Elisa kits for PARP1 |
| Status | RUO |
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Human PARP1 (Poly [ADP-ribose] polymerase 1) ELISA Kit
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PARP1 antibody
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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