Poly ADP-ribose Polymerase 1 (PARP1) Antibody
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Description
Poly ADP-ribose Polymerase 1 (PARP1) Antibody is a Mouse Monoclonal antibody against POLY(ADP-RIBOSE) POLYMERASE-1.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Poly ADP-ribose Polymerase 1 (PARP1) |
| Host | Mouse |
| Reactivity | Human |
| Recommended Dilution | Validated in IHC-F and IHC-P. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Monoclonal |
| Conjugation | Unconjugated |
| Isotype | IgG1 |
| Purification | Purified |
| Size 1 | 100 µg |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC, IF/ICC, IP |
| Buffer | PBS. Contains sodium azide. |
| Availability | Shipped within 3-7 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P09874 |
| Background | Antibody anti-PARP1 |
| Status | RUO |
| Note | Concentration: 1.0 mg/ml - |
Descripción
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anti- 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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anti- PARP1 antibody
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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