ZRANB3 antibody
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Description
DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | zinc finger, RAN-binding domain containing 3 (ZRANB3) |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | WB: 1:200-1:2000; IF: 1:20-1:200 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 150 kDa and 50 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | Q5FWF4 |
| Gene ID | 84083 |
| Alias | DNA annealing helicase and endonuclease ZRANB3,Annealing helicase 2 (AH2),Zinc finger Ran-binding domain-containing protein 3,ZRANB3 |
| Background | Antibody anti-ZRANB3 |
| Status | RUO |
| Note | Mol. Weight 150 kDa and 50 kDa |
Descripción
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DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks.
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