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Pds1 is an anaphase inhibitor and plays important role in DNA damage and spindle check point pathways. Pds1 inhibits sister chromatid separation by binding and inhibiting Esp1, cystein protease that causes cleavage of the cohesin Scc1 that binds the sister chromatids together. Pds1 is responsible for targeting of Esp1 to nucleus and its binding to the spindle. Degradation of Pds1 occurs shortly before anaphase, which liberates Esp1 and is a prerequisite for anaphase entry. Pds1 is targeted for degradation by ubiquitination mediated by cyclosome/anaphase-promoting complex (APC) functioning as a ubiquitin ligase. In response to DNA damage Chk1 phosphorylates Pds1 to stabilize it against the APC mediated destruction, hence preventing the entry of such a cell into anaphase. Host Species: MouseClone: DCS-280Isotype: IgG2a/κSpecies Reactivity: Human. Others not known.Epitope: Not determinedImmunogen: Human recombinant full-length Pds1 proteinMolecular Weight: 42kDaPositive Control: HeLa cells, TonsilCellular Localization: Nuclear Recommended for:Immunohistochemistry (Formalin/paraffin)Western Blotting (Not verified) Note:USA: RUO; Int'l: RUO
