ESPL1 Antibody, HRP conjugated

1. Separase activity measurement may therefore be useful as a novel additional molecular marker for disease monitoring PMID:29370237
2. Studies identified and characterized the role of separase in mitosis, meiosis, non-canonical roles, its regulation, as a regulator of centriole disengagement, non proteolytic roles, diverse substrates, structural insights, and association of separase with cancer. [review] PMID:27966791
3. High ESP expression is associated with breast cancer. PMID:28859055
4. Proximity mapping of human separase has been presented. PMID:27495871
5. The assay was used to quantify Separase proteolytic activity in leukemic cell lines and peripheral blood samples from leukemia patients. PMID:26267133
6. Recruitment and activation of separase at centrosomes are two distinct steps that do not require microtubules. PMID:25299182
7. Separase protein levels decrease and Separase proteolytic activity increases exclusively in b3a2 p210BCR-ABL-positive cell lines under Imatinib treatment. PMID:26087013
8. Separase is an oncogene whose overexpression induces tumorigenesis, and indicate that Separase overexpression and aberrant nuclear localization are common in many tumor types and may predict outcome in some human malignancies. PMID:24792645
9. High ESPL1 mRNA expression was associated with luminal B breast cancers. PMID:25086634
10. Data indicate that separase is subject to native-state cis/trans isomerization by peptidyl-prolyl-isomerase Pin1. PMID:25921067
11. By consecutively acting as a protease and a cdk1 inhibitor, separase coordinates two key processes to achieve simultaneous and abrupt separation of sister chromatids. PMID:22814604
12. Kendrin is a novel and crucial substrate for separase (ESPL1) at the centrosome, protecting the engaged centrioles from premature disengagement and thereby blocking reduplication until the cell passes through mitosis. PMID:22542101
13. Plk1-mediated phosphorylation of Cdc6 promotes the interaction of Cdc6 and Cdk1, leading to the attenuation of Cdk1 activity, release of separase, and subsequent anaphase progression. PMID:21041660
14. Anaphase specific auto-cleavage of separase. PMID:12297314
15. Processing, localization, and requirement of separase for normal anaphase progression. PMID:12672959
16. Separase function is not restricted to anaphase initiation; its role in promoting loss of sister chromatid cohesion might be preferentially at arms but not centromeres. PMID:16177575
17. Protein phosphatase 2A and separase form a complex regulated by separase autocleavage PMID:17604273
18. Phosphorylation promotes complex formation indirectly, possibly by inducing a conformational change in full-length separase. PMID:17974570
19. The complete removal of cohesin from chromosome arms depends on separase. PMID:18003702
20. Separase has targets involved in regulation of G(2) to M progression after DNA damage in lung cancer cells. PMID:18616699
21. These results collectively suggest that Separase is an oncogene, whose overexpression alone in mammary epithelial cells is sufficient to induce aneuploidy and tumorigenesis in a p53 mutant background. PMID:18728194
22. Study reports that cohesin cleavage by human separase requires DNA in a sequence-nonspecific manner. PMID:19345191
23. Separase might be an oncogene, whose overexpression induces tumorigenesis. Separase overexpression and aberrant nuclear localization are common in many tumor types and may predict outcome in some human cancers. PMID:19351757
24. Plk1 and separase act at different times during M phase to license centrosome duplication, reminiscent of their roles in removing cohesin from chromosomes PMID:19758559

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HGNC: 16856

UNIGENE: Hs.153479

KEGG: hsa:9700

STRING: 9606.ENSP00000257934

OMIM: 604143