Recombinant Human Separase protein

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Separase also known as ESPL1 is a cysteine protease weighing around 230 kDa. It plays an important mechanical role in the cell cycle specifically during the anaphase of mitosis. Separase executes its function by cleaving the cohesin complex which is important for sister chromatid separation. This protein is expressed in a variety of tissues predominantly during cell division. Separase's activity is tightly regulated by securin and cyclin-dependent kinases to prevent premature chromatid separation.

Biological function summary

Separase contributes to the essential process of chromosome segregation by acting as a part of the chromosomal passenger complex. This complex also includes aurora B kinase and survivin which coordinate chromosomal and cytoskeletal dynamics during mitosis. Separase’s activation enables proper anaphase progression and genomic stability as it ensures timely dissolution of cohesin bonds holding sister chromatids together. Its regulation prevents errors in chromosomal distribution that could lead to aneuploidy.

Pathways

Separase integrates into the mitotic spindle checkpoint and DNA damage response pathways critical for maintaining genomic integrity. Aurora B kinase a related protein phosphorylates components of these pathways to coordinate division processes accurately. Separase by ensuring correct chromosomal segregation plays a pivotal role in preventing propagation of cells with damaged DNA or chromosomal abnormalities.

Separase dysfunction links to cancer and congenital cohesinopathies. Abnormal Separase activity can lead to improper chromatid separation contributing to genomic instability a hallmark of cancer. For instance dysregulation of securin a regulatory protein of Separase could lead to tumorigenesis. Additionally defects in separase activity associate with cohesinopathies a group of disorders characterized by developmental anomalies.