Separase is a site-specific endopeptidase belonging to the CD clan cysteine protease group which cleaves kleisin subunit (Rad21/Scc1/Mcd1/Rec8) of cohesin complex. Separase is distantly related to the caspases which are well known for their role in programmed cell death (PCD). Within the cell, separase shows wide distribution. For example, this protease has been detected in the nucleus, cytoplasm, mitochondria and at spindle. Owing to irreversible action, a key regulator of cell cycle and recently, an association of separase with diverse types of cancer and other medical consequences, it is anticipated that the activity of this CD clan endopeptidase must be under tight regulation and cells may have evolved different ways of regulating separase activity. It is not surprising that the premature cleavage of the cohesin complex and untimely disengagement of centrioles by untimely or abrupt separase activity results in aneuploidy, a major cause of cancer. Thus one can believe that separase may act as an important oncogene[1]. Deregulated separase activity is associated with aneuploidy, a hallmark of most human cancers. In fact, separase is highly overexpressed in many solid cancers, making it an attractive chemotherapeutic target[2]. Separase emerges as an important oncogene that both increased and reduced activity of separase was found to be associated with several types of malignancies. Thus, to make sure that separase activity remains at an optimum level, both inhibitors and activators are needed as separase regulator[1].