纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ESPL1 |
Uniprot No | Q14674 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 586-701aa |
氨基酸序列 | REELQAYKAVRADTGQERFNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLLDSVRPEAQARDQLLDDKAQALLWLYICTLEAKIQEGIERDR |
分子量 | 38.5 kDa |
蛋白标签 | GST-tag at N-terminal |
缓冲液 | 0 |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
1. **"Cleavage of cohesin by the CD clan protease separin regulates anaphase onset in yeast"**
*作者:Uhlmann, F., et al. (2000)*
摘要:该研究首次阐明酵母Separase(ESPL1同源物)通过切割 cohesin 复合体触发姐妹染色单体的分离,并描述了其重组酶的表达与活性分析方法。
2. **"Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation of Cdc20 to Cdh1"**
*作者:Zou, H., et al. (2002)*
摘要:研究利用重组人ESPL1蛋白,揭示了其在调控染色体分离及纺锤体检查点中的功能,通过体外实验验证其与securin的相互作用及酶切动力学。
3. **"Structure of the cohesin cleavage module and implications for the mechanism of sister chromatid separation"**
*作者:Lin, Z., et al. (2016)*
摘要:通过重组表达人ESPL1蛋白并解析其与cohesin复合体的共晶结构,阐明了ESPL1酶切位点的特异性识别机制及其在分裂中的构象变化。
4. **"Separase is recruited to mitotic chromosomes by phosphorylation-mediated interactions with the Bub family of proteins"**
*作者:Papi, M., et al. (2005)*
摘要:该研究利用重组人ESPL1蛋白进行免疫共沉淀及功能实验,证明其与Bub蛋白家族的磷酸化依赖性结合,调控染色体正确分离的分子机制。
---
以上文献覆盖ESPL1的结构、功能、调控机制及重组蛋白实验方法,适用于进一步研究其酶学特性或疾病(如癌症)中的异常激活机制。
Recombinant human ESPL1 protein, also known as separase, is a cysteine protease critical for chromosomal segregation during cell division. ESPL1 cleaves the cohesin complex that holds sister chromatids together, enabling their separation in the anaphase stage of mitosis and meiosis. Its activity is tightly regulated by binding to securin, an inhibitory chaperone, and phosphorylation events linked to the cell cycle. Dysregulation of ESPL1 has been implicated in genomic instability, a hallmark of cancers and developmental disorders.
The recombinant form is typically produced in expression systems like *E. coli* or mammalian cells, enabling studies of its structure-function relationships, enzymatic kinetics, and interactions with regulatory partners. Purified recombinant ESPL1 is utilized to investigate mechanisms of chromosome segregation errors, screen for potential inhibitors, and explore therapeutic strategies targeting cell cycle abnormalities. Research on recombinant ESPL1 has advanced understanding of aneuploidy-driven diseases and may inform drug development for cancer or conditions linked to defective cell division.
×