Recombinant Human Securin protein (His tag N-Terminus)
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(2 Publications)
Recombinant Human Securin protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >80%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
EAP1, PTTG, TUTR1, PTTG1, Securin, Esp1-associated protein, Pituitary tumor-transforming gene 1 protein, Tumor-transforming protein 1, hPTTG
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Securin protein (His tag N-Terminus) (AB87664)
ab87664 on 15% SDS-PAGE (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Securing proper chromosome segregation Securin forms a complex with Separase. By inhibiting Separase Securin ensures that separation of chromatids occurs only at the correct stage of mitosis. This regulatory function is critical for maintaining genomic stability and avoiding aneuploidy which can lead to tumorigenesis. The presence of Securin in dividing cells highlights its role in the cell cycle.
Pathways
Securin functions are integrated within the cell cycle and apoptosis pathways. In the cell cycle pathway Securin controls the metaphase-anaphase transition. This involves interaction with cyclin-dependent kinases (CDKs) and the anaphase-promoting complex (APC/C). In terms of apoptosis Securin may interact with proteins like Bcl-2 impacting cell survival and death decisions under stress conditions.
Specifications
Form
Liquid
Additional notes
Purified by using conventional chromatography techniques.
General info
Function
Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation.
Sequence similarities
Belongs to the securin family.
Post-translational modifications
Phosphorylated at Ser-165 by CDK1 during mitosis.. Phosphorylated in vitro by ds-DNA kinase.. Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation. 'Lys-11'-linked ubiquitination is mediated by the E2 ligase UBE2C/UBCH10.
Subcellular localisation
Nucleus
Target data
Publications (2)
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ACS chemical biology 17:2605-2618 PubMed35952650
2022
Applications
Unspecified application
Species
Unspecified reactive species
Nature communications 13:2089 PubMed35440621
2022
Applications
Unspecified application
Species
Unspecified reactive species
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