Analytical Data
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Gene name
TRIP13
- Application
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Alternative Names
(Human papillomavirus type 16 E1 protein-binding protein)(16E1-BP)(HPV16 E1 protein-binding protein)(Thyroid hormone receptor interactor 13)(Thyroid receptor-interacting protein 13)(TR-interacting protein 13)(TRIP-13)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15645
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Expression Region
1-432aa
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Molecular Weight
54.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
TRIP13, or thyroid hormone receptor interactor 13, is an ATPase that plays a crucial role in various cellular processes, particularly in the context of the cell cycle and DNA repair. Its importance has been underscored by its involvement in the regulation of mitotic progression and the maintenance of genome stability. Recent studies have revealed that TRIP13 functions as a key regulator of the spindle assembly checkpoint, ensuring proper chromosome segregation during cell division. Dysregulation of TRIP13 has been linked to various cancers, suggesting that it may operate as a potential biomarker or therapeutic target. Furthermore, TRIP13 is known to interact with several proteins involved in the repair of DNA double-strand breaks, highlighting its pivotal role in maintaining cellular integrity under stress conditions. Research into TRIP13 is expanding, with investigations focusing on its structural features, mechanistic functions, and implications in disease pathogenesis. Understanding the multifaceted roles of TRIP13 could provide valuable insights into tumor biology and pave the way for novel therapeutic strategies in cancer treatment and other diseases characterized by genomic instability.
