Analytical Data
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Gene name
XPO1
- Application
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Alternative Names
Exp1; CRM1 Homolog,Yeast; Chromosome region maintenance 1 protein homolog
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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
O14980
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Expression Region
Thr917~Asp1071
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Molecular Weight
21kDa
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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
XPO1, also known as exportin 1, is a crucial transport protein involved in the nuclear-cytoplasmic export of various macromolecules, including RNA and proteins. This protein operates through a unique mechanism that recognizes and binds to cargoes containing a nuclear export signal (NES), facilitating their transport through the nuclear pore complex. Research on XPO1 has gained significant attention due to its role in the regulation of numerous cellular processes, including gene expression, cell cycle progression, and apoptosis. Dysregulation of XPO1 has been implicated in various pathological conditions, including cancer, where it contributes to the export of tumor suppressor proteins and other regulatory molecules, promoting malignancy. The study of XPO1 and its associated pathways has led to the development of novel therapeutic strategies, such as the use of selective inhibitors to disrupt its function in cancer cells. This has prompted extensive investigations into the structural and functional characteristics of XPO1, including the characterization of its recombinant protein forms. Understanding the intricacies of XPO1’s operation and developing recombinant versions of this protein provides valuable insight into its biological significance and potential as a therapeutic target. Thus, research focused on XPO1 recombinant proteins is essential for advancing our knowledge of cellular transport mechanisms and their implications in health and disease.
