Analytical Data
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Gene name
XPO6
- Application
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Alternative Names
EXP6; RANBP20; RAN Binding Protein 20; Ran-binding protein 20
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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
Q96QU8
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Expression Region
Ala2~Leu271
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Molecular Weight
34.3kDa
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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
XPO6, or exportin 6, is a member of the karyopherin family, which plays a crucial role in the nucleocytoplasmic transport of proteins and RNA. Recent studies have highlighted XPO6's involvement in the export of specific cargoes, particularly those containing the nuclear export signal (NES). This has significant implications for various physiological processes and diseases, including cancer, as it affects cellular signaling pathways and the localization of tumor suppressor proteins. The precise mechanisms by which XPO6 binds and transports its substrates are not fully understood, making it a target of interest for biochemical research. Investigating the structure and function of recombinant XPO6 protein can provide insights into its interaction with cargo and other transport machinery, which may unveil potential therapeutic strategies for diseases linked to dysregulated nuclear transport. Additionally, as XPO6 may exhibit tissue-specific expression and function, understanding its role across different cell types could also shed light on developmental biology and cellular homeostasis. Thus, the study of XPO6 recombinant protein is pivotal for elucidating its biological roles and therapeutic applications, warranting further research and exploration in the field of molecular biology and medicine.
