Analytical Data
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Gene name
NUP188
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5SRE5
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Expression Region
Thr540~Gly782
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Molecular Weight
56kDa
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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
NUP188, a member of the nucleoporin family, is an integral component of the nuclear pore complex (NPC) that plays a crucial role in nucleocytoplasmic transport, facilitating the movement of proteins and RNA across the nuclear envelope. Recent studies have highlighted the importance of NUP188 in various cellular processes, including gene expression regulation, cell signaling, and maintaining nuclear integrity. Dysregulation of NUP188 has been implicated in several diseases, notably cancers, where alterations in nucleocytoplasmic transport mechanisms can lead to aberrant cell proliferation and survival. The study of recombinant NUP188 protein presents an opportunity to better understand its structural and functional properties, including its interactions with other nucleoporins and its role in the assembly of the NPC. By producing and characterizing recombinant NUP188, researchers aim to elucidate its specific contributions to nucleocytoplasmic transport and identify potential therapeutic targets for diseases associated with its dysregulation. This research is particularly relevant given the growing recognition of the nuclear pore complex as a pivotal player in cell biology and disease pathology, making NUP188 a promising candidate for further investigation in the context of cellular transport mechanisms and oncogenesis.
