Analytical Data
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Gene name
TNPO1
- Application
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Alternative Names
TNPO1；KPNB2；MIP1；TRN；Transportin-1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92973-2
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Expression Region
25-141aa
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AA Sequence
PDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSEDEPTRSLSGLILKN NVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASKGELQ NWPDLLPKLCSLLDSED*
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Molecular Weight
39 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
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Protein Description
TNPO1 (Transportin 1) is a nuclear transport receptor that plays a critical role in the import of proteins and RNA into the nucleus. It is particularly responsible for shuttling proteins containing a nuclear localization signal (NLS) across the nuclear pore complex. Research into TNPO1 became prominent due to its involvement in various cellular processes, including gene expression regulation, cellular signaling, and the maintenance of nuclear-cytoplasmic transport. Additionally, TNPO1 has been implicated in several diseases, including cancer and viral infections, as certain viruses exploit this transport mechanism to facilitate their replication and pathogenesis. The study of recombinant TNPO1 protein offers valuable insights into its structural and functional attributes, enabling researchers to dissect the molecular mechanisms underlying its transport activities. Moreover, elucidating the interactions between TNPO1 and its cargo proteins can unveil potential therapeutic targets for diseases related to aberrant nuclear transport. The production of recombinant TNPO1 in systems such as bacteria or yeast can also facilitate the study of its biochemical properties and interactions, paving the way for developing inhibitors or modulators that could disrupt its function in pathological conditions. Overall, the investigation of TNPO1 and its recombinant form is essential for understanding cellular dynamics and could contribute to innovative strategies for disease management and therapeutic advancements.
