Analytical Data
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Gene name
TFE3
- Application
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Alternative Names
TFE3；BHLHE33；Transcription factor E3
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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
P19532
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Expression Region
166-254aa
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AA Sequence
RPPPAQVPREVLKVQTHLENPTRYHLQQARRQQVKQYLSTTLGPKLASQA LTPPPGPASAQPLPAPEAAHTTGPTGSAPNSPMALLTIG
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Molecular Weight
36 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
TFE3 (Transcription Factor E3) is a member of the microphthalmia family of basic helix-loop-helix (bHLH) transcription factors. It plays a significant role in various biological processes, including cellular differentiation, proliferation, and apoptosis. The study of TFE3 has garnered interest due to its involvement in several diseases, particularly cancers and metabolic disorders. Abnormal expression or activity of TFE3 has been implicated in the pathogenesis of particular tumors, such as clear cell renal carcinoma and Alveolar soft part sarcoma, often associated with genetic rearrangements leading to TFE3 fusion proteins. These fusions typically enhance its transcriptional activity, resulting in the aberrant regulation of target genes. In addition, TFE3 is critical in governing lysosomal biogenesis and cellular responses to stress, thus influencing metabolic homeostasis. The development of TFE3 recombinant proteins facilitates the exploration of its functional roles and the mechanisms underlying its activity. These studies are further propelled by advances in molecular biology techniques, providing insights into TFE3's interactions with other biomolecules and its downstream effects. Consequently, the investigation of TFE3 recombinant proteins not only enhances our understanding of TFE3's physiological roles but also offers potential therapeutic avenues for targeting diseases associated with TFE3 dysregulation.
