Cat: IPD-X39371

Recombinant Human TFE3 Protein,His

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Analytical Data

  • Gene name

    TFE3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RCCP2; TFEA; BHLHE33; Transcription Tactor E Family Member A; Class E basic helix-loop-helix protein 33; Transcription factor E3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P19532

  • Expression Region

    Met1~Asn350

  • Molecular Weight

    45kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

TFE3 (Transcription Factor E3) is a member of the microphthalmia-associated transcription factor (MITF) family, which plays a crucial role in various biological processes, including cell differentiation, proliferation, and responses to environmental stimuli. Recently, TFE3 has garnered attention due to its involvement in specific types of cancers and its function as a crucial regulator in the autophagy pathway. Research has demonstrated that TFE3 is activated in response to stress conditions, leading to the transcription of genes that facilitate cellular survival and adaptation. Notably, TFE3 can undergo translocation in certain tumors, resulting in aberrant activation and contributing to oncogenesis. This has spurred interest in its potential as a therapeutic target and biomarker for cancer diagnosis and prognosis. Moreover, TFE3 has been implicated in various cellular processes, such as lysosomal biogenesis and metabolism, influencing both normal physiology and disease states. The production of recombinant TFE3 protein allows for detailed studies of its structure-function relationships, cellular roles, and the mechanisms underlying its regulation. Understanding TFE3's functions and interactions at the molecular level could unveil novel therapeutic strategies for conditions where TFE3 is dysregulated, thereby highlighting its significance in both basic research and clinical applications.

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