Cat: IPD-X28480

Recombinant Human SERT Protein (HEK293),Strep

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Analytical Data

  • Gene name

    SERT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HTT; SERT

  • Species

    Human

  • Source

    HEK293

  • Tag

    Strep

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P31645-1

  • Expression Region

    E73-T616

  • Protein Length

    Partial

  • 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

The serotonin transporter (SERT) is a critical protein involved in the reuptake of serotonin (5-HT) from the synaptic cleft, playing a vital role in regulating mood, anxiety, and various neurological disorders. Dysregulation of SERT function has been implicated in conditions such as depression, anxiety disorders, and obsessive-compulsive disorder, making it a significant target for pharmacological intervention. Research into the SERT protein has advanced through the development of recombinant SERT, which facilitates detailed studies of its structure, function, and interactions with various ligands, including selective serotonin reuptake inhibitors (SSRIs). Techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into its conformational changes and substrate binding mechanisms. Moreover, understanding SERT's role in serotonin signaling is crucial for deciphering the complexities of mental health disorders and developing more effective therapeutics. This ongoing research not only enhances our comprehension of SERT's biological significance but also paves the way for novel treatment strategies targeting serotonin reuptake pathways.

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