Analytical Data
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Gene name
SERT
- Application
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Alternative Names
SLC6A4; SLC6-A4; HTT; 5-HTT; 5HTT; OCD1; hSERT; Solute Carrier Family 6,Member 4; Neurotransmitter Transporter,Serotonin; Sodium-dependent serotonin transporter
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
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Expression Region
Ser483~Val630
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Molecular Weight
20kDa
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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
SERT, or serotonin transporter, plays a crucial role in the regulation of synaptic serotonin levels, which are pivotal for mood, anxiety, and overall mental health. Abnormalities in SERT function have been linked to various psychiatric disorders, including depression, anxiety, and obsessive-compulsive disorder. Understanding SERT at a molecular level is essential for developing new therapeutic strategies for these conditions. Research into SERT has advanced significantly with the advent of recombinant protein technology, allowing for the expression and purification of SERT in controlled laboratory settings. This has enabled scientists to study the transport mechanisms, structural characteristics, and pharmacological properties of SERT in detail. Recent studies utilizing techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into the conformational changes of SERT during the transport cycle, revealing potential drug binding sites and elucidating how different inhibitors interact with the transporter. Moreover, mutations in the SERT gene have been shown to influence its function and are implicated in individual variability in response to antidepressant treatments. As the understanding of SERT biology deepens, it holds promise for the development of novel pharmacological agents aimed at modulating its activity, thus offering hope for improved treatment options for mental health disorders. Overall, SERT recombinant protein research not only enhances our fundamental understanding of serotonin transport but also contributes to the broader field of neuropharmacology and mental health therapeutics.
