Analytical Data
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Gene name
DTNa
- Application
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Alternative Names
DTN-A; DRP3; DTN; LVNC1; Dystrophin-Related Protein 3
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Species
Human
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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
Q9Y4J8
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Expression Region
Met1~Glu288
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Molecular Weight
36kDa
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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
DTNa, a recombinant protein derived from the tetanus toxin, has garnered significant attention in scientific research due to its potential applications in various fields, including vaccine development and neurobiology. The understanding of the structure and function of DTNa is crucial because it serves as a key component in the design of improved vaccines against tetanus. The protein’s ability to act as a non-toxic carrier for antigen delivery makes it a valuable tool for generating immune responses without the risks associated with the entire toxin. Furthermore, DTNa's unique interactions with neuronal cells have opened new avenues in the study of synaptic transmission and neurodegenerative diseases. Research has focused on the optimization of DTNa production through recombinant techniques, allowing for higher yields and better functional properties. Additionally, the exploration of DTNa's immunogenicity, stability, and pharmacokinetics is vital for advancing its use in clinical settings. Overall, the investigation of DTNa as a recombinant protein not only enhances our understanding of its biological mechanisms but also paves the way for innovative therapeutic strategies against diseases associated with the tetanus toxin and related neurological disorders.
