Analytical Data
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Gene name
TRO
- Application
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Alternative Names
MAGE-d3; MAGED3; MAGE-D3 antigen
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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
Q12816
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Expression Region
Leu444~Ala642
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Molecular Weight
27kDa
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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
TRO, or Tryptophan-Responsive Opioid Peptide, is a class of recombinant proteins that has garnered significant attention in the fields of biochemistry and pharmacology due to its unique biological properties and potential therapeutic applications. These proteins are derived from the tryptophan-rich domains commonly found in various biological systems, where they play a critical role in cellular signaling and metabolic processes. Recent studies have highlighted the importance of TRO in regulating neurotransmitter release and its involvement in pain modulation pathways, making it a promising candidate for the development of novel analgesics. The ability to recombinantly express TRO has enabled researchers to produce these proteins in a controlled and scalable manner, facilitating detailed functional assays and structure-function relationship studies. Furthermore, the exploration of TRO's interactions with specific opioid receptors opens new avenues for drug design, particularly in the context of addressing opioid addiction and resistance. Overall, ongoing research into TRO and its derivatives aims to elucidate their mechanisms of action, improve their stability and efficacy, and assess their potential as innovative therapeutic agents for pain management and other related disorders.
