Analytical Data
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Gene name
Transthyretin/TTR
- Application
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Alternative Names
ATTR Prealbumin; TBPA; PALB;
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Species
Pongo abelii
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5NVS2
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Expression Region
21-147aa
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Molecular Weight
29.7 kDa
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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
Transthyretin (TTR) is a tetrameric protein primarily produced in the liver and is crucial for the transport of thyroxine and retinol-binding protein. It plays a significant role in maintaining thyroid hormone balance and vitamin A metabolism in the human body. However, mutations in the TTR gene can lead to various amyloid diseases, such as familial amyloidotic polyneuropathy and senile systemic amyloidosis, which are characterized by the deposition of misfolded TTR. The study of recombinant TTR proteins has gained momentum due to their potential therapeutic applications, including the development of small molecules that stabilize the tetrameric form of TTR and prevent its misfolding. Moreover, recombinant TTR can be utilized to explore the mechanisms of amyloidogenesis, investigate structure-function relationships, and enhance our understanding of TTR-related pathologies. Current research is focused on elucidating the protein’s folding pathways, identifying stabilizing ligands, and evaluating their implications in drug design. The advancement of recombinant DNA technology has facilitated the expression and purification of TTR in various model systems, enabling high-throughput screening of compounds that may mitigate the aggregation propensity of TTR. With ongoing studies, recombinant TTR represents a promising avenue for effective therapeutic strategies aimed at combating TTR-related diseases and improving patient outcomes.
