Analytical Data
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Gene name
TDH
- Application
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Alternative Names
Tdh;L-threonine 3-dehydrogenase. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P20132
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Expression Region
1-328aa
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AA Sequence
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVCGGSNISLAQLRALKEQLGMTNRLPK
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Molecular Weight
42.1 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
The study of TDH (thioredoxin-like protein) recombinant proteins has gained substantial attention in recent years due to their significant roles in various biological processes and potential applications in biotechnology and medicine. TDH, primarily known as a key enzyme in redox regulation, plays a critical role in maintaining cellular homeostasis and responding to oxidative stress. Its ability to facilitate protein folding and protect against denaturation has positioned it as a valuable candidate for therapeutic applications, including cancer therapy and neuroprotection. Moreover, the advancement of recombinant DNA technology has enabled the production of TDH proteins in various expression systems, enhancing their availability for research and industrial purposes. The ability to produce high yields of functional TDH proteins allows for extensive studies into their biochemical properties, interactions, and mechanisms of action. Consequently, research into TDH recombinant proteins not only sheds light on fundamental cellular processes but also opens new avenues for the development of novel therapeutic strategies and the improvement of biotechnological applications. As the understanding of TDH continues to deepen, its potential as a biomolecular tool and therapeutic agent is increasingly recognized, highlighting the importance of continued investigation in this field.
