Analytical Data
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Gene name
DLST
- Application
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Alternative Names
(2-oxoglutarate dehydrogenase complex component E2)(OGDC-E2)(Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex)(E2K)
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Species
Rat
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q01205
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Expression Region
69-454aa
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Molecular Weight
48.9 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
DLST, or Dihydrolipoamide S-acetyltransferase, is an essential enzyme in the cellular metabolism of the 2-oxoglutarate and branched-chain alpha-ketoacid dehydrogenase complexes, playing a critical role in the mitochondrial energy production pathway. Research into DLST recombinant proteins has garnered attention due to their potential implications in understanding metabolic disorders and mitochondrial dysfunctions, which are linked to various diseases, including diabetes, neurodegenerative conditions, and cancer. By producing DLST in a recombinant form, researchers aim to elucidate its structural and functional characteristics, paving the way for insights into enzyme regulation and its interactions within multienzyme complexes. This work is crucial for elucidating the biochemical pathways in which DLST participates and may lead to the development of therapeutic strategies targeting metabolic diseases. Furthermore, recombinant DLST can be used as a tool to identify inhibitors or activators that could modulate its activity, providing avenues for drug development and precision medicine. Given the increasing prevalence of metabolic-related diseases globally, DLST research is positioned at the forefront of scientific inquiry that seeks to unravel complex metabolic networks and improve human health outcomes.
