Analytical Data
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Gene name
DLAT
- Application
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Alternative Names
DLTA; PDC-E2; PBC; M2 antigen complex 70 kDa subunit; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E2
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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 95% as determined by SDS-PAGE.
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Uniprot
P10515
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Expression Region
Gln374~Trp631
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Molecular Weight
28kDa
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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
DLAT, or dihydrolipoamide acetyltransferase, is a critical enzyme in the mitochondrial pyruvate dehydrogenase complex (PDC), playing a pivotal role in cellular energy metabolism by catalyzing the conversion of pyruvate into acetyl-CoA. Research into DLAT recombinant protein is increasingly important due to its involvement in various metabolic disorders, including diabetes and certain neurodegenerative diseases. Mutations or dysregulation of DLAT can lead to impaired metabolic functions, underscoring the need for a comprehensive understanding of its structural and functional properties. Recombinant DLAT protein enables researchers to study the enzyme in vitro, facilitating investigations into its enzymatic mechanisms, interacting partners, and regulatory pathways. Furthermore, the study of DLAT's structure through techniques such as X-ray crystallography and NMR spectroscopy can reveal insights into substrate binding and activity modulation. This research has the potential to inform therapeutic strategies aimed at restoring normal metabolic function in conditions where DLAT is compromised, making it a significant focus in the field of biochemical research and metabolic disease therapy.
