Analytical Data
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Gene name
DBT
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简介
DBT proteins are components of the branched-chain α-keto dehydrogenase complex, which catalyzes the conversion of α-keto acids into acyl-CoA and CO(2). This complex includes branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2), and lipoamide dehydrogenase (E3). DBT Protein, Human (sf9, His) is the recombinant human-derived DBT protein, expressed by Sf9 insect cells , with N-His labeled tag.
- Application
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Alternative Names
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; BCKAD-E2; DBT
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Species
Human
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Source
Baculovirus
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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
P11182
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Expression Region
G62-K482
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Protein Length
Full Length of Mature Protein
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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
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Protein Description
DBT, or Dihydrolipoamide Branched-Chain Transacylase, is a crucial component of the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC), which plays a vital role in the metabolism of branched-chain amino acids (BCAAs) like leucine, isoleucine, and valine. Deficiencies in DBT or dysfunctions in the BCKDC are associated with metabolic disorders, including maple syrup urine disease (MSUD), which can lead to severe neurological impairments if left untreated. The study of DBT restructuring has gained prominence as researchers explore its potential therapeutic applications, particularly in understanding the enzyme's structure-function relationships, enhancing stability, and improving its catalytic efficiency. Advances in protein engineering and structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have facilitated a deeper understanding of DBT's active sites and interaction mechanisms, allowing for the design of more effective enzyme variants. Furthermore, the findings from DBT research may have broader implications beyond metabolic disorders, potentially illuminating pathways in cancer metabolism and other diseases influenced by BCAA metabolism. Overall, DBT represents a vital target for research aimed at unraveling metabolic pathways and developing innovative treatments for related diseases.
