Analytical Data
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Gene name
Dlst
- Application
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Alternative Names
Dlst；KIAA1630；2-oxoadipate dehydrogenase complex component E1
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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
P36957
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Expression Region
1-453aa
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AA Sequence
MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFFRTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
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Molecular Weight
48.7kDa
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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
Dlst (dihydrolipoamide S-acetyltransferase) is a crucial enzyme that plays a significant role in the mitochondrial metabolism of energy and the tricarboxylic acid (TCA) cycle. It participates in the oxidative decarboxylation of pyruvate, linking glycolysis and the TCA cycle, and is also involved in the regulation of various metabolic pathways by facilitating the transfer of acyl groups. Research on Dlst recombinant protein has gained momentum due to its potential implications in understanding metabolic disorders, including diabetes and obesity, as well as neurodegenerative diseases linked to mitochondrial dysfunction. The exploration of Dlst's structure and function through recombinant technology allows for detailed studies on its enzymatic activity, interactions with other metabolic components, and regulatory mechanisms. Additionally, insights derived from Dlst research could pave the way for the development of targeted therapeutics aimed at correcting metabolic imbalances. Advances in protein engineering techniques are enabling scientists to create modified versions of Dlst with enhanced stability and activity, thereby contributing to a deeper understanding of mitochondrial biology and its relevance to human health. The study of Dlst's recombinant forms also provides a valuable platform for investigating potential inhibitors or activators of the enzyme, which could lead to novel treatment options for conditions that stem from metabolic dysregulation. Overall, Dlst continues to be a focal point of research within the fields of biochemistry and pharmacology, highlighting its importance in metabolic health and disease.
