Analytical Data
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Gene name
DLD
- Application
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Alternative Names
DLD;Probable D-lactate 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
P98173
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Expression Region
34-230aa
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AA Sequence
MKHHHHHHAS FPRIQQLFTS PESSVTAAPR ARKYKCGLPQ PCPEEHLAFR VVSGAANVIG PKICLEDKML MSSVKDNVGR GLNIALVNGV SGELIEARAF DMWAGDVNDL LKFIRPLHEG TLVFVASYDD PATKMNEETR KLFSELGSRN AKELAFRDSW VFVGAKGVQN KSPFEQHVKN SKHSNKYEGW PEALEMEGCI PRRSTAS
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Molecular Weight
23 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
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Protein Description
DLD (Dihydrolipoamide Dehydrogenase) is an essential enzyme involved in mitochondrial metabolism, playing a crucial role in the purview of energy production and redox homeostasis. Its dysfunction has been associated with various metabolic disorders and neurodegenerative diseases, making it an important target for therapeutic interventions. The study of recombinant DLD proteins has gained momentum as researchers seek to understand the biochemical properties and functional mechanisms of this enzyme. Recombinant DLD production allows for the exploration of its structure-function relationship and post-translational modifications, which are crucial for its enzymatic activity. Additionally, the ability to produce DLD in a controlled environment enables researchers to assess its interactions with other proteins and potential substrates. Investigating the recombinant form of DLD not only sheds light on its biological significance but also facilitates the development of novel drugs aimed at rectifying its dysfunction. Advances in protein engineering and purification techniques have further enhanced the feasibility of studying this enzyme, paving the way for a deeper understanding of mitochondrial diseases and the creation of innovative therapeutic strategies. As the research unfolds, it holds promise not only for basic science but also for clinical applications, addressing the pressing need for effective treatments for conditions linked to DLD deficiencies.
