Analytical Data
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Gene name
DGAT2
- Application
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Alternative Names
ARAT; Acyl-CoA retinol O-fatty-acyltransferase; Diglyceride acyltransferase 2
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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 90% as determined by SDS-PAGE.
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Uniprot
Q96PD7
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Expression Region
Arg268~Phe377
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Molecular Weight
17kDa
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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
DGAT2 (Diacylglycerol O-acyltransferase 2) is a critical enzyme involved in lipid metabolism, playing a pivotal role in triacylglycerol (TAG) synthesis. Its importance lies in the growing concerns surrounding metabolic disorders, obesity, and related diseases, as TAG accumulation is closely linked to these conditions. Research on DGAT2 has gained momentum due to its potential as a therapeutic target for treating lipid-related diseases. Understanding the structural and functional characteristics of DGAT2 through recombinant protein studies is essential, as it allows researchers to elucidate its enzymatic mechanisms and interactions with other proteins and substrates. Recombinant DGAT2 proteins serve as invaluable tools for investigating substrate specificity, inhibition mechanisms, and the effects of genetic variations on enzyme activity. Furthermore, these studies can enhance our knowledge about lipid storage and mobilization processes, potentially leading to novel strategies for managing fatty liver disease and metabolic syndrome. The successful expression and purification of DGAT2 in heterologous systems facilitate detailed biochemical assays and structural analyses, paving the way for the development of small-molecule inhibitors or modulators that could regulate its activity in vivo. Thus, the research on DGAT2 recombinant proteins is crucial for both fundamental science and the advancement of clinical applications aimed at addressing lipid dysregulation.
