Analytical Data
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Gene name
DGAT2
- Application
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Alternative Names
DGAT2；Diacylglycerol O-acyltransferase 2
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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
Q96PD7
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Expression Region
1-388aa
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AA Sequence
MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN
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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 an enzyme crucial for triglyceride biosynthesis, playing a significant role in lipid metabolism and energy storage within cells. The enzyme catalyzes the final step of triacylglycerol formation, converting diacylglycerol and acyl-CoA into triglycerides, which are essential for maintaining cellular energy balance. Understanding the structure and function of DGAT2 is pivotal due to its implications in metabolic disorders and obesity, as dysregulation of lipid metabolism can lead to conditions such as non-alcoholic fatty liver disease (NAFLD) and cardiovascular diseases. Overexpression or inhibition of DGAT2 has been shown to influence fat accumulation in various tissues, making it a potential therapeutic target for treating metabolic syndromes. Recent studies focus on the recombinant expression of DGAT2 to examine its enzymatic properties, interaction with other proteins, and potential role in lipid droplet formation. By utilizing recombinant technology, researchers aim to gain insights into the enzyme’s structure-function relationship, facilitating the development of selective inhibitors or activators that could serve as novel treatments for obesity and related metabolic disorders. This research area continues to grow, emphasizing the need for efficient methods of producing high-quality DGAT2 protein for in vitro studies and potential drug design applications.
