Analytical Data
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Gene name
AGPAT2
- Application
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Alternative Names
AGPAT2; 1-acyl-sn-glycerol-3-phosphate acyltransferase beta; 1-acylglycerol-3-phosphate O-acyltransferase 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15120
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Expression Region
1-278aa
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AA Sequence
MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ
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Molecular Weight
57.3 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
Related Products
Protein Description
AGPAT2, or 1-acylglycerol-3-phosphate O-acyltransferase 2, is an enzyme that plays a crucial role in lipid metabolism, particularly in the biosynthesis of triglycerides and phospholipids. Mutations in the AGPAT2 gene have been linked to human diseases such as congenital Lipodystrophy, characterized by the abnormal accumulation of fat in certain areas of the body and a deficiency in adipose tissue. This condition can lead to severe metabolic complications, including insulin resistance and fatty liver disease. Given the significance of AGPAT2 in maintaining lipid homeostasis, researchers have focused on the development and characterization of AGPAT2 recombinant protein to study its enzymatic activity and regulatory mechanisms. This research is particularly important for understanding the molecular pathways involved in lipid metabolism and for exploring potential therapeutic strategies for metabolic disorders. By producing AGPAT2 as a recombinant protein, scientists can investigate its structure-function relationship, interactions with other cellular components, and the effects of specific mutations. Data obtained from these studies could provide insights into the biochemical pathways impacted by AGPAT2 dysfunction and lay the groundwork for innovative treatments tailored to combat metabolic diseases associated with lipid dysregulation.











