Analytical Data
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Gene name
ACAT1
- Application
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Alternative Names
ACAT1；ACACT；ACACT1；ACAT；Sterol O-acyltransferase 1
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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
P24752
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Expression Region
249-321aa
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AA Sequence
PPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYL YFLFAPTLIYRDSYPRNPTVRWG
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Molecular Weight
34 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
ACAT1 (Acyl-CoA cholesterol acyltransferase 1) is an important enzyme involved in lipid metabolism, specifically in the esterification of cholesterol and fatty acids. This process is critical for maintaining cholesterol homeostasis and regulating its transport and storage within cells. Dysregulation of ACAT1 has been implicated in various pathological conditions, including cardiovascular diseases, atherosclerosis, and neurodegenerative disorders. Research into ACAT1 recombinant protein has gained traction as scientists seek to better understand its biochemical properties and physiological roles. By producing and purifying ACAT1 in a recombinant form, researchers can investigate its enzymatic activity, substrate specificity, and interactions with other cellular components. Furthermore, characterizing the recombinant protein can provide insights into the mechanisms of diseases associated with altered ACAT1 function, potentially leading to the development of novel therapeutic strategies targeting this enzyme. Overall, the study of ACAT1 recombinant protein is crucial for elucidating its role in lipid metabolism and its implications for human health, making it a significant focus in biochemical and pharmaceutical research.
