Analytical Data
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Gene name
LPCAT4
- Application
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Alternative Names
AYTL3; AGPAT7; LPAAT; LPEAT2; Lysophosphatidylethanolamine Acyltransferase 2; Acyltransferase Like 3; 1-Acylglycerol-3-Phosphate O-Acyltransferase 7; Plasmalogen synthase
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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
Q643R3
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Expression Region
Pro175~Asp524
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Molecular Weight
42kDa
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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
LPCAT4 (Lysophosphatidylcholine acyltransferase 4) is an enzyme that plays a critical role in the synthesis of phospholipids, particularly in the incorporation of fatty acids into lysophosphatidylcholine to form phosphatidylcholine, a major component of cell membranes. Recent research has highlighted the significance of LPCAT4 in various biological processes, including lipid metabolism, cell signaling, and inflammatory responses. Abnormalities in LPCAT4 expression and function have been linked to several pathological conditions, such as metabolic disorders, cardiovascular diseases, and certain types of cancer. Given its pivotal role in cellular and physiological functions, LPCAT4 has emerged as a potential therapeutic target for combating these diseases. The study of recombinant LPCAT4 proteins allows researchers to delve into its enzymatic properties, regulatory mechanisms, and interactions with other molecular pathways. By producing and characterizing these recombinant proteins, scientists can better understand LPCAT4's function and its implications in health and disease. This research has the potential to pave the way for novel therapeutic approaches aimed at modulating LPCAT4 activity in various clinical contexts, ultimately contributing to advancements in medical treatment strategies.











