Analytical Data
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Gene name
LPCAT3
- Application
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Alternative Names
MBOAT5; C3F; OACT5; Nessy; LPSAT; Membrane Bound O-AcylTransferase Domain Containing 5; Lysophospholipid Acyltransferase 5; Lysophosphatidylserine acyltransferase
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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
Q6P1A2
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Expression Region
Met122~Arg233
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Molecular Weight
19kDa
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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
LPCAT3 (lysophosphatidylcholine acyltransferase 3) is an enzyme that plays a crucial role in lipid metabolism, specifically in the synthesis of phosphatidylcholine, a major component of cell membranes. Research into LPCAT3 has gained significant attention due to its involvement in various physiological and pathological processes, including inflammation, atherosclerosis, and cancer. Dysregulation of LPCAT3 expression and activity has been implicated in several diseases, making it a potential therapeutic target. The enzyme catalyzes the acylation of lysophosphatidylcholine, thereby influencing lipid composition and cellular signaling pathways. Understanding the structure and function of LPCAT3, through recombinant protein studies, may provide insights into its regulatory mechanisms and the development of lipid-based therapies. Furthermore, investigating LPCAT3's role in cellular processes can help elucidate its contribution to disease progression and reveal novel pharmacological approaches for modulating its activity in pathological conditions. Overall, research on LPCAT3 recombinant proteins not only enhances our understanding of lipid biochemistry but may also pave the way for innovative strategies in treating lipid-related disorders.
