Analytical Data
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Gene name
LIPA
- Application
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Alternative Names
LIPA；Lysosomal acid lipase/cholesteryl ester hydrolase
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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
P38571
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Expression Region
22-399aa
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AA Sequence
SGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ
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Molecular Weight
47.1 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
LIPA (Lysosomal Acid Lipase) is an enzyme that plays a critical role in lipid metabolism, particularly in the hydrolysis of triglycerides and cholesterol esters within lysosomes. Deficiencies in LIPA activity are associated with disorders such as Wolman disease and cholesteryl ester storage disease, both of which can lead to severe metabolic dysfunction due to the accumulation of lipids in various tissues. The exploration of LIPA's structure and function is vital for understanding these conditions and developing therapeutic interventions. Recent advances in recombinant protein technology have enabled researchers to produce LIPA in a laboratory setting, facilitating detailed studies of its enzymatic activity and substrate specificity. This research not only contributes to the fundamental understanding of lipid metabolism but also paves the way for potential enzyme replacement therapies that could provide relief for patients suffering from LIPA-related disorders. By investigating the application of recombinant LIPA, scientists aim to develop treatments that target the underlying causes of lipid accumulation and promote healthier metabolic profiles, thereby enhancing patient outcomes in lipid storage diseases.
