Analytical Data
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Gene name
LIPA
- Application
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Alternative Names
LAL; CESD; Lipase A,Lysosomal Acid,Cholesterol Esterase(Wolman Disease); Acid Cholesteryl Ester Hydrolase; Lysosomal acid lipase/cholesteryl ester hydrolase
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q64194
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Expression Region
Asn32~Ile358
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Molecular Weight
41kDa
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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, or lysosomal acid lipase, is an enzyme that plays a critical role in lipid metabolism by hydrolyzing triglycerides and cholesteryl esters within lysosomes. Mutations in the LIPA gene can lead to severe disorders such as Wolman disease and cholesteryl ester storage disease, which are characterized by the accumulation of lipids in various tissues, resulting in significant health complications. The study of LIPA, particularly its recombinant form, has gained substantial interest in recent years due to the potential for therapeutic applications and a better understanding of lipid-related diseases. Recombinant LIPA can be produced in various expression systems, enabling researchers to investigate its structural and functional properties in detail. Studies have focused on its enzymatic mechanisms, substrate specificity, and the effects of specific mutations on its activity. These investigations are crucial for developing enzyme replacement therapies and improving diagnostic tools for related diseases. Moreover, understanding the molecular intricacies of LIPA can also shed light on broader metabolic pathways and the interplay between lipid metabolism and various health conditions, including cardiovascular diseases and obesity. Overall, the research on recombinant LIPA not only aims to address specific metabolic disorders but also contributes to the wider field of metabolic research, providing insights that could lead to novel therapeutic strategies and improved patient outcomes.
