Analytical Data
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Gene name
Gastric lipase
- Application
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Alternative Names
HGL; HLAL; Gastric lipase
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P07098
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Expression Region
Leu20~Lys398
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Molecular Weight
74kDa
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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
Gastric lipase is a crucial enzyme primarily produced in the stomach, playing a vital role in the digestion of dietary fats. Its primary function is to hydrolyze triglycerides into free fatty acids and diglycerides, which facilitates fat absorption in the intestines. Recent studies have shown that gastric lipase not only contributes to lipid digestion but also has potential implications in metabolic disorders and obesity, making it a subject of significant interest in the field of nutrition and health. However, the study of gastric lipase has been limited due to challenges in obtaining pure and active enzyme samples. Recombinant protein technology has emerged as a valuable method to produce gastric lipase in larger quantities and with enhanced purity. This approach allows for detailed biochemical characterization and functional analysis, offering insights into its enzymatic mechanisms and potential therapeutic applications. Furthermore, recombinant gastric lipase can be utilized in various industrial applications, including food processing and pharmaceutical formulations. As research progresses, understanding gastric lipase's structure-function relationship will pave the way for innovative strategies to target lipid metabolism disorders, enhancing human health and well-being.
