Analytical Data
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Gene name
Carboxyl Ester Lipase/CEL
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简介
Carboxyester lipase/CEL protein plays a crucial role in cellular processes as it catalyzes the hydrolysis of a variety of substrates, including cholesterol esters, phospholipids, lysophospholipids, diacylglycerols and triacylglycerols, and lipids of hydroxy fatty acids acid ester. FAHF). Carboxyl Ester Lipase/CEL Protein, Mouse (sf9, His) is the recombinant mouse-derived Carboxyl Ester Lipase/CEL protein, expressed by Sf9 insect cells , with C-His labeled tag.
- Application
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Alternative Names
Bile salt-activated lipase; BAL; BSSL; Cel; Lip1
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Species
Mouse
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Source
Baculovirus
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q64285
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Expression Region
M1-L534
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Protein Length
Partial
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Molecular Weight
133.9 kDa & 59.1 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
Carboxyl Ester Lipase (CEL) is a member of the lipase family, known for its ability to hydrolyze ester bonds in lipids, which has garnered significant interest in biochemical and industrial applications. CEL is primarily produced in the pancreas and plays a crucial role in lipid metabolism, making it essential for understanding various physiological processes and disorders, such as obesity and metabolic syndromes. The research surrounding CEL has expanded due to the enzyme's potential in biocatalysis, particularly in synthesizing biodiesel, producing flavor compounds, and in pharmaceutical industries for drug development and formulation. The recombinant protein of CEL is often produced in microbial hosts, allowing for high yields and ease of purification, which facilitates detailed studies of its enzymatic activity and structure-function relationships. Advances in molecular biology techniques have enabled the engineering of CEL to improve its stability and specificity, enhancing its practicality in diverse applications. By studying the recombinant CEL, researchers aim to uncover the underlying mechanisms of its activity, optimize its performance for industrial processes, and potentially develop novel therapeutic strategies targeting lipid metabolism disorders. The growing body of research on CEL not only contributes to our fundamental understanding of lipase biology but also opens avenues for innovative approaches in biotechnology and medicine.
