Analytical Data
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Gene name
Lipase
- Application
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Alternative Names
Lipase; EC 3.1.1.3; Triacylglycerol lipase
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Species
Rhizomucor miehei
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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
P19515
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Expression Region
25-363aa
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Molecular Weight
40.8 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
Lipase, a crucial enzyme involved in lipid metabolism, catalyzes the hydrolysis of triglycerides into glycerol and free fatty acids, playing a significant role in various biological processes. The increasing demand for lipases in industrial applications, including food processing, pharmaceuticals, and biofuels, has driven extensive research into their properties and functions. The development of recombinant lipases has emerged as a promising strategy to enhance their yield, stability, and specificity. By utilizing recombinant DNA technology, scientists can produce lipase proteins in host organisms such as bacteria, yeast, or mammalian cells, allowing for high-level expression and easy purification. Moreover, the genetic modification of lipases can lead to improved enzymatic characteristics, enabling them to function under extreme conditions, such as high temperatures or varying pH levels, which are often required in industrial processes. Research in this area not only aims to optimize lipase production but also to explore the structure-function relationship of these enzymes, which can offer insights into their catalytic mechanisms. As the understanding of lipase structure and function advances, it opens new avenues for the development of customized lipase variants tailored for specific applications, thus contributing to innovations in biotechnology and sustainable practices.
