Analytical Data
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Gene name
LIPB
- Application
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Alternative Names
SCGB1D2; LPHB; Secretoglobin Family 1D Member 2
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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 90% as determined by SDS-PAGE.
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Uniprot
O95969
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Expression Region
Glu22~Val90
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Molecular Weight
42kDa
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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
LIPB (Lipase B from *Candida antarctica*) is an important enzyme widely studied for its applications in various fields, including biocatalysis, pharmaceuticals, and food industries. As a member of the lipase family, LIPB exhibits unique properties such as broad substrate specificity and high catalytic efficiency, making it suitable for diverse biochemical reactions, including esterification and transesterification. The interest in LIPB research has grown due to its potential to replace traditional chemical processes with more environmentally friendly biocatalytic approaches. Advances in recombinant DNA technology have enabled the production of LIPB in heterologous expression systems, allowing for increased yields and more straightforward purification methods. Additionally, the study of LIPB's structure and function enhances our understanding of enzyme mechanisms, which can lead to the development of engineered variants with improved properties for specific industrial applications. Overall, the exploration of LIPB not only contributes to fundamental biological knowledge but also paves the way for innovative solutions in sustainable chemistry and biotechnology.
