Analytical Data
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Gene name
PPL
- Application
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Alternative Names
PPL；PPL13；Placental Protein 13-like
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60437
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Expression Region
全长
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AA Sequence
full
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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
Protein-protein interactions (PPIs) play a crucial role in various biological processes, and understanding these interactions is essential for elucidating molecular functions and developing therapeutic interventions. The study of PPL (Pseudomonas putida Lipase) and its recombinant proteins has garnered significant attention due to their potential applications in biotechnology and medicine. PPL is known for its hydrolytic activity and stability under extreme conditions, making it a suitable candidate for industrial applications, such as biodiesel production and bioremediation. Researchers have focused on engineering PPL to enhance its catalytic efficiency and specificity through techniques like site-directed mutagenesis and directed evolution. This recombinant approach allows for the optimization of the enzyme's properties, thereby expanding its applicability in various fields. Additionally, the study of PPL recombinant proteins provides insights into the fundamental mechanisms of enzyme activity and stability, contributing to the broader understanding of lipase function. Moreover, the exploration of PPL and its engineered variants could lead to the development of new therapeutic strategies, particularly in the treatment of diseases related to dysfunctional lipid metabolism. Overall, the ongoing research on PPL and its recombinant forms highlights the importance of protein engineering in advancing both scientific knowledge and practical applications in diverse domains.
