Analytical Data
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Gene name
Pal
- Application
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Alternative Names
(PAL)(19 kDa surface antigen)(PPL)
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Species
Legionella pneumophila
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P26493
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Expression Region
22-176aa
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Molecular Weight
17.0 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
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Protein Description
Pal (palmitoyl protein thioesterase) is a crucial enzyme involved in the post-translational modification of proteins through palmitoylation, a lipidation process that influences various cellular functions, including membrane localization, protein stability, and signaling pathways. The significance of Pal in cellular dynamics and its potential implications in diseases such as Alzheimer's, Huntington's disease, and cancer have prompted extensive research. Altered palmitoylation patterns due to the dysfunction of Pal can disrupt normal cellular processes and contribute to the pathogenesis of these conditions. Additionally, the modulation of palmitoylation is being explored as a therapeutic strategy, highlighting the need for a deeper understanding of the molecular mechanisms governing Pal's activity. Recent advances in structural biology and biochemistry have enabled researchers to elucidate the functional roles of Pal in palmitoylation and its interactions with various target proteins. By leveraging techniques such as mutagenesis, biochemical assays, and high-resolution imaging, scientists are investigating how alterations in Pal function affect cellular homeostasis and contribute to disease mechanisms. The ongoing research on Pal and its associated pathways holds potential for developing innovative therapeutic approaches to modulate palmitoylation-dependent processes, offering hope for targeted interventions in diseases characterized by aberrant protein modifications. Understanding Pal's role in cellular physiology further enhances our grasp of the complex network of protein modifications, emphasizing the necessity of continued exploration in this area to uncover new insights and clinical applications.
