Analytical Data
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Gene name
pal
- Application
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Alternative Names
pal；KIAA0198；Zinc finger Protein PLAGL2
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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
P0A913
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Expression Region
22-173aa
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AA Sequence
CSSNKNASNDGSEGMLGAGTGMDANGGNGNMSSEEQARLQMQQLQQNNIVYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGERRANAVKMYLQGKGVSADQISIVSYGKEKPAVLGHDEAAYSKNRRAVLVY
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Molecular Weight
18.8kDa
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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.
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Protein Description
PAL (phenylalanine ammonia-lyase) is an important enzyme involved in the phenylpropanoid biosynthetic pathway, which plays a crucial role in plant secondary metabolism. This enzyme catalyzes the conversion of phenylalanine to trans-cinnamic acid, serving as a precursor for various vital compounds, including flavonoids, lignins, and other phenolic substances. Research on PAL has gained significant attention due to its potential applications in enhancing plant growth, stress tolerance, and secondary metabolite production, which are essential for plant defense and adaptation in adverse environmental conditions. Additionally, PAL has been implicated in improving the nutritional and medicinal qualities of crops, making it a target for biotechnological manipulation. The study of PAL involves understanding its gene expression, regulation, and the impact of environmental factors on its activity, as well as exploring methods for recombinant protein production to facilitate in-depth functional studies. Various approaches, including molecular cloning, genetic engineering, and protein expression systems, have been employed to characterize and manipulate PAL to harness its benefits in agriculture and biotechnology. As research continues to unfold, PAL’s role in metabolic engineering and sustainable agricultural practices is becoming increasingly prominent, paving the way for advancements in crop improvement strategies and the development of novel therapeutic agents derived from plant metabolites. Understanding the mechanisms governing PAL activity and its regulation will provide insights into optimizing phenylpropanoid pathways for enhanced production of valuable compounds, thus contributing to food security and health enhancement in a rapidly changing world.
