Analytical Data
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Gene name
PAS
- Application
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Alternative Names
Komagataella phaffii (strain GS115 / ATCC 20864); Yeast; Oxidoreductase
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Species
Others
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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
C4R4L0
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Expression Region
M1-K354
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Protein Length
Full Length
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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
The study of PAS (Per-ARNT-Sim) domain-containing proteins has gained significant interest due to their crucial roles in various biological processes, including circadian rhythms, hypoxia response, and cellular signaling pathways. PAS domains are conserved protein motifs that facilitate protein-protein interactions and are found in a diverse array of proteins across different organisms, primarily in transcription factors and sensor proteins. These domains enable the proteins to sense environmental signals, such as light and oxygen levels, and transduce these signals to regulate gene expression accordingly. Research has revealed that dysfunctional PAS domain proteins are implicated in various diseases, including cancer and metabolic disorders, highlighting their potential as therapeutic targets. Furthermore, the recombinant expression of PAS domain-containing proteins allows for detailed biophysical and biochemical characterization, enabling the elucidation of their mechanisms of action. This synthetic approach also fosters the development of novel biomolecular tools and therapeutics. Overall, the exploration of PAS domain proteins not only enhances our understanding of fundamental biological processes but also opens new avenues for medical research and biotechnological applications.
