Analytical Data
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Gene name
PPAN
- Application
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Alternative Names
Brix domain-containing protein 3;Peter Pan homolog
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NQ55
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Expression Region
1-473aa
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Molecular Weight
55.2 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
Related Products
Protein Description
PPAN (Poly(A)-binding Protein, Interacting Protein) is a protein of significant interest in molecular biology due to its pivotal role in various cellular processes, including mRNA processing, stability, and translation. Research on PPAN has gained momentum as its interactions with the Poly(A)-binding protein (PABP) and other RNA-binding proteins highlight its influence on gene expression regulation. The involvement of PPAN in critical cellular pathways, such as the cell cycle and response to stress, has been linked to various diseases, including cancer and neurodegenerative disorders. Understanding the structural and functional properties of PPAN is essential for elucidating its mechanisms in post-transcriptional regulation. Recent advancements in recombinant protein technology have enabled the production and study of PPAN in vitro, facilitating the exploration of its binding affinities and functional dynamics. Furthermore, by investigating the reconstitution of PPAN with RNA and other associated factors, researchers aim to delineate its role in ribonucleoprotein complex formation and its overall contribution to the cellular RNA landscape. This body of research not only enhances our understanding of PPAN but also holds potential for identifying novel therapeutic targets that could modulate its activity in disease contexts. As such, the study of PPAN and its recombinant forms is a promising frontier in cellular molecular biology and therapeutic development.
