Analytical Data
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Gene name
PION
- Application
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Alternative Names
A530088I07Rik; DKFZp667B242; Gamma-secretase-activating protein 16 kDa C-terminal form; GSAP; GSAP-16K; GSAP_HUMAN; MGC126548; Pigeon homolog (Drosophila) ; Pion; Protein pigeon homolog; tcag7.1314
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A4D1B5
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Expression Region
1-344 aa
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AA Sequence
MSEQRLYYIDLKKSRSILKCIQFYADESYNLMFEVPLDISLSNSGFKLVNFGCDYHQYRDKFSKHLTLCVFTNHTGSLCVCYSPKCASWGQITYSVFYIHKGHSKTFTTSLENVGSHMTKGITFLNLDYYVAVYLPGHFFHLLNVQHPDLICHNLFLTGNNEMIDMLPHCPLQSLSGSLVLDCCSGKLYRALLSQSSLLQLLQNTCLDCEKMAALHCALYCGQGAQFLEAQIIQWISENVSACHSFDLIQEFIIASSYWSVYSETSNMDKLLPHSSVLTWNTEIPGITLVTEDIALPLMKVLSFKGYWEKLNSNLEYVKYAKPHFHYNNSVVRREWHNLISEEV
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Molecular Weight
65.9 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
PION (Pioneer Interferon-Alpha) recombinant protein research has emerged due to the growing interest in understanding the therapeutic potentials of interferon-alpha and its variants in treating various diseases, including viral infections, certain types of cancers, and autoimmune disorders. Interferon-alpha has been recognized for its antiviral properties and its ability to modulate the immune response. The recombinant version, PION, is engineered to enhance stability, efficacy, and specificity compared to native forms, which may suffer from variability in biological activity and short half-lives. Recent advancements in biotechnology have facilitated the production of high-purity recombinant proteins, allowing researchers to explore PION's mechanisms of action, optimal dosing strategies, and potential combination therapies. Additionally, as global health challenges such as emerging viral pathogens and increasing cancer prevalence continue to escalate, the demand for effective biologics like PION is becoming more pronounced. Investigating its structure-function relationship, immunogenicity, and therapeutic windows can significantly advance our understanding of its clinical applications, paving the way for the development of new treatment regimens that harness the immune system's capabilities to combat diseases more effectively.
