Analytical Data
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Gene name
AER
- Application
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Alternative Names
AER；AER61；C3orf64；EOGT1；EGF domain-specific O-linked N-acetylglucosamine transferase
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Species
E.coli
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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
Q39172
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Expression Region
1-345aa
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AA Sequence
MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVVARE
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Molecular Weight
38.1 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
AER (Atypical Erythropoietin Receptor) fusion proteins have garnered significant interest in biomedical research due to their unique structural and functional properties. Erythropoietin (EPO), primarily known for its role in red blood cell production, operates through its specific receptor, which has a well-characterized signaling pathway. However, the AER variant exhibits atypical characteristics that suggest its involvement in alternative biological processes, such as cell survival, proliferation, and even metabolic regulation. Researchers have begun to explore the potential applications of AER fusion proteins in therapeutic contexts, such as in the treatment of anemia and other blood disorders, as well as in cancer therapy, where modulation of the pathways influenced by AER could provide innovative approaches for intervention. The ability to engineer AER fusion proteins opens up opportunities for developing novel drugs that can target specific cellular functions, leading to improved efficacy and reduced side effects compared to traditional therapies. Furthermore, ongoing studies aim to elucidate the intricate mechanisms underlying AER's role in various physiological and pathological conditions, which may reveal new insights into the modulation of immune responses and tissue regeneration. As the field of protein engineering advances, the AER fusion protein stands out as a promising candidate for novel therapeutic strategies, warranting deeper investigations into its molecular biology and potential clinical applications.
