Analytical Data
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基因名
AER
- Application
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别名
AER;AER61;C3orf64;EOGT1;EGF domain-specific O-linked N-acetylglucosamine transferase
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q39172
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表达区间
1-345aa
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氨基酸序列
MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVVARE
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分子量
38.1 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












