Analytical Data
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基因名
Pru p 1.01
- Application
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别名
/
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种属
Prunus dulcis x Prunus persica
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
B6CQR8
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表达区间
1-160aa
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分子量
33.6 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
Pru p 1.01 is a major allergen derived from the peach tree (Prunus persica) and is primarily responsible for allergic reactions in sensitized individuals, particularly those with oral allergy syndrome. The significance of studying Pru p 1.01 lies in its prevalence among fruit allergy sufferers, especially in regions where peaches are commonly consumed. Research has shown that this protein shares structural similarities with pathogenesis-related proteins found in other plants, which may contribute to cross-reactivity among various fruit allergens. The molecular characterization and structural analysis of Pru p 1.01 can provide insights into its allergenic properties, immune responses, and the mechanisms underlying fruit allergies. Additionally, understanding the biochemical pathways involved in the expression and IgE-binding capabilities of Pru p 1.01 may aid in developing targeted immunotherapies and diagnostic tools for peach allergies. The increasing incidence of food allergies globally highlights the need for a deeper understanding of key allergens like Pru p 1.01, making it a vital subject of ongoing research in allergy and immunology. Through recombinant protein technology, researchers aim to produce Pru p 1.01 in sufficient quantities for further study, allowing for advances in both therapeutic interventions and the development of hypoallergenic peach varieties to mitigate allergic reactions in predisposed individuals.
