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Recombinant Human OVA protein

  • 中文名: 卵白蛋白(OVA)天然蛋白
  • 别    名: OVA;Ccr11;Lccr;C-C chemokine receptor-like 2
货号: PA2000-1050
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点OVA
Uniprot No O00421
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-344aa
氨基酸序列MANYTLAPEDEYDVLIEGELESDEAEQCDKYDAQALSAQLVPSLCSAVFVIGVLDNLLVVLILVKYKGLKRVENIYLLNLAVSNLCFLLTLPFWAHAGGDPMCKILIGLYFVGLYSETFFNCLLTVQRYLVFLHKGNFFSARRRVPCGIITSVLAWVTAILATLPEFVVYKPQMEDQKYKCAFSRTPFLPADETFWKHFLTLKMNISVLVLPLFIFTFLYVQMRKTLRFREQRYSLFKLVFAIMVVFLLMWAPYNIAFFLSTFKEHFSLSDCKSSYNLDKSVHITKLIATTHCCINPLLYAFLDGTFSKYLCRCFHLRSNTPLQPRGQSAQGTSREEPDHSTEV
预测分子量39,5 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是3条与重组OVA蛋白相关的参考文献示例(注:以下内容为假设性示例,实际文献需通过学术数据库查询验证):

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1. **文献名称**: *"High-level expression and purification of recombinant chicken ovalbumin in Escherichia coli for immunological studies"*

**作者**: Smith J, et al.

**摘要**: 本研究报道了利用大肠杆菌表达系统高效表达重组鸡卵白蛋白(OVA),并通过亲和层析纯化获得高纯度蛋白。实验证明该重组OVA能够在小鼠模型中诱导特异性抗体反应,适用于疫苗研发及免疫应答机制研究。

2. **文献名称**: *"Yeast-derived recombinant ovalbumin as a tool for studying antigen presentation in dendritic cells"*

**作者**: Lee H, et al.

**摘要**: 通过毕赤酵母系统表达重组OVA蛋白,并验证其与哺乳动物来源OVA的结构和功能相似性。研究表明,酵母表达的OVA可有效被树突状细胞摄取并提呈,为感染或肿瘤免疫研究提供了标准化抗原工具。

3. **文献名称**: *"Comparative analysis of recombinant ovalbumin produced in different expression systems for allergy research"*

**作者**: Zhang Y, et al.

**摘要**: 对比昆虫细胞、哺乳动物细胞及原核系统表达的重组OVA的翻译后修饰差异,发现糖基化模式显著影响OVA的过敏原性。结果为食物过敏模型中抗原选择提供了关键依据。

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如需实际文献,建议在PubMed或Web of Science中检索关键词:**"recombinant ovalbumin" + "expression" / "immune response" / "allergy"**。

背景信息

Ovalbumin (OVA), a glycoprotein comprising approximately 385 amino acids, is the predominant protein in egg white, accounting for 54–60% of its total protein content. As a member of the serpin (serine protease inhibitor) superfamily, OVA exhibits structural homology with protease inhibitors, though its primary biological role in eggs is nutrient storage for embryonic development. Its molecular weight is approximately 45 kDa, with a characteristic phosphorylated site and a single N-linked glycosylation site, contributing to its stability and solubility.

Recombinant OVA is produced using heterologous expression systems such as *E. coli*, yeast, insect, or mammalian cells. These systems enable scalable, animal-free production while retaining key immunological and biochemical properties of native OVA. Genetic engineering allows modifications, including epitope tagging, mutagenesis, or fusion with other proteins, to tailor OVA for specific research or therapeutic applications. For instance, recombinant OVA is widely utilized as a model antigen in immunology to study T-cell responses, vaccine efficacy, and immune tolerance due to its well-defined immunodominant epitopes (e.g., OVA257–264 for MHC-I presentation).

In biomedical research, recombinant OVA serves as a tool for drug delivery studies, allergenicity testing, and molecular chaperone investigations. Its low toxicity and high biocompatibility make it suitable for nanoparticle conjugation or as a carrier protein. Additionally, OVA-derived peptides are critical in cancer immunotherapy research, particularly in dendritic cell-based vaccines.

The shift to recombinant production addresses ethical and batch variability concerns associated with egg-derived OVA, ensuring reproducibility in experimental and clinical settings. Advances in expression systems continue to enhance yield and post-translational modification fidelity, solidifying recombinant OVA’s role as a versatile reagent in both basic science and translational applications.

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