| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ORM2 |
| Uniprot No | P19652 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-201aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMQIPLCANLVPVPITNATLDRITGKW FYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQNQCFYN SSYLNVQRENGTVSRYEGGREHVAHLLFLRDTKTLMFGSYLDDEKNWGLS FYADKPETTKEQLGEFYEALDCLCIPRSDVMYTDWKKDKCEPLEKQHEKE RKQEEGES |
| 预测分子量 | 24 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. |
以下是3条关于ORM2重组蛋白的假设性参考文献示例(注：文献为虚构，仅作格式参考)：
1. **《重组人ORM2蛋白在大肠杆菌中的高效表达及纯化》**
- 作者：Zhang L, et al.
- 摘要：本研究通过优化密码子及诱导条件，在大肠杆菌中成功表达可溶性人ORM2重组蛋白，并利用镍柱亲和层析纯化，获得高纯度蛋白用于后续功能研究。
2. **《ORM2的结构解析及其与免疫调控因子的相互作用》**
- 作者：Wang Y, et al.
- 摘要：通过X射线晶体学解析了重组ORM2蛋白的三维结构，揭示其糖基化位点对结合炎症相关细胞因子(如IL-6)的关键作用，为靶向药物设计提供依据。
3. **《重组ORM2在急性炎症模型中的抗凋亡功能研究》**
- 作者：Kim S, et al.
- 摘要：利用哺乳动物细胞表达系统制备重组ORM2.证实其通过抑制线粒体途径凋亡减轻小鼠急性肝损伤，提示其作为潜在治疗分子的价值。
(注：实际文献需通过PubMed、Web of Science等平台检索关键词“ORM2 recombinant protein”或“Orosomucoid 2 expression”获取。)
**Background of ORM2 Recombinant Protein**
Orosomucoid 2 (ORM2), also known as alpha-1-acid glycoprotein 2. is a member of the acute-phase protein family predominantly synthesized in the liver. It plays a critical role in modulating immune responses and maintaining homeostasis during inflammation. Structurally, ORM2 is characterized by its high carbohydrate content and membership in the immunocalin family, which enables interactions with small hydrophobic molecules, immune cells, and pathogens. Its expression is sharply upregulated during acute-phase reactions triggered by infection, trauma, or stress, mediated by pro-inflammatory cytokines like IL-6 and IL-1β.
Functionally, ORM2 exhibits immunosuppressive and anti-inflammatory properties. It regulates neutrophil activation, inhibits apoptosis in immune cells, and binds to drugs or toxins, altering their pharmacokinetics. Emerging studies suggest its involvement in metabolic disorders, cancer progression, and autoimmune diseases, highlighting its dual role as both a protective agent and a potential disease biomarker.
Recombinant ORM2 protein is produced using genetic engineering techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. This engineered protein retains the biological activity of native ORM2. enabling *in vitro* and *in vivo* studies to dissect its mechanisms in inflammation, drug metabolism, and cellular signaling. Researchers leverage recombinant ORM2 to explore its therapeutic potential, such as mitigating excessive inflammation or enhancing drug delivery efficiency.
Despite its promise, challenges remain in understanding context-dependent roles, particularly its glycosylation-dependent functions and interactions with pathogens. Ongoing research aims to clarify these aspects, positioning ORM2 as a versatile tool for both basic science and clinical applications.
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