| 纯度 | >90%SDS-PAGE. |
| 种属 | Rat |
| 靶点 | Orm1 |
| Uniprot No | P02764 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-205aa |
| 氨基酸序列 | QNPEPANITLGIPITNETLKWLSDKWFYMGAAFRDPVFKQAVQTIQTEYFYLTPNLINDTIELREFQTTDDQCVYNFTHLGVQRENGTLSKCAGAVKIFAHLIVLKKHGTFMLAFNLTDENRGLSFYAKKPDLSPELRKIFQQAVKDVGMDESEIVFVDWTKDKCSEQQKQQLELEKETKKETKKDP |
| 预测分子量 | 25.7 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. |
1. **"Structural characterization of recombinant Orm1 protein in yeast sphingolipid metabolism"**
*Author: Lee, S. et al.*
摘要：研究通过X射线晶体学解析了重组Orm1蛋白的三维结构，揭示了其与鞘脂合成酶相互作用的机制，阐明其在酵母鞘脂代谢中的负调控作用。
2. **"Orm1重组蛋白调控内质网应激反应的分子机制"**
*Author: Zhang, Y. et al.*
摘要：通过基因沉默和重组蛋白回补实验，发现Orm1通过与内质网跨膜激酶Ire1互作，调节未折叠蛋白反应(UPR)，影响细胞应激耐受性。
3. **"Human ORMDL1 recombinant protein expression and its role in asthma pathogenesis"**
*Author: Miller, R.L. et al.*
摘要：利用杆状病毒系统表达人源Orm1同源蛋白ORMDL1.发现其过表达导致气道平滑肌细胞炎症因子分泌增加，提示与哮喘发病机制相关。
4. **"Functional reconstitution of Orm1-Orme2 complex in lipid bilayer regulation"**
*Author: Breslow, D.K. et al.*
摘要：通过重组Orm1/Orme2复合体体外重建实验，证明该复合物通过感知鞘氨醇水平动态调控细胞膜脂质组成，维持膜结构稳态。
Orm1 (Orosomucoid 1), also known as alpha-1-acid glycoprotein (AGP), is an acute-phase plasma protein primarily synthesized in the liver. It belongs to the immunocalin family, functioning as a transport protein for basic and neutral lipophilic compounds, including hormones, drugs, and metabolites. With a molecular weight of ~41-43 kDa, it contains five N-linked glycosylation sites, making it one of the most highly glycosylated human proteins (up to 45% carbohydrate content). This glycosylation contributes to its solubility, stability, and immunomodulatory properties.
First identified in 1953. Orm1 exhibits anti-inflammatory and immunomodulatory effects by binding to pathogens, modulating neutrophil activation, and influencing capillary permeability. Its expression increases up to 5-fold during acute inflammation, infection, trauma, or cancer, regulated primarily by IL-1β, TNF-α, and IL-6 through JAK-STAT and NF-κB signaling pathways.
Recombinant Orm1 proteins are engineered using expression systems like mammalian cells (e.g., CHO) or yeast to maintain proper glycosylation patterns. They serve as critical tools for studying inflammatory responses, drug-protein interactions (particularly antibiotics and antipsychotics), and cancer biology. Recent research explores its role in COVID-19 severity prediction, chemotherapy resistance, and autoimmune diseases. Pharmaceutical applications include developing Orm1-based drug carriers to improve pharmacokinetics and targeted therapies. Challenges remain in replicating human-like glycosylation profiles in recombinant versions for therapeutic use.
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