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Recombinant Human APOM protein

  • 中文名: 载脂蛋白M(APOM)重组蛋白
  • 别    名: APOM;G3A;NG20;Apolipoprotein M
货号: PA1000-200DB
Price: ¥询价
数量:
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产品详情

纯度> 90 % SDS-PAGE.
种属Human
靶点APOM
Uniprot NoO95445
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间23-188aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN
预测分子量21 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

以下是关于APOM(载脂蛋白M)重组蛋白研究的3-4条参考文献的示例(注:以下文献为模拟示例,具体内容需根据实际文献调整):

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1. **文献名称**: *"Recombinant human apolipoprotein M exerts anti-inflammatory effects via regulating HDL function"*

**作者**: Xu N, et al.

**摘要**: 本研究成功通过大肠杆菌表达系统制备了重组人源APOM蛋白,并验证其与高密度脂蛋白(HDL)的结合能力。实验表明,重组APOM可通过增强HDL的抗炎活性抑制内皮细胞炎症反应,提示其在动脉粥样硬化治疗中的潜在应用价值。

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2. **文献名称**: *"Structural and functional characterization of recombinant apolipoprotein M–S1P complex"*

**作者**: Christoffersen C, et al.

**摘要**: 通过哺乳动物细胞表达体系获得重组APOM蛋白,并解析其与鞘氨醇-1-磷酸(S1P)的复合物结构。研究发现APOM通过疏水口袋结合S1P,并证实该复合物在调节血管内皮细胞迁移和血管生成中的关键作用。

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3. **文献名称**: *"Apolipoprotein M overexpression prevents atherosclerosis in murine models"*

**作者**: Zhang Y, et al.

**摘要**: 利用腺病毒载体在ApoE敲除小鼠中过表达重组APOM,结果显示APOM显著减少动脉粥样硬化斑块形成。机制研究表明,APOM通过促进胆固醇逆向转运和抑制巨噬细胞炎症反应发挥作用。

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4. **文献名称**: *"Efficient production of bioactive recombinant apolipoprotein M in Pichia pastoris"*

**作者**: Liu X, et al.

**摘要**: 报道了一种在毕赤酵母系统中高效表达重组APOM的优化方法,获得的蛋白具有天然构象和生物活性。研究还评估了重组APOM在体外促进胆固醇外流的能力,为其规模化生产提供了技术基础。

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如需具体文献,建议通过PubMed、Web of Science等数据库检索关键词 **"apolipoprotein M recombinant"** 或 **"ApoM expression and function"** 获取最新研究。

背景信息

**Background of APOM Recombinant Protein**

Apolipoprotein M (APOM) is a lipid-binding protein predominantly associated with high-density lipoprotein (HDL) particles, playing a critical role in lipid metabolism and vascular homeostasis. It is a member of the lipocalin protein family, characterized by its ability to transport small hydrophobic molecules. APOM is synthesized primarily in the liver and kidneys and is known to bind sphingosine-1-phosphate (S1P), a bioactive lipid involved in endothelial cell function, inflammation regulation, and cardiovascular protection.

The interest in APOM stems from its dual role in lipid transport and cellular signaling. Studies suggest that APOM modulates HDL functionality, influencing cholesterol efflux and anti-atherogenic properties. Additionally, its interaction with S1P highlights its potential in maintaining endothelial barrier integrity and mitigating inflammatory responses. Dysregulation of APOM has been linked to metabolic disorders, including atherosclerosis, diabetes, and chronic kidney disease, making it a promising biomarker and therapeutic target.

Recombinant APOM protein is engineered using biotechnological platforms, such as *E. coli* or mammalian expression systems, to ensure proper folding and post-translational modifications. This recombinant form retains the native protein’s bioactivity, enabling researchers to study its structural and functional properties in vitro and in vivo. Applications include elucidating APOM-S1P signaling pathways, developing diagnostic assays, and exploring therapeutic strategies for cardiovascular and metabolic diseases.

Recent advancements in protein engineering and HDL-targeted therapies have further amplified the relevance of APOM recombinant protein in preclinical and clinical research, offering insights into personalized medicine approaches for complex lipid-associated pathologies.

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