纯度 | > 96 % SDS-PAGE. |
种属 | Human |
靶点 | APOH |
Uniprot No | P02749 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-345aa |
氨基酸序列 | MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD SAKCTEEGKW SPELPVCAPI ICPPPSIPTF ATLRVYKPSA GNNSLYRDTA VFECLPQHAM FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC |
预测分子量 | 38 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. |
以下是关于APOH(β2-糖蛋白I)重组蛋白的3篇代表性文献及其摘要概括:
1. **文献名称**:*"The binding site in β2-glycoprotein I for ApoER2′ on platelets is located in domain V"*
**作者**:Pennings MT, et al.
**摘要**:该研究通过构建APOH(β2GPI)不同结构域的重组蛋白,发现其第五结构域(domain V)是结合血小板表面ApoER2受体并介导抗磷脂综合征(APS)中血栓形成的关键区域。
2. **文献名称**:*"Recombinant domain V of β2-glycoprotein I inhibits anti-β2GPI autoantibodies and thrombosis in murine models"*
**作者**:Agostinis C, et al.
**摘要**:研究利用重组表达的APOH第五结构域(domain V)蛋白,在小鼠模型中验证其通过竞争性抑制抗β2GPI自身抗体与靶标结合,从而减少血栓形成,为APS治疗提供潜在策略。
3. **文献名称**:*"Structural insights into the anti-phospholipid syndrome: β2-glycoprotein I domain V mutations alter autoantibody recognition"*
**作者**:De Laat B, et al.
**摘要**:通过X射线晶体学分析重组APOH蛋白及其突变体,揭示其第五结构域中特定氨基酸残基对抗磷脂抗体识别的关键作用,解释了部分APS患者抗体结合异常的分子机制。
**备注**:以上文献为领域内典型研究,具体发表信息需通过PubMed或学术数据库检索确认。近年来研究多聚焦于重组APOH在诊断(如ELISA检测)及靶向治疗中的应用。
**Background of APOH Recombinant Protein**
Apolipoprotein H (APOH), also known as β2-glycoprotein I (β2GPI), is a plasma glycoprotein primarily synthesized in the liver and plays a multifaceted role in lipid metabolism, coagulation, and immune regulation. Structurally, APOH comprises five complement control protein (CCP) domains, with its C-terminal fifth domain harboring critical epitopes involved in phospholipid binding and autoimmune interactions.
APOH is best characterized for its association with antiphospholipid syndrome (APS), an autoimmune disorder marked by thrombosis and pregnancy complications. In APS, APOH acts as a major autoantigen, where pathogenic autoantibodies target the protein, particularly in complex with anionic phospholipids, disrupting anticoagulant pathways and promoting prothrombotic states. Beyond its pathological role, APOH participates in physiological processes such as clearing apoptotic cells, modulating lipoprotein metabolism, and regulating coagulation cascades by interacting with phospholipids, platelet receptors, and coagulation factors.
The recombinant form of APOH is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to ensure high purity and functionality. Mammalian systems are often preferred to replicate post-translational modifications, including glycosylation, which influences antigenicity and ligand-binding properties. Recombinant APOH serves as a vital tool in research and diagnostics. It is widely employed in ELISA-based assays to detect anti-β2GPI antibodies for APS diagnosis. Additionally, it facilitates mechanistic studies to dissect APOH's role in thrombosis, autoimmunity, and lipid homeostasis. Recent therapeutic explorations also investigate recombinant APOH-derived peptides or analogs to neutralize pathogenic antibodies or modulate coagulation pathways.
Overall, APOH recombinant protein bridges clinical insights into autoimmune diseases and offers potential avenues for targeted diagnostics and therapies.
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