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Recombinant Human SERPIND1 protein

  • 中文名: 丝氨蛋白酶抑制因子D1(SERPIND1)重组蛋白
  • 别    名: SERPIND1;HCF2;Heparin cofactor 2
货号: PA1000-2890
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点SERPIND1
Uniprot NoP05546
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间20-499aa
氨基酸序列GSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDW IPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHG KSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGL KGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLR SVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKL TKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNERE VVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTL EAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFD KNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRF TVDRPFLFLIYEHRTSCLLFMGRVANPSRS
预测分子量56 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SERPIND1重组蛋白的3篇参考文献示例(文献为模拟内容,仅供参考):

1. **标题**:*Recombinant Heparin Cofactor II (SERPIND1) Expression in E. coli and Functional Characterization*

**作者**:Li, X. et al.

**摘要**:研究通过大肠杆菌系统表达重组SERPIND1蛋白,优化纯化条件并验证其抑制凝血酶活性,证明其与天然HCII功能相似,为大规模生产提供方法。

2. **标题**:*Structural and Functional Analysis of Glycosylated SERPIND1 Produced in Mammalian Cells*

**作者**:Park, S. et al.

**摘要**:利用哺乳动物HEK293细胞表达糖基化重组SERPIND1.通过X射线晶体学解析结构,发现糖基化修饰影响其与肝素的结合能力,但对凝血酶抑制活性无显著影响。

3. **标题**:*Therapeutic Potential of Recombinant SERPIND1 in a Murine Thrombosis Model*

**作者**:Chen, R. et al.

**摘要**:在小鼠模型中评估重组SERPIND1的抗凝效果,结果显示其显著减少血栓形成,且未引起出血副作用,提示其作为新型抗凝药物的潜力。

4. **标题**:*High-Yield Purification of Recombinant SERPIND1 and Its Interaction with Heparan Sulfate*

**作者**:Gomez, M. et al.

**摘要**:开发了一种基于肝素亲和层析的高效纯化方法,获得高纯度重组SERPIND1.并揭示其与硫酸乙酰肝素的结合动力学,为机制研究提供工具。

(注:以上文献为示例,实际文献需通过PubMed或SciHub等平台检索。)

背景信息

SERPIND1. also known as Serpin Family D Member 1. encodes heparin cofactor II (HCII), a plasma glycoprotein that belongs to the serpin superfamily of serine protease inhibitors. Primarily synthesized in the liver, HCII plays a critical role in regulating blood coagulation by inactivating thrombin, a key enzyme in the clotting cascade. Unlike antithrombin III (another thrombin inhibitor), HCII specifically targets thrombin in a glycosaminoglycan-dependent manner, showing high affinity for dermatan sulfate or heparin. This interaction accelerates thrombin inhibition, providing a secondary anticoagulant mechanism that complements other pathways to prevent pathological thrombosis.

Recombinant SERPIND1 protein is produced using biotechnological methods, often expressed in mammalian cell systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, including glycosylation, which is essential for its biological activity. The recombinant form retains the functional domains of native HCII, particularly its reactive center loop that binds and neutralizes thrombin. Researchers utilize this protein to study thrombin-HCII interactions, investigate coagulation disorders linked to HCII deficiency, and explore therapeutic applications. For instance, recombinant HCII has been proposed as a potential treatment for patients with hereditary HCII deficiency or as an adjunct anticoagulant in specific clinical scenarios where heparin resistance occurs.

Recent studies also suggest HCII's involvement in vascular remodeling and inflammation, expanding its relevance beyond hemostasis. The development of recombinant SERPIND1 protein facilitates drug discovery and mechanistic studies, offering tools for diagnostic assays and targeted therapies in cardiovascular diseases. Ongoing research aims to optimize production yields and evaluate its efficacy in preclinical models, highlighting its dual significance in basic science and translational medicine.

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