纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | SERPINA10 |
Uniprot No | Q9UK55 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 22-444aa |
氨基酸序列 | LAPSPQSPE TPAPQNQTSR VVQAPKEEEE DEQEASEEKA SEEEKAWLMA SRQQLAKETS NFGFSLLRKI SMRHDGNMVF SPFGMSLAMT GLMLGATGPT ETQIKRGLHL QALKPTKPGL LPSLFKGLRE TLSRNLELGL TQGSFAFIHK DFDVKETFFN LSKRYFDTEC VPMNFRNASQ AKRLMNHYIN KETRGKIPKL FDEINPETKL ILVDYILFKG KWLTPFDPVF TEVDTFHLDK YKTIKVPMMY GAGKFASTFD KNFRCHVLKL PYQGNATMLV VLMEKMGDHL ALEDYLTTDL VETWLRNMKT RNMEVFFPKF KLDQKYEMHE LLRQMGIRRI FSPFADLSEL SATGRNLQVS RVLQRTVIEV DERGTEAVAG ILSEITAYSM PPVIKVDRPF HFMIYEETSG MLLFLGRVVN PTLL |
预测分子量 | 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篇关于SERPINA10重组蛋白的参考文献示例(注:内容为模拟概括,实际文献需通过学术数据库验证):
1. **"Recombinant SERPINA10 inhibits thrombosis via regulating protein Z-dependent protease inhibition"**
*作者: Smith J, et al.*
摘要: 研究通过哺乳动物细胞表达系统制备重组SERPINA10蛋白,证实其通过结合蛋白Z增强抗凝血酶活性,抑制血栓形成,为血栓性疾病治疗提供新靶点。
2. **"Structural characterization of SERPINA10 and its interaction with coagulation factors"**
*作者: Chen L, et al.*
摘要: 利用X射线晶体学解析重组SERPINA10的三维结构,揭示其与凝血因子Xa的结合位点,阐明其通过构象变化抑制凝血级联反应的分子机制。
3. **"Aberrant SERPINA10 expression in ovarian cancer and its recombinant protein-based therapeutic potential"**
*作者: Wang Y, et al.*
摘要: 发现SERPINA10在卵巢癌组织中显著低表达,重组蛋白体外实验显示其可抑制肿瘤血管生成,提示其作为癌症生物标志物及治疗剂的潜力。
(提示:实际研究中建议通过PubMed或Google Scholar搜索最新文献,关键词可组合 "SERPINA10 recombinant"、"protein Z inhibitor" 或 "SERPINA10 structure/function")
SERPINA10. also known as protein Z-dependent protease inhibitor (ZPI), is a member of the serine protease inhibitor (serpin) superfamily, which plays critical roles in regulating proteolytic processes involved in coagulation, inflammation, and cellular homeostasis. Encoded by the *SERPINA10* gene, this glycoprotein is primarily synthesized in the liver and circulates in plasma. It functions as a anticoagulant by inhibiting activated factor XI (FXIa) and factor Xa (FXa) in a protein Z (PZ)-dependent manner, thereby modulating thrombin generation and preventing excessive blood clotting.
Structurally, SERPINA10 contains a reactive center loop (RCL) that interacts with target proteases, leading to irreversible inhibition through a conformational change. Recombinant SERPINA10 protein is produced using expression systems like mammalian cells (e.g., HEK293 or CHO cells) or *E. coli* to ensure proper folding and post-translational modifications. Its recombinant form retains functional activity, enabling studies on its mechanism, structure-function relationships, and potential therapeutic applications.
Research on SERPINA10 has linked it to thrombotic disorders, liver diseases, and cancer. For example, mutations or dysregulation of SERPINA10 are associated with venous thromboembolism (VTE) and hepatocellular carcinoma progression. Recombinant SERPINA10 is also explored as a biomarker for coagulation abnormalities or a candidate for antithrombotic drug development. Despite its established role in hemostasis, ongoing studies aim to clarify its interactions with other serpins, tissue-specific functions, and contributions to inflammatory or oncogenic pathways. Overall, SERPINA10 recombinant protein serves as a vital tool for dissecting its biological significance and translational potential in hematologic and metabolic diseases.
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