| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERPINB12 |
| Uniprot No | Q96P63 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-425aa |
| 氨基酸序列 | MDSLVTANTKFCFDLFQEIGKDDRHKNIFFSPLSLSAALGMVRLGARSDSAHQIDEVLHF NEFSQNESKEPDPCLKSNKQKVLADSSLEGQKKTTEPLDQQAGSLNNESGLVSCYFGQLL SKLDRIKTDYTLSIANRLYGEQEFPICQEYLDGVIQFYHTTIESVDFQKNPEKSRQEINF WVECQSQGKIKELFSKDAINAETVLVLVNAVYFKAKWETYFDHENTVDAPFCLNANENKS VKMMTQKGLYRIGFIEEVKAQILEMRYTKGKLSMFVLLPSHSKDNLKGLEELERKITYEK MVAWSSSENMSEESVVLSFPRFTLEDSYDLNSILQDMGITDIFDETRADLTGISPSPNLY LSKIIHKTFVEVDENGTQAAAATGAVVSERSLRSWVEFNANHPFLFFIRHNKTQTILFYG RVCSP |
| 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. |
以下是关于SERPINB12重组蛋白的3篇参考文献(示例基于领域常见研究方向，具体文献需根据实际数据库查询验证)：
1. **文献名称**：*"SERPINB12 inhibits human neutrophil elastase and regulates skin barrier function"*
**作者**：Zhang Y, et al.
**摘要**：研究通过重组SERPINB12蛋白证实其能够抑制中性粒细胞弹性蛋白酶活性，并揭示其在维持表皮屏障功能中的作用。
2. **文献名称**：*"Recombinant SERPINB12 suppresses viral protease activity and modulates host antiviral responses"*
**作者**：Li X, et al.
**摘要**：该文献报道利用大肠杆菌表达系统纯化重组SERPINB12.证明其通过抑制特定病毒蛋白酶活性(如冠状病毒3CL蛋白酶)发挥潜在抗病毒效应。
3. **文献名称**：*"Structural and functional characterization of SERPINB12 as a tumor-associated serpin"*
**作者**：Wang H, et al.
**摘要**：通过重组蛋白晶体结构分析，揭示了SERPINB12与靶标蛋白酶相互作用的分子机制，并发现其在多种癌症中异常表达，可能影响肿瘤转移。
4. **文献名称**：*"Optimization of SERPINB12 recombinant protein production in mammalian cells for therapeutic screening"*
**作者**：Chen L, et al.
**摘要**：研究优化了哺乳动物细胞中SERPINB12重组蛋白的表达与纯化工艺，并验证其在体外模型中对炎症相关蛋白酶的抑制活性，为药物开发提供基础。
**注意**：以上文献为示例性概括，实际引用需以真实发表的论文为准。建议通过PubMed、Google Scholar等平台用关键词“SERPINB12 recombinant”检索最新研究。
SERPINB12 is a member of the serine protease inhibitor (serpin) superfamily, which plays critical roles in regulating proteolytic pathways involved in diverse biological processes, including blood coagulation, inflammation, and cellular homeostasis. As part of the clade B serpins, SERPINB12 is primarily intracellular and expressed in epithelial tissues, such as the skin, respiratory tract, and gastrointestinal system. Its exact physiological function remains incompletely understood, though studies suggest potential involvement in inhibiting trypsin-like serine proteases to maintain tissue integrity or modulate immune responses. Unlike some serpins with well-characterized targets (e.g., SERPINB1 in neutrophil elastase inhibition), SERPINB12’s specificity and mechanisms are less defined, prompting ongoing research to elucidate its biological relevance.
Recombinant SERPINB12 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for functional and structural studies. The recombinant form retains the conserved serpin architecture, featuring a reactive center loop (RCL) critical for protease interaction. Researchers utilize this protein to investigate its inhibitory kinetics, structural stability, and potential binding partners through techniques such as crystallography, enzyme assays, and proteomics. Its recombinant expression also facilitates exploration of its role in disease contexts, including cancer, inflammatory disorders, or genetic serpinopathies, where dysregulated protease activity contributes to pathogenesis.
Despite progress, challenges persist in clarifying SERPINB12’s precise physiological role and therapeutic potential. Some studies propose anti-inflammatory or antimicrobial functions, while others link its variants to skin barrier defects or esophageal squamous cell carcinoma. Recombinant SERPINB12 serves as a vital tool to resolve these ambiguities, offering insights into serpin biology and paving the way for applications in biomarker discovery or targeted therapies. Ongoing work aims to define its protease targets, regulatory networks, and relevance in human health, underscoring its emerging significance in both basic and translational research.
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