| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERPINB9 |
| Uniprot No | P50453 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-376aa |
| 氨基酸序列 | METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP |
| 预测分子量 | 90.2 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SERPINB9重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Production of recombinant human serpin B9 (PI-9) and its functional characterization as a granzyme B inhibitor"*
**作者**：Annema, A., et al.
**摘要**：该研究报道了在哺乳动物表达系统中重组表达人源SERPINB9(PI-9)的方法，并验证其通过抑制颗粒酶B(granzyme B)活性保护细胞免受细胞毒性T细胞攻击的功能。
2. **文献名称**：*"Structural basis for serpin-mediated inhibition of granzyme B: Insights into the cytotoxic cell protease regulation"*
**作者**：Law, R.H.P., et al.
**摘要**：通过X射线晶体学解析了重组SERPINB9与颗粒酶B的复合物结构，揭示了SERPINB9通过构象变化不可逆抑制颗粒酶B的分子机制，为免疫逃逸机制研究提供结构基础。
3. **文献名称**：*"SERPINB9 (PI-9) protects cytotoxic lymphocytes from self-inflicted apoptosis by inhibiting granzyme B-mediated mitochondrial damage"*
**作者**：Bots, M., et al.
**摘要**：利用重组SERPINB9蛋白证明其通过抑制颗粒酶B活性，保护细胞毒性淋巴细胞免受自身颗粒酶B引发的线粒体凋亡通路激活，维持免疫细胞存活。
(注：以上文献信息为示例性质，实际引用时需核对具体文献的准确性及发表年份。)
SERPINB9. a member of the serine protease inhibitor (serpin) superfamily, plays a critical role in regulating proteolytic pathways involved in apoptosis, inflammation, and immune responses. It is specifically known for inhibiting granzyme B (GzmB), a protease released by cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells to induce target cell death. By neutralizing GzmB, SERPINB9 protects cells from unintended damage during immune surveillance, maintaining a balance between effective pathogen clearance and prevention of autoimmune tissue injury. This function highlights its importance in immune homeostasis and its potential link to diseases like cancer, autoimmune disorders, and chronic inflammation.
Recombinant SERPINB9 protein is produced using expression systems such as *E. coli* or mammalian cells, followed by purification to ensure biological activity. Its structure features a conserved serpin fold, characterized by three β-sheets and a reactive center loop (RCL) that interacts with target proteases. The RCL undergoes a conformational change upon protease binding, irreversibly inactivating the enzyme through a “suicide substrate” mechanism.
In research, recombinant SERPINB9 serves as a tool to study immune evasion mechanisms in tumors, which often overexpress this protein to resist CTL-mediated killing. It is also explored for therapeutic applications, such as mitigating GzmB-induced tissue damage in inflammatory diseases or improving the efficacy of immunotherapies. Additionally, it aids in developing diagnostic assays to monitor protease activity in pathological conditions. Studies using recombinant SERPINB9 have provided insights into its dual role—protecting healthy cells while potentially enabling tumor survival—making it a compelling target for drug development. Ongoing research aims to elucidate its broader interactions with proteases beyond GzmB and its regulatory effects on cell death pathways.
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