| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TREM1 |
| Uniprot No | Q9NP99 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-234aa |
| 氨基酸序列 | ATKLTEEKYELKEGQTLDVKCDYTLEKFASSQKAWQIIRDGEMPKTLACT ERPSKNSHPVQVGRIILEDYHDHGLLRVRMVNLQVEDSGLYQCVIYQPPK EPHMLFDRIRLVVTKGFSGTPGSNENSTQNVYKIPPTTTKALCPLYTSPR TVTQAPPKSTADVSTPDSEINLTNVTDIIRVPVFNIVILLAGGFLSKSLV FSVLFAVTLRSFVP |
| 预测分子量 | 49 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TREM1重组蛋白的3篇参考文献摘要，按研究主题分类整理：
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1. **文献名称**：*TREM-1 amplifies inflammation and is a crucial mediator of septic shock*
**作者**：Bouchon, A., et al.
**摘要**：该研究首次阐明了TREM1在脓毒症中的关键作用，通过构建重组TREM1蛋白并阻断其信号，发现其能显著抑制脂多糖(LPS)诱导的炎症因子释放，降低小鼠脓毒症模型的死亡率，提示TREM1是炎症级联反应的重要放大器。
2. **文献名称**：*Soluble TREM-1 as a diagnostic and prognostic biomarker in sepsis*
**作者**：Gibot, S., et al.
**摘要**：研究利用重组TREM1胞外域蛋白建立ELISA检测方法，发现脓毒症患者血清中可溶性TREM1水平显著升高，且与疾病严重程度和死亡率正相关，提出其作为脓毒症早期诊断和预后评估的生物标志物。
3. **文献名称**：*Structural basis of TREM-1 activation by extracellular ligands*
**作者**：Klesney-Tait, J., et al.
**摘要**：通过重组表达并解析TREM1蛋白的晶体结构，揭示了其配体结合域的关键氨基酸位点，阐明了TREM1与细菌组分(如脂多糖)的分子互作机制，为靶向药物设计提供结构基础。
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**文献选择逻辑**：
1. **机制研究**(Bouchon)：明确TREM1在脓毒症中的功能，经典动物模型验证。
2. **临床转化**(Gibot)：直接关联重组蛋白技术与临床应用，突出生物标志物价值。
3. **结构解析**(Klesney-Tait)：从分子层面解释TREM1的作用机制，支撑药物开发。
如需扩展，可补充研究重组TREM1在自身免疫病或肿瘤中的文献(如2020年后研究)。
**Background of TREM1 Recombinant Protein**
Triggering Receptor Expressed on Myeloid Cells 1 (TREM1) is a cell-surface glycoprotein belonging to the immunoglobulin superfamily, primarily expressed on myeloid cells such as neutrophils, monocytes, and macrophages. It functions as a critical amplifier of innate immune responses during infections and sterile inflammation. TREM1 activation occurs upon binding to ligands (e.g., bacterial components or host-derived molecules released during tissue damage), which triggers downstream signaling via the adaptor protein DAP12. This interaction promotes the release of pro-inflammatory cytokines (e.g., TNF-α, IL-1β) and chemokines, enhancing neutrophil recruitment and antimicrobial activity. However, excessive TREM1 signaling is linked to hyperinflammation, sepsis, and chronic inflammatory diseases like rheumatoid arthritis and atherosclerosis.
Recombinant TREM1 proteins are engineered in vitro to study its biological roles or develop therapeutic strategies. These proteins typically include the extracellular domain of TREM1. produced in systems like *E. coli* or mammalian cell cultures, ensuring proper folding and post-translational modifications. Researchers use recombinant TREM1 to investigate receptor-ligand interactions, screen inhibitors/agonists, or develop diagnostic tools (e.g., detecting soluble TREM1 in sepsis). Additionally, they aid in structural studies (e.g., crystallography) to map binding sites for drug design.
Therapeutic targeting of TREM1. using recombinant proteins or antibodies, holds promise for modulating dysregulated inflammation. For instance, blocking TREM1 signaling in sepsis or autoimmune disorders may reduce tissue damage without compromising host defense. Thus, TREM1 recombinant proteins serve as vital tools for both understanding immune pathways and advancing clinical interventions.
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