| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hamp |
| Uniprot No | P81172 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 60-84aa |
| 氨基酸序列 | DTHFPICIFCCGCCHRSKCGMCCKT |
| 预测分子量 | 29.5 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HAMP结构域重组蛋白的3篇示例文献(注：文献为示例性质，实际引用需核实数据库):
1. **标题**: *Structural modeling of the HAMP domain-mediated signal transduction mechanism*
**作者**: Dunin-Horkawicz S, et al.
**摘要**: 研究HAMP结构域在跨膜信号传导中的构象变化机制，通过重组表达和分子动力学模拟，揭示其螺旋间相互作用对下游激酶活性的调控作用。
2. **标题**: *Functional characterization of a recombinant HAMP domain from bacterial histidine kinase*
**作者**: Appleman JA, et al.
**摘要**: 在大肠杆菌中重组表达并纯化细菌组氨酸激酶的HAMP结构域，通过圆二色谱和等温滴定量热法分析其与调控蛋白的结合特性，证实其在信号传递中的核心作用。
3. **标题**: *Engineered HAMP domains as modular switches in synthetic transmembrane signaling pathways*
**作者**: Swain KE, et al.
**摘要**: 开发基于重组HAMP结构域的合成生物学元件，通过定向进化改造获得可调控的跨膜信号开关，为人工信号通路设计提供新工具。
4. **标题**: *Crystal structure of a recombinant archaeal HAMP domain reveals conserved helical packing*
**作者**: Park SY, et al.
**摘要**: 解析古菌来源重组HAMP结构域的晶体结构(2.1Å)，发现其螺旋束的保守折叠模式，为理解HAMP家族蛋白的进化关系提供结构依据。
**建议**：可通过PubMed或Google Scholar以关键词"HAMP domain recombinant"+"expression/structure/engineering"检索最新文献，重点关注《Journal of Molecular Biology》《Protein Science》等期刊的相关研究。
**Background of hAMP Recombinant Proteins**
Human antimicrobial peptides (hAMPs), also known as host defense peptides, are small, cationic molecules integral to the innate immune system. They exhibit broad-spectrum activity against bacteria, fungi, viruses, and even cancer cells. Naturally produced by epithelial cells and immune cells, hAMPs act by disrupting microbial membranes or modulating immune responses. However, their low natural abundance and structural complexity limit large-scale extraction for therapeutic use.
Recombinant protein technology emerged as a solution, enabling scalable production of hAMPs. Using genetic engineering, hAMP genes are inserted into expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to synthesize these peptides in vitro. This approach overcomes challenges like low yield and high cost associated with chemical synthesis. Advances in codon optimization, fusion tags, and purification methods have enhanced solubility and bioactivity of recombinant hAMPs.
Research on hAMP recombinant proteins focuses on combating antibiotic resistance, as they offer mechanisms distinct from traditional antibiotics. Their immunomodulatory properties—such as promoting wound healing or neutralizing endotoxins—further broaden therapeutic potential. However, hurdles remain, including protease susceptibility in vivo and potential cytotoxicity. Ongoing studies aim to engineer stabilized analogs and targeted delivery systems.
In summary, recombinant hAMPs represent a promising frontier in antimicrobial therapy, merging natural defense mechanisms with biotechnological innovation to address global health challenges.
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