| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LEAP2 |
| Uniprot No | Q969E1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 38-77aa |
| 氨基酸序列 | MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSLSVAQE |
| 预测分子量 | 36.1 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LEAP2重组蛋白的3篇代表性文献(信息基于公开研究总结，非真实引用，仅供参考)：
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1. **标题**：*"Production and Characterization of Recombinant Human LEAP2 in Escherichia coli"*
**作者**：Zhang Y et al.
**摘要**：本研究报道了在大肠杆菌系统中高效表达重组人源LEAP2的方法，通过优化密码子和诱导条件提高可溶性蛋白产量。纯化的LEAP2经质谱和圆二色谱验证结构正确性，并证实其能抑制ghrelin受体(GHSR1a)的活性，提示其在代谢疾病治疗中的潜力。
2. **标题**：*"Structural Insights into LEAP2-Ghrelin Receptor Interaction by Cryo-EM"*
**作者**：Wang L et al.
**摘要**：利用冷冻电镜解析重组LEAP2蛋白与ghrelin受体(GHSR1a)的复合物结构，揭示了LEAP2通过特定疏水残基阻断ghrelin信号传导的分子机制，为开发肥胖相关疾病的靶向药物提供结构基础。
3. **标题**：*"Recombinant LEAP2 Attenuates Hepatic Steatosis in Diet-Induced Obese Mice"*
**作者**：Chen H et al.
**摘要**：通过哺乳动物细胞表达系统制备重组LEAP2.证明其能有效改善高脂饮食小鼠的胰岛素抵抗和肝脏脂质积累，机制涉及AMPK/mTOR通路调控，提示LEAP2在代谢综合征中的治疗价值。
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**备注**：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science检索真实论文(关键词：LEAP2. recombinant, ghrelin receptor, metabolic regulation)。
LEAP2 (Liver Expressed Antimicrobial Peptide 2) is a small, cysteine-rich protein initially identified for its antimicrobial properties. It was discovered in 2003 as part of the LEAP family, which includes the iron-regulatory hormone hepcidin (LEAP1). Encoded by the *LEAP2* gene in humans, this peptide is predominantly synthesized in the liver and gastrointestinal tract. While early studies highlighted its role in innate immunity against pathogens, subsequent research revealed broader physiological functions, particularly in metabolic regulation.
Structurally, LEAP2 consists of a conserved N-terminal signal peptide and a mature domain stabilized by disulfide bonds. Its interaction with the ghrelin receptor (GHSR), a key player in appetite and energy homeostasis, has positioned LEAP2 as a critical modulator of metabolic signaling. LEAP2 antagonizes ghrelin, the "hunger hormone," thereby suppressing appetite and influencing glucose metabolism. This interplay has implications for obesity, diabetes, and cachexia, sparking interest in therapeutic applications.
Recombinant LEAP2 is produced using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling scalable synthesis for research and drug development. Its stability and specificity make it a valuable tool for studying GHSR signaling and metabolic pathways. Preclinical studies suggest potential in treating metabolic disorders, infections, and inflammation, though clinical validation is ongoing.
Beyond metabolism, LEAP2's antimicrobial activity against bacteria, fungi, and parasites underscores its dual role in immunity and homeostasis. However, its primary significance lies in bridging metabolic and immune regulation, offering a multifaceted target for translational research. As understanding of its mechanisms deepens, recombinant LEAP2 continues to serve as both a biological probe and a promising candidate for novel therapies.
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