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| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LEP |
| Uniprot No | P41159 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-167aa |
| 氨基酸序列 | VPIQKVQDDT KTLIKTIVTR INDISHTQSV SSKQKVTGLD FIPGLHPILT LSKMDQTLAV YQQILTSMPS RNVIQISNDL ENLRDLLHVL AFSKSCHLPW ASGLETLDSL GGVLEASGYS TEVVALSRLQ GSLQDMLWQL DLSPGC |
| 预测分子量 | 16.0 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LEP(瘦素)重组蛋白的模拟参考文献示例(注：内容为虚构，仅供参考格式)：
1. **"High-yield expression and purification of recombinant human Leptin in *Escherichia coli*"**
- 作者：Zhang, Y., et al.
- 摘要：研究通过大肠杆菌表达系统高效生产重组人瘦素蛋白，优化诱导条件并采用亲和层析纯化，验证其生物活性。
2. **"Structural and functional characterization of mammalian cell-derived recombinant LEP"**
- 作者：Smith, J.R., & Lee, T.
- 摘要：利用CHO细胞表达重组LEP，通过质谱和圆二色谱分析其结构，证明其与瘦素受体结合能力与天然蛋白一致。
3. **"Therapeutic potential of recombinant Leptin in obesity models"**
- 作者：Johnson, M., et al.
- 摘要：在小鼠肥胖模型中评估重组LEP的疗效，结果显示其显著降低体重并改善代谢指标，提示临床转化潜力。
4. **"Comparative analysis of yeast and bacterial systems for LEP production"**
- 作者：Brown, K., et al.
- 摘要：对比毕赤酵母和大肠杆菌表达重组LEP的产量、糖基化差异及生物活性，探讨不同系统的优劣。
(注：以上文献为示例，实际引用需检索PubMed、Web of Science等数据库获取真实研究。)
The LEP (Leptin) recombinant protein is a biologically engineered form of leptin, a hormone predominantly secreted by adipose tissue. Discovered in 1994. leptin plays a critical role in regulating energy homeostasis by signaling satiety to the hypothalamus, thereby modulating appetite and metabolic rate. Its name derives from the Greek "leptos" (thin), reflecting its association with body weight regulation. The recombinant LEP protein is produced using genetic engineering techniques, typically through expression systems like *E. coli* or mammalian cell cultures, ensuring high purity and consistency for research and therapeutic applications.
Leptin deficiency, linked to mutations in the *LEP* gene, causes severe early-onset obesity and metabolic disorders. Recombinant leptin (metreleptin) has been developed as a replacement therapy for such cases, demonstrating efficacy in normalizing hunger signaling and improving metabolic parameters. Beyond congenital deficiencies, leptin is implicated in broader metabolic research, including obesity, diabetes, and immune regulation. However, most obesity cases involve leptin resistance rather than deficiency, limiting therapeutic utility in general populations.
Research on LEP recombinant protein also explores its role in reproductive health, bone metabolism, and immune responses, given leptin's pleiotropic effects. Challenges persist in optimizing delivery methods and overcoming resistance mechanisms. Current studies focus on leptin analogs, combination therapies, and nanoparticle-based delivery systems to enhance bioavailability. As a tool in molecular biology, recombinant leptin enables mechanistic studies of signaling pathways, offering insights into metabolic diseases and potential interventions. Its development underscores the intersection of genetic engineering and translational medicine in addressing complex endocrine disorders.
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