| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | LCN13 |
| Uniprot No | Q8K1H9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-176aa |
| 氨基酸序列 | MKSLLLTILLLGLVAVLKAQEAPPDDLVDYSGIWYAKAMVHNGTLPSHKIPSIVFPVRIIALEEGDLETTVVFWNNGHCREFKFVMKKTEEPGKYTAFHNTKVIHVEKTSVNEHYIFYCEGRHNGTSSFGMGKLMGRDSGENPEAMEEFKNFIKRMNLRLENMFVPEIGDKCVESD |
| 预测分子量 | 19,9 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LCN13重组蛋白的模拟参考文献(实际文献需通过学术数据库核实)：
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1. **《重组LCN13蛋白在精子成熟中的功能研究》**
Zhang Y. et al. (2018)
摘要：本研究通过大肠杆菌表达系统成功纯化重组LCN13蛋白，并发现其在体外能够结合胆固醇，可能参与调节哺乳动物精子膜的脂质代谢与功能成熟。
2. **《LCN13重组蛋白对代谢综合征小鼠模型的影响》**
Chen L. et al. (2020)
摘要：利用昆虫细胞体系表达重组LCN13蛋白，验证其通过调节脂肪酸代谢改善高脂饮食小鼠的胰岛素抵抗，提示其潜在代谢调控作用。
3. **《LCN13蛋白的晶体结构与配体结合特性分析》**
Singh R. & Kumar S. (2019)
摘要：解析了重组LCN13蛋白的晶体结构，揭示其脂质结合口袋的关键氨基酸残基，为设计靶向小分子药物提供结构基础。
4. **《重组LCN13在生殖医学中的潜在应用》**
Wang X. et al. (2021)
摘要：研究发现重组LCN13蛋白可增强人类精子活力，并通过体外实验证明其可能通过调控氧化应激通路保护生殖细胞。
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**注意**：以上内容为模拟生成，实际文献需通过PubMed、Web of Science或Google Scholar等平台以关键词“LCN13 recombinant protein”“Lipocalin 13 expression”等检索。若研究较少，可扩大关键词范围(如“lipocalin family”或“reproductive protein engineering”)。
**Background of LCN13 Recombinant Protein**
LCN13 (Lipocalin 13) is a member of the lipocalin protein family, characterized by a conserved eight-stranded β-barrel structure that facilitates the binding and transport of small hydrophobic molecules, such as lipids, steroids, and retinoids. This family plays roles in diverse physiological processes, including immune regulation, cell signaling, and metabolic homeostasis. LCN13. specifically, has garnered attention for its potential involvement in energy metabolism and obesity-related pathways. Studies suggest it may interact with cell surface receptors or circulating factors to modulate adipose tissue function or systemic glucose/lipid metabolism, though its precise mechanisms remain under investigation.
Recombinant LCN13 protein is produced using genetic engineering techniques, typically through expression in bacterial (e.g., *E. coli*) or mammalian cell systems, followed by purification to ensure high specificity and bioactivity. This engineered protein retains the functional domains of native LCN13. enabling researchers to study its structure-function relationships, ligand-binding properties, and therapeutic potential in preclinical models.
Interest in LCN13 stems from its association with metabolic disorders. Animal studies indicate that LCN13 overexpression or administration improves insulin sensitivity, reduces adiposity, and mitigates diet-induced obesity, positioning it as a candidate for metabolic disease therapeutics. Additionally, its role in inflammation and cellular stress responses suggests broader applications in conditions like diabetes, non-alcoholic fatty liver disease (NAFLD), and cardiovascular disorders.
Despite promising findings, challenges persist in elucidating LCN13’s endogenous ligands, signaling pathways, and tissue-specific effects. Further research is needed to validate its clinical relevance and optimize recombinant production for therapeutic scalability. Current work focuses on unraveling its molecular interactions and exploring engineered variants for enhanced stability or targeting capabilities.
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