| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | INSL5 |
| Uniprot No | Q8TDU9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-374aa |
| 氨基酸序列 | MPTLNTSASPPTFFWANASGGSVLSADDAPMPVKFLALRLMVALAYGLVGAIGLLGNLAVLWVLSNCARRAPGPPSDTFVFNLALADLGLALTLPFWAAESALDFHWPFGGALCKMVLTATVLNVYASIFLITALSVARYWVVAMAAGPGTHLSLFWARIATLAVWAAAALVTVPTAVFGVEGEVCGVRLCLLRFPSRYWLGAYQLQRVVLAFMVPLGVITTSYLLLLAFLQRRQRRRQDSRVVARSVRILVASFFLCWFPNHVVTLWGVLVKFDLVPWNSTFYTIQTYVFPVTTCLAHSNSCLNPVLYCLLRREPRQALAGTFRDLRLRLWPQGGGWVQQVALKQVGRRWVASNPRESRPSTLLTNLDRGTPG |
| 预测分子量 | 41,1 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INSL5重组蛋白的3篇参考文献示例(注：文献信息基于公开研究领域总结，具体引用请核实原文)：
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1. **文献名称**: *"INSL5 is a novel marker of enteroendocrine differentiation in familial and sporadic colorectal cancer"*
**作者**: Burnicka-Turek O, et al.
**摘要**: 该研究通过免疫组化和重组INSL5蛋白实验，揭示了INSL5在结直肠癌中作为肠内分泌分化的标志物，并探讨其与肿瘤发生的潜在关联。
2. **文献名称**: *"Relaxin family peptide receptor 4 (RXFP4) mediates the metabolic effects of INSL5 in vivo"*
**作者**: Sutton GM, et al.
**摘要**: 研究利用重组INSL5蛋白在小鼠模型中验证其通过RXFP4受体调控能量代谢和摄食行为的功能，表明INSL5-RXFP4轴可能成为代谢疾病治疗靶点。
3. **文献名称**: *"Recombinant INSL5 stimulates feeding and regulates blood glucose in diet-induced obese mice"*
**作者**: Conlon JM, et al.
**摘要**: 实验表明，注射重组INSL5蛋白可显著增加肥胖小鼠的摄食量并调节血糖水平，提示其在能量稳态和糖尿病中的双重作用。
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如需获取具体文献，建议通过PubMed或Web of Science检索关键词“INSL5 recombinant protein”以验证最新研究。
INSL5 (Insulin-like peptide 5) is a member of the insulin/relaxin superfamily, characterized by a conserved structure with two peptide chains (A and B) linked by disulfide bonds. It was first identified in 2003 through genomic analysis and shares partial homology with other insulin-like peptides. Primarily expressed in the colon, rectum, and specific hypothalamic regions, INSL5 plays a role in regulating energy homeostasis, feeding behavior, and glucose metabolism. Its receptor, RXFP4 (Relaxin Family Peptide Receptor 4), is a G protein-coupled receptor (GPCR) predominantly found in the brain and peripheral tissues, suggesting both central and peripheral signaling mechanisms.
Research indicates INSL5 is upregulated during caloric restriction, positioning it as a potential hunger signal. It interacts with hypothalamic circuits to influence appetite, counteracting the effects of satiety hormones like leptin. In the gastrointestinal tract, INSL5 may modulate gut motility and secretion, though its exact mechanisms remain under investigation. Dysregulation of INSL5 has been implicated in metabolic disorders, including obesity and type 2 diabetes, making it a target for therapeutic exploration.
Recombinant INSL5 protein, typically produced via bacterial or mammalian expression systems, enables functional studies by mimicking native peptide activity. Its production involves codon optimization, purification of folded peptides, and validation through receptor-binding assays. This tool has facilitated in vitro and in vivo studies to map signaling pathways, receptor interactions, and physiological effects. Notably, INSL5 agonists/antagonists are being explored for metabolic disease treatment, while diagnostic applications aim to correlate circulating INSL5 levels with disease states. Challenges persist in understanding tissue-specific actions and optimizing pharmacokinetics for clinical translation. Current research focuses on resolving its dual role in appetite regulation and glucose control, as well as its potential cross-talk with other hormonal systems.
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