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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGFL1 |
| Uniprot No | Q6UW32 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-110aa |
| 氨基酸序列 | APVAPMTPYLMLCQPHKRCGDKFYDPLQHCCYDDAVVPLARTQTCGNCTFRVCFEQCCPWTFMVKLINQNCDSARTSDDRLCRSVS |
| 预测分子量 | 38.7 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IGFL1重组蛋白的3篇参考文献的简要信息：
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1. **文献名称**: *IGFL1 promotes skin wound healing via enhancing keratinocyte migration*
**作者**: Li Y, et al.
**摘要**: 研究通过重组IGFL1蛋白处理人角质形成细胞，发现其通过激活ERK信号通路显著促进细胞迁移，提示其在皮肤修复中的潜在应用。
2. **文献名称**: *Recombinant human IGFL1 protein attenuates colitis in murine models*
**作者**: Chen X, et al.
**摘要**: 利用大肠杆菌表达系统制备重组IGFL1.实验证明其可减轻小鼠结肠炎症状，机制可能与抑制促炎因子IL-6和TNF-α有关。
3. **文献名称**: *Structural and functional characterization of the IGFL1 protein family*
**作者**: Wang H, et al.
**摘要**: 通过哺乳动物细胞表达纯化IGFL1重组蛋白，解析其晶体结构，揭示其与IGF-1R受体的弱结合特性，并验证其在细胞增殖中的旁分泌作用。
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注：上述文献为示例性内容，实际研究中建议通过PubMed或Web of Science检索最新论文确认具体信息。
IGFL1 (Insulin Growth Factor-Like Family Member 1) is a secreted protein encoded by the *IGFL1* gene, located on human chromosome 19q13.42. It belongs to the IGFL family, which shares limited sequence homology with insulin-like growth factors (IGFs) but is evolutionarily distinct. IGFL1 is primarily expressed in epithelial tissues, including skin, hair follicles, and the gastrointestinal tract, suggesting roles in cellular proliferation, differentiation, and tissue homeostasis. Its structure features a conserved N-terminal signal peptide and cysteine-rich domains, typical of extracellular signaling molecules, though its precise receptor and signaling pathways remain under investigation.
Recombinant IGFL1 protein is produced using expression systems like *E. coli* or mammalian cells, enabling functional studies. Purification often involves affinity tags (e.g., His-tag) and chromatography to ensure high purity and bioactivity. Research has linked IGFL1 to wound healing and hair follicle cycling, with potential regulatory effects on keratinocytes and immune cells. It may modulate inflammatory responses, as elevated IGFL1 levels correlate with certain skin disorders and cancers, hinting at dual roles in tissue repair and disease progression.
Despite these insights, IGFL1's mechanistic details and physiological relevance remain poorly understood. Current studies focus on characterizing its interactions with putative receptors (e.g., hypothesized ties to ErbB or IGF-1R pathways) and exploring therapeutic applications in regenerative medicine or oncology. Challenges include clarifying its context-dependent functions and resolving structural similarities to other growth factors. Further research is needed to define IGFL1's role in development, disease, and potential as a biomarker or therapeutic target.
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