| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIFR |
| Uniprot No | P42702 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 45-833aa |
| 氨基酸序列 | QKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLE KTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNL SADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTL NGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNI SWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDG ENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETH DLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQ LLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDI NSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLV ALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWRE WSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKA EIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGIL LTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPG IRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKW EDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQK TLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENS |
| 预测分子量 | 116 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LIFR重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*Structural basis of leukemia inhibitory factor receptor signaling revealed by cryo-EM*
**作者**：Huyton, T., et al.
**摘要**：该研究通过冷冻电镜技术解析了LIFR与gp130受体复合物的三维结构，揭示了LIFR在结合配体LIF后如何激活下游JAK-STAT信号通路的分子机制，为靶向LIFR的疾病治疗提供结构基础。
2. **文献名称**：*LIFR regulates tumor metastasis through transcriptional activation of autophagy*
**作者**：Luo, S., et al.
**摘要**：研究发现LIFR重组蛋白通过调控自噬相关基因的转录抑制乳腺癌转移，并证明LIFR缺失会导致自噬异常激活，促进肿瘤细胞侵袭，提示LIFR可能作为癌症治疗的潜在靶点。
3. **文献名称**：*Recombinant LIFR-Fc fusion protein enhances pluripotency maintenance in human embryonic stem cells*
**作者**：Williams, R., et al.
**摘要**：该文献报道了一种LIFR-Fc重组融合蛋白的开发，证实其可通过稳定激活STAT3信号通路有效维持人胚胎干细胞的多能性，为干细胞体外培养提供了新型无血清培养基质方案。
注：以上文献信息为示例性质，具体研究请以实际发表的论文内容为准。建议通过PubMed或Web of Science检索关键词“LIFR recombinant protein”获取最新文献。
LIFR (Leukemia Inhibitory Factor Receptor) is a transmembrane glycoprotein that belongs to the class I cytokine receptor family. It plays a critical role in mediating cellular signaling pathways, particularly through its interaction with leukemia inhibitory factor (LIF), ciliary neurotrophic factor (CNTF), cardiotrophin-1 (CT-1), and other interleukin-6 (IL-6) family cytokines. Structurally, LIFR forms heterodimeric complexes with gp130. a common signal-transducing subunit, to activate downstream JAK/STAT, MAPK, and PI3K/AKT pathways. These pathways regulate diverse biological processes, including embryonic development, hematopoiesis, neuroprotection, and stem cell maintenance.
Recombinant LIFR proteins are engineered using expression systems (e.g., bacterial, mammalian, or insect cells) to produce soluble forms of the receptor for research and therapeutic applications. These proteins retain ligand-binding capabilities, enabling studies on cytokine-receptor interactions and signal modulation. In research, recombinant LIFR is utilized to investigate its dual role in cancer—acting as both a tumor suppressor (via differentiation promotion) and a potential oncogenic driver in certain contexts. It also serves as a tool to explore regenerative medicine strategies, particularly in maintaining pluripotency in stem cells.
Therapeutic interest in LIFR focuses on targeting its signaling in diseases like leukemia, muscle atrophy, and neurodegenerative disorders. However, challenges include optimizing protein stability, avoiding off-target effects, and mimicking native post-translational modifications. Advances in protein engineering, such as Fc-fusion constructs or site-specific mutagenesis, aim to enhance bioavailability and functional specificity. Ongoing studies continue to unravel LIFR's context-dependent signaling mechanisms, driving innovation in biologics design and precision medicine approaches.
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