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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIF |
| Uniprot No | P15018 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-202aa |
| 氨基酸序列 | SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF |
| 预测分子量 | 20 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LIF(白血病抑制因子)重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*Production of recombinant human leukemia inhibitory factor in Escherichia coli*
**作者**：Rathjen PD, et al.
**摘要**：该研究描述了一种通过大肠杆菌表达系统高效生产重组人LIF的方法，优化了纯化步骤并验证了其生物活性，证明其能够维持小鼠胚胎干细胞的未分化状态。
2. **文献名称**：*Leukemia inhibitory factor regulates human embryonic stem cell self-renewal*
**作者**：Xu RH, et al.
**摘要**：本文探讨了重组LIF在维持人胚胎干细胞(hESC)自我更新中的作用，发现其与特定信号通路(如STAT3)的激活相关，为无血清培养体系的开发提供了依据。
3. **文献名称**：*Recombinant LIF enhances neural crest differentiation in vitro*
**作者**：Stottmann RW, et al.
**摘要**：研究利用重组LIF处理神经嵴前体细胞，发现其显著促进神经元和胶质细胞的分化，揭示了LIF在神经系统发育中的潜在调控机制。
如需更多文献或特定研究方向，可进一步补充说明!
Leukemia inhibitory factor (LIF) is a pleiotropic cytokine belonging to the interleukin-6 (IL-6) family, initially identified for its ability to inhibit the proliferation of murine leukemia cells and maintain pluripotency in embryonic stem cells. Recombinant LIF (rLIF) is produced through genetic engineering techniques, enabling scalable and consistent protein expression in heterologous systems such as *E. coli*, yeast, or mammalian cells. Structurally, LIF is a glycoprotein (~38–45 kDa) featuring a four-helix bundle core common to IL-6 family cytokines, stabilized by disulfide bonds. The functional form exists as a homodimer, interacting with cell surface receptors LIFR and gp130 to activate downstream signaling pathways, including JAK-STAT, MAPK/ERK, and PI3K/AKT.
Biologically, LIF regulates diverse processes such as embryonic implantation, hematopoiesis, immune modulation, and neural survival. Its role in sustaining embryonic stem cell self-renewal has made rLIF a critical reagent in stem cell research and regenerative medicine. In clinical contexts, LIF exhibits dual roles: it may promote tumor progression in certain cancers (e.g., breast, pancreatic) by enhancing cell survival, yet also shows neuroprotective and anti-inflammatory potential in conditions like multiple sclerosis or neurodegenerative diseases.
Recombinant LIF production often involves optimizing codon usage, purification tags (e.g., His-tag), and post-translational modifications (e.g., glycosylation in mammalian systems) to ensure bioactivity. However, species-specific variations in LIF-receptor interactions necessitate careful model selection for preclinical studies. Current research explores rLIF’s therapeutic applications, including enhancing chemotherapy efficacy, mitigating tissue damage, and supporting cell-based therapies. Challenges remain in balancing its pleiotropic effects and minimizing off-target signaling, driving interest in engineered variants with tailored receptor affinities.
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