| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ILK |
| Uniprot No | Q13418 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-452aa |
| 氨基酸序列 | MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK |
| 预测分子量 | 54.8 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. |
以下为关于ILK重组蛋白的参考文献示例(内容基于领域内典型研究方向，非真实文献)：
1. **《重组整合素连接激酶(ILK)的分子克隆与功能表征》**
作者：Hannigan GE 等
摘要：本研究首次报道了人源ILK基因的克隆及其在大肠杆菌中的重组表达，证实重组ILK具有激酶活性，并参与整合素介导的细胞黏附信号通路调控。
2. **《重组ILK蛋白抑制肿瘤细胞迁移的机制研究》**
作者：Wu C 等
摘要：通过昆虫细胞系统表达并纯化重组ILK蛋白，发现其可通过竞争性结合胞内信号分子抑制多种癌细胞迁移，为靶向ILK的抗肿瘤治疗提供实验依据。
3. **《ILK与生长因子受体信号交叉调控的结构基础》**
作者：Troussard AA 等
摘要：利用重组ILK蛋白的晶体结构分析，揭示了其PH结构域与生长因子受体(如RTKs)的相互作用机制，阐明ILK在细胞增殖和存活中的双重调节作用。
4. **《基于His标签的重组ILK蛋白高效纯化方法开发》**
作者：Serrano I 等
摘要：优化了ILK重组蛋白在原核系统中的表达条件，建立镍柱亲和层析结合分子筛的纯化流程，获得高纯度及活性的ILK蛋白用于体外激酶活性检测。
注：以上文献名为示例性质，实际引用时建议通过学术数据库核实具体文献信息。
Integrin-Linked Kinase (ILK) is a multifunctional intracellular protein that plays a pivotal role in cell adhesion, signaling, and cytoskeletal organization. Discovered in the mid-1990s, ILK interacts directly with the cytoplasmic tails of β-integrins, serving as a critical bridge between extracellular matrix (ECM) components and intracellular signaling pathways. Structurally, ILK contains an N-terminal ankyrin repeat domain, a central pleckstrin homology (PH)-like domain, and a C-terminal kinase-like domain. Although initially classified as a serine/threonine kinase, its catalytic activity remains debated, with studies suggesting it may act as a pseudokinase or require co-factors for enzymatic function.
Recombinant ILK proteins are engineered using genetic engineering techniques to express and purify ILK in heterologous systems, such as *E. coli* or mammalian cell lines (e.g., HEK293). These proteins retain key functional domains, enabling researchers to study ILK’s interactions with binding partners (e.g., PINCH, PARVIN, and α/β-integrins) and its role in regulating downstream effectors like AKT, GSK-3β, and β-catenin. Recombinant ILK is widely used to investigate signaling pathways implicated in cell survival, proliferation, migration, and angiogenesis. Its dysregulation has been linked to pathologies such as cancer, fibrosis, and cardiovascular diseases, making it a potential therapeutic target.
Applications of recombinant ILK span *in vitro* assays, structural studies, and drug discovery. For example, it aids in elucidating mechanisms of tumor metastasis or testing inhibitors targeting ILK-mediated pathways. Production typically involves affinity chromatography (e.g., His-tag purification) followed by validation via SDS-PAGE, Western blot, or mass spectrometry. Despite challenges in maintaining native conformation during purification, recombinant ILK remains indispensable for advancing molecular and biomedical research, offering insights into cell-ECM crosstalk and opportunities for therapeutic intervention.
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