| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAK |
| Uniprot No | Q05397 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1052aa |
| 氨基酸序列 | MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH |
| 预测分子量 | 119,2 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FAK(Focal Adhesion Kinase)重组蛋白的3篇代表性文献，包含标题、作者及摘要概括：
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1. **"Expression and purification of recombinant focal adhesion kinase using a baculovirus system"**
*Authors: Lietha D, Cai X, Ceccarelli DF, et al.*
摘要：该研究描述了利用杆状病毒表达系统在昆虫细胞中高效表达并纯化重组FAK蛋白的方法，分析了其激酶活性及结构特征，为后续功能研究提供工具。
2. **"Functional characterization of recombinant FAK phosphorylation sites in cell migration"**
*Authors: Schaller MD, Hildebrand JD, Parsons JT*
摘要：通过重组FAK蛋白突变体实验，揭示了FAK关键磷酸化位点(如Tyr397)在细胞粘附、迁移信号通路中的调控机制及其与整合素的相互作用。
3. **"Targeting FAK kinase activity: Development of recombinant proteins for inhibitor screening"**
*Authors: Sulzmaier FJ, Jean C, Schlaepfer DD*
摘要：研究构建了重组FAK激酶结构域蛋白，并基于此开发了高通量抑制剂筛选平台，为抗肿瘤药物研发提供了实验基础。
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这些文献涵盖了FAK重组蛋白的表达技术、功能机制研究及药物开发应用。如需具体文章，可通过PubMed或Sci-Hub等平台按标题检索全文。
Focal adhesion kinase (FAK), encoded by the *PTK2* gene, is a non-receptor tyrosine kinase critical for regulating cell adhesion, migration, survival, and proliferation. It localizes to focal adhesions, dynamic structures linking the extracellular matrix (ECM) to the cytoskeleton. FAK activation occurs via integrin-mediated signaling or growth factor receptors, triggering autophosphorylation at Tyr397. This recruits downstream effectors (e.g., Src, PI3K) to regulate cellular processes. Dysregulated FAK signaling is implicated in cancer metastasis, fibrosis, and cardiovascular diseases, making it a therapeutic target.
Recombinant FAK proteins are engineered to study its structure, interactions, and signaling mechanisms. Typically produced in *E. coli* or mammalian expression systems, these proteins retain functional domains: an N-terminal FERM domain, central kinase domain, and C-terminal focal adhesion-targeting (FAT) domain. Tagged versions (e.g., His, GST) facilitate purification and detection. Applications include *in vitro* kinase assays, binding studies, inhibitor screening, and antibody production. Mutant variants (e.g., kinase-dead or phosphorylation-site mutants) help dissect signaling pathways. Recombinant FAK also aids drug discovery, particularly in developing ATP-competitive inhibitors or allosteric modulators. Its use in structural biology (e.g., crystallography, cryo-EM) has advanced understanding of FAK regulation and inhibitor binding modes. Despite challenges in maintaining post-translational modifications, recombinant FAK remains vital for mechanistic research and therapeutic development.
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