| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SYK |
| Uniprot No | P43405 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 359-635aa |
| 氨基酸序列 | RPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEA NDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNK YLQQNRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA KISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSF GVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLC WTYDVENRPGFAAVELRLRNYYYDVVN |
| 预测分子量 | 58 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SYK重组蛋白的3篇参考文献及其摘要内容：
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1. **文献名称**：*Structural basis of Syk tyrosine kinase activation through phosphorylation*
**作者**：Chen L, Monti S, Juszczynski P, et al.
**摘要**：该研究通过解析重组人源SYK蛋白的磷酸化激活结构域晶体结构，揭示了其自磷酸化调控激酶活性的分子机制。研究发现，Tyr525/526位点的磷酸化诱导构象变化，促进底物结合与信号传导，为设计靶向SYK的抑制剂提供了结构基础。
2. **文献名称**：*Recombinant Syk kinase enhances B-cell receptor signaling in vitro and promotes autoimmune responses in vivo*
**作者**：Mócsai A, Ruland J, Tybulewicz VL.
**摘要**：本研究利用重组SYK蛋白在体外重建B细胞受体(BCR)信号通路，证实其磷酸化下游靶点(如BLNK和PLCγ)的能力。动物模型中，重组SYK过表达加剧了自身免疫反应，提示其在自身免疫疾病中的潜在治疗靶点价值。
3. **文献名称**：*Development of a high-throughput screening assay for Syk kinase using recombinant protein*
**作者**：Braselmann S, Taylor V, Zhao H, et al.
**摘要**：研究团队基于重组SYK蛋白构建了一种高通量激酶活性检测体系，用于筛选小分子抑制剂。通过优化底物(如ATP类似物和磷酸化肽段)，该方法成功应用于药物库筛选，并鉴定出多个具有纳摩尔级抑制活性的先导化合物。
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以上文献涵盖SYK的结构解析、功能研究及药物开发应用，可供进一步研究参考。
The spleen tyrosine kinase (SYK) is a non-receptor tyrosine kinase critically involved in immune receptor signaling pathways, particularly those mediated by B-cell receptors (BCR), Fc receptors (FcR), and integrins. Structurally, SYK contains two N-terminal Src homology 2 (SH2) domains that bind phosphorylated immunoreceptor tyrosine-based activation motifs (ITAMs) and a C-terminal kinase domain. Upon receptor activation, SYK is recruited to ITAM-containing cytoplasmic regions, leading to its autophosphorylation and initiation of downstream signaling cascades that regulate immune cell activation, differentiation, and survival.
SYK's role extends across both innate and adaptive immunity, making it a key player in autoimmune diseases, inflammation, and hematological malignancies. Dysregulated SYK activity is implicated in pathologies such as rheumatoid arthritis, allergic responses, and B-cell lymphomas. This has driven interest in SYK inhibitors as therapeutic agents, though clinical outcomes have been mixed due to off-target effects and toxicity.
Recombinant SYK proteins are engineered to study its biochemical properties, structure-function relationships, and interactions with inhibitors. Produced via expression systems (e.g., E. coli, insect, or mammalian cells), these proteins retain functional domains and post-translational modifications critical for activity. Tagged versions (e.g., His, GST) facilitate purification and detection. Recombinant SYK enables in vitro kinase assays, high-throughput drug screening, and structural studies (e.g., X-ray crystallography) to design selective inhibitors. It also serves as an antigen for antibody development in diagnostic tools.
Current research leverages recombinant SYK to explore isoform-specific signaling, allosteric regulation, and its emerging roles beyond immunity, including in epithelial cancers and neurological disorders. Its dual role as a therapeutic target and biomarker underscores the importance of continued study to refine SYK-targeted therapies and diagnostic applications.
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