| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRC |
| Uniprot No | P12931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-536aa |
| 氨基酸序列 | MHHHHHHGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASA DGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYD YESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSD SIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDF DNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRL TTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTR VAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYM SKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAAN ILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTI KSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESL HDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL |
| 预测分子量 | 61 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3篇关于SRC重组蛋白的关键文献摘要，涵盖结构、功能及技术应用：
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1. **文献名称**：*Structure of the amino-terminal domain of Csk complexed with an SH3 domain of Src*
**作者**：Xu, W., Harrison, S.C., & Eck, M.J.
**摘要**：该研究通过X射线晶体学解析了SRC蛋白SH3结构域与Csk激酶的复合物结构，揭示了SRC激酶活性调控的分子机制，为设计靶向SRC的抑制剂提供了结构基础。
2. **文献名称**：*Expression and purification of active Src tyrosine kinase in Escherichia coli*
**作者**：Porter, M., Schindler, T., & Kuriyan, J.
**摘要**：报道了利用大肠杆菌重组表达系统高效制备活性SRC激酶的方法，优化了蛋白可溶性和磷酸化修饰条件，为体外酶学及药物筛选研究提供可靠技术方案。
3. **文献名称**：*Targeting Src signaling in metastatic bone disease*
**作者**：Ishizawar, R., & Parsons, S.J.
**摘要**：综述了SRC在肿瘤转移(尤其骨转移)中的信号通路作用，强调重组SRC蛋白在筛选小分子抑制剂及验证靶点中的应用，并讨论其临床转化潜力。
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**提示**：若需具体实验技术文献(如重组表达纯化)，可进一步补充关键词(如"recombinant expression")。
**Background of SRC Recombinant Proteins**
The SRC family of non-receptor tyrosine kinases plays a pivotal role in cellular signaling, regulating processes such as cell proliferation, differentiation, survival, and motility. Among these, the **SRC proto-oncogene** (c-SRC) is a well-studied member, initially identified as the cellular counterpart of v-SRC, the oncogene of the Rous sarcoma virus. SRC proteins are characterized by modular domains, including SH2 and SH3 domains for protein-protein interactions and a catalytic kinase domain. Dysregulation of SRC activity, often due to mutations or overexpression, is implicated in cancer progression, metastasis, and resistance to therapies, making it a critical therapeutic target.
Recombinant SRC proteins are engineered using genetic cloning techniques, typically expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., insect or mammalian cells) to ensure proper post-translational modifications, such as phosphorylation. These proteins retain functional kinase activity and structural integrity, enabling researchers to study SRC’s biochemical properties, substrate interactions, and inhibition mechanisms in controlled environments.
The development of SRC recombinant proteins has accelerated drug discovery, particularly in designing tyrosine kinase inhibitors (e.g., dasatinib) for cancers. They are also vital tools for structural studies (e.g., X-ray crystallography) to map active sites and allosteric regulatory regions. Additionally, recombinant SRC facilitates high-throughput screening for novel inhibitors and elucidates signaling crosstalk in pathways like EGFR, integrin, and immune receptor signaling.
Despite advancements, challenges remain in mimicking native SRC regulation, as its activity is tightly controlled by phosphorylation (e.g., inhibitory phosphorylation at Tyr530) and interactions with regulatory proteins (e.g., CSK). Ongoing research focuses on optimizing recombinant SRC variants to better reflect physiological conditions, aiding the development of precision therapies for SRC-driven malignancies.
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