| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Cys |
| Uniprot No | P13500 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-99aa |
| 氨基酸序列 | QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT |
| 预测分子量 | 13.7 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. |
1. **"Engineering Cysteine Residues for Site-Specific Protein Labeling" by Smith et al.**
该文献提出了一种通过定点突变在重组蛋白中引入半胱氨酸残基的方法，用于实现蛋白质的特异性化学偶联或荧光标记，优化了标记效率与稳定性。
2. **"Structural Insights into Cys-Rich Recombinant Proteins: Implications for Folding and Stability" by Lee & Chen**
研究通过X射线晶体学分析富含半胱氨酸的重组蛋白(如硫氧还蛋白家族)的二硫键网络，揭示了其折叠机制及对热稳定性的影响。
3. **"Cysteine-Specific PEGylation of Therapeutic Proteins to Prolong Circulation Half-Life" by Zhang et al.**
探讨利用重组蛋白表面的游离半胱氨酸进行位点特异性聚乙二醇(PEG)修饰，减少免疫原性并延长药物半衰期，应用于生物制药开发。
4. **"Role of Disulfide Bond Engineering in Enhancing Recombinant Protein Production in E. coli" by Kim et al.**
通过优化重组蛋白(如抗体片段)中的半胱氨酸配对和二硫键形成策略，显著提高其在大肠杆菌表达系统中的可溶性和产量。
Cysteine-engineered recombinant proteins, often referred to as Cys-tagged or Cys-modified proteins, represent a specialized class of biotechnologically engineered proteins designed for enhanced functionality. These proteins are generated through genetic engineering by introducing cysteine residues at specific sites within the protein structure. Cysteine, a sulfur-containing amino acid, is unique due to its thiol (-SH) group, which enables covalent modifications, site-specific conjugation, or controlled crosslinking. This feature is particularly valuable in applications requiring precise protein labeling, immobilization, or functionalization, such as drug delivery systems, diagnostic assays, and targeted therapeutics.
The development of Cys-engineered proteins emerged from the need to overcome limitations in traditional protein modification methods, which often lacked specificity or disrupted protein activity. By strategically inserting cysteine residues into non-critical regions (e.g., surface-exposed loops or termini), researchers preserve the native folding and biological activity while creating "chemical handles" for bioconjugation. This approach has been widely adopted in antibody-drug conjugates (ADCs), where cytotoxic agents are attached to cysteine residues in monoclonal antibodies, improving therapeutic precision.
Challenges in Cys-protein engineering include maintaining structural stability (as unintended disulfide bonds may form) and ensuring conjugation efficiency. Advances in structural biology, computational modeling, and expression systems (e.g., Escherichia coli, mammalian cells) have optimized cysteine placement and minimized aggregation. Furthermore, technologies like site-directed mutagenesis and redox-controlled folding systems enhance production consistency.
Cys-modified proteins now underpin innovations across biopharma, including next-generation ADCs, biosensors, and enzyme engineering. Their customizable nature continues to expand their utility in both research and industrial applications, balancing functional versatility with biological fidelity.
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