| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | CYS4 |
| Uniprot No | P32582 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MTKSEQQADSRHNVIDLVGNTPLIALKKLPKALGIKPQIYAKLELYNPGGSIKDRIAKSMVEEAEASGRIHPSRSTLIEPTSGNTGIGLALIGAIKGYRTIITLPEKMSNEKVSVLKALGAEIIRTPTAAAWDSPESHIGVAKKLEKEIPGAVILDQYNNMMNPEAHYFGTGREIQRQLEDLNLFDNLRAVVAGAGTGGTISGISKYLKEQNDKIQIVGADPFGSILAQPENLNKTDITDYKVEGIGYDFVPQVLDRKLIDVWYKTDDKPSFKYARQLISNEGVLVGGSSGSAFTAVVKYCEDHPELTEDDVIVAIFPDSIRSYLTKFVDDEWLKKNNLWDDDVL |
| 预测分子量 | 42.0 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CYS4重组蛋白的假设参考文献示例(注：文献为虚构，仅供格式参考)：
1. **《Heterologous Expression of Saccharomyces cerevisiae CYS4 in Escherichia coli for Serine O-Acetyltransferase Activity Analysis》**
- 作者：Smith, J. et al.
- 摘要：研究通过在大肠杆菌中重组表达酿酒酵母CYS4蛋白，优化表达条件并纯化，验证其丝氨酸乙酰转移酶活性，为半胱氨酸合成途径的酶学研究提供基础。
2. **《Crystal Structure of Recombinant CYS4 from Saccharomyces cerevisiae: Insights into Substrate Binding Mechanisms》**
- 作者：Zhang, L. et al.
- 摘要：解析重组CYS4蛋白的晶体结构，揭示其底物结合位点及催化机制，为设计半胱氨酸代谢调控分子提供结构依据。
3. **《Metabolic Engineering of Yeast Using Recombinant CYS4 to Enhance Cysteine Biosynthesis》**
- 作者：Lee, H. et al.
- 摘要：通过过表达重组CYS4蛋白改造酵母代谢网络，显著提高半胱氨酸产量，探讨其在工业发酵中的应用潜力。
4. **《Optimization of Recombinant CYS4 Protein Purification and Stability for Biotechnological Applications》**
- 作者：Jones, R. et al.
- 摘要：开发高效重组CYS4蛋白纯化流程，评估其在不同条件下的稳定性，为酶制剂开发提供技术参考。
(注：实际文献需通过学术数据库检索确认。)
CYS4 recombinant protein is a genetically engineered form of the cystathionine beta-lyase (CβL) enzyme, originally derived from the yeast *Saccharomyces cerevisiae*. This enzyme plays a critical role in the **cysteine biosynthesis pathway**, specifically catalyzing the cleavage of cystathionine to produce cysteine, α-ketobutyrate, and ammonia. In yeast, CYS4 is essential for sulfur metabolism, linking methionine degradation to cysteine production, which is vital for cellular processes like protein synthesis, redox homeostasis, and antioxidant defense (e.g., glutathione production).
The recombinant CYS4 protein is typically expressed in heterologous systems such as *E. coli* or insect cells, enabling large-scale production for research and industrial applications. Its structure includes a pyridoxal 5'-phosphate (PLP) cofactor-binding domain, characteristic of enzymes in the **fold type I** PLP-dependent family. Researchers often study CYS4 to explore sulfur amino acid metabolism, enzyme kinetics, and potential therapeutic targets in diseases linked to cysteine dysregulation, such as **homocystinuria** or oxidative stress-related disorders.
In biotechnology, CYS4 is utilized to engineer microbial strains for enhanced cysteine production, which has commercial relevance in pharmaceuticals, food additives, and nutraceuticals. Additionally, its role in hydrogen sulfide (H₂S) generation—via alternative substrate reactions—has sparked interest in studying H₂S as a signaling molecule in cardiovascular and neurological systems.
Overall, CYS4 recombinant protein serves as a valuable tool for both basic research in metabolic pathways and applied biotechnological innovations.
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