| 纯度 | >90%SDS-PAGE. |
| 种属 | E.Coli |
| 靶点 | sak |
| Uniprot No | P15240 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-163aa |
| 氨基酸序列 | SSSFDKGKYK KGDDASYFEP TGPYLMVNVT GVDGKRNELL SPRYVEFPIK PGTTLTKEKI EYYVEWALDA TAYKEFRVVE LDPSAKIEVT YYDKNKKKEE TKSFPITEKG FVVPDLSEHI KNPGFNLITK VVIEKK |
| 预测分子量 | 15.6 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. |
以下为3条关于sak(链激酶)重组蛋白的参考文献示例：
1. **《High-level expression and purification of recombinant streptokinase in Escherichia coli》**
- 作者：Zhang et al.
- 摘要：研究通过优化大肠杆菌表达系统，实现链激酶的高效表达与纯化，产物具有显著溶栓活性，为大规模生产提供方案。
2. **《Characterization of a novel sak mutant with enhanced fibrinolytic activity in a murine thrombosis model》**
- 作者：Wang & Li
- 摘要：通过定点突变技术改造sak蛋白，获得溶栓活性增强的突变体，并在小鼠模型中验证其优于野生型的血栓溶解效果。
3. **《Expression of recombinant streptokinase in Pichia pastoris and its interaction with plasminogen》**
- 作者：Chen et al.
- 摘要：利用毕赤酵母系统表达重组链激酶，分析其与纤溶酶原的相互作用机制，证明其结构稳定性与潜在临床应用价值。
(注：以上为模拟文献，实际引用需以具体论文数据为准。)
Staphylokinase (SAK), a fibrin-specific plasminogen activator, is a promising thrombolytic agent originally derived from *Staphylococcus aureus*. Discovered in the mid-20th century, SAK works by forming a 1:1 complex with plasminogen, converting it into plasmin—an enzyme that degrades fibrin clots. Unlike streptokinase, SAK exhibits higher clot specificity, reducing systemic bleeding risks. However, native SAK from pathogenic *S. aureus* raised safety concerns, prompting the development of recombinant SAK (rSAK) through genetic engineering.
Recombinant SAK is produced using non-pathogenic expression systems like *E. coli* or yeast, ensuring purity and eliminating bacterial toxin risks. Its 136-amino-acid structure lacks cysteine residues, simplifying refolding and enhancing stability. Studies show rSAK retains fibrinolytic efficacy while inducing minimal immunogenicity compared to native SAK. Preclinical and clinical trials highlight its potential in treating acute myocardial infarction, ischemic stroke, and pulmonary embolism, with faster clot lysis and lower reocclusion rates than older thrombolytics.
Research continues to optimize rSAK variants through protein engineering. PEGylation and fusion proteins aim to prolong its short plasma half-life (~6 minutes). Mutagenesis studies focus on reducing antibody neutralization in patients with pre-existing anti-SAK immunity. As a cost-effective alternative to tissue plasminogen activator (tPA), rSAK holds promise for global thrombolytic therapy, particularly in resource-limited settings. Ongoing efforts address production scalability and long-term safety to facilitate clinical translation.
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