| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UA |
| Uniprot No | Q13838 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-251aa |
| 氨基酸序列 | AENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFV |
| 预测分子量 | 55.2kDa |
| 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. |
以下是关于重组尿激酶型纤溶酶原激活剂(uPA)的3篇参考文献及其摘要概括：
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1. **文献名称**：*Expression and characterization of recombinant urokinase-type plasminogen activator (uPA) in E. coli*
**作者**：Smith A, et al.
**摘要**：研究通过大肠杆菌系统高效表达重组uPA蛋白，优化表达条件后获得高活性酶，验证其体外纤溶功能及潜在溶栓治疗应用。
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2. **文献名称**：*High-yield production of recombinant uPA in CHO cells and its antitumor effects in vitro*
**作者**：Zhang L, et al.
**摘要**：利用CHO细胞稳定表达重组uPA，建立规模化生产工艺，证实其通过调控细胞外基质降解抑制肿瘤细胞侵袭转移的能力。
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3. **文献名称**：*A novel purification strategy for recombinant uPA with enhanced thrombolytic activity*
**作者**：Johnson R, et al.
**摘要**：开发基于亲和层析与分子筛的新型纯化方法，显著提高重组uPA纯度，动物实验显示其溶栓效率优于传统制剂。
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(注：以上文献为示例，实际引用时需以真实发表的论文为准。)
**Background of Recombinant UA Protein**
Recombinant UA protein, commonly referring to urate oxidase (UOX) or uricase, is a genetically engineered enzyme designed to catalyze the conversion of uric acid into allantoin, a more soluble and easily excreted compound. Naturally produced in some mammals (e.g., rodents), humans lack functional uricase due to evolutionary gene silencing, leading to the accumulation of uric acid, which is associated with hyperuricemia, gout, and tumor lysis syndrome.
The development of recombinant UA protein emerged to address clinical needs for effective uric acid management. Early versions, such as Rasburicase (derived from *Aspergillus flavus*), were among the first FDA-approved recombinant uricases, offering superior efficacy over traditional therapies like allopurinol. However, immunogenicity and short half-life limited their use. Advances in protein engineering, including PEGylation (e.g., Pegloticase) and fusion technologies, have since improved stability, reduced immunogenicity, and extended circulatory half-life, enhancing therapeutic outcomes.
Recombinant UA proteins are typically produced using microbial (e.g., *E. coli*, yeast) or mammalian expression systems, ensuring high purity and scalable manufacturing. Beyond therapeutics, they find applications in diagnostics and bioremediation, such as degrading uric acid in industrial waste.
Research continues to optimize UA protein variants for broader clinical use, including chronic kidney disease and cardiovascular disorders linked to hyperuricemia. Additionally, studies explore its role in mitigating oxidative stress, as uric acid degradation reduces reactive oxygen species production.
In summary, recombinant UA protein represents a critical innovation in biotechnology, bridging a metabolic gap in humans and offering versatile solutions for healthcare and environmental challenges. Ongoing advancements aim to refine its efficacy, safety, and applicability across diverse fields.
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