纯度 | >90%SDS-PAGE. |
种属 | Synechocystis sp |
靶点 | CysC |
Uniprot No | P72940 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-177aa |
氨基酸序列 | MQQRGVTIWL TGLSGAGKTT ITHALEKKLR DSGYRLEVLD GDVVRTNLTK GLGFSKEDRD TNIRRIGFVS HLLTRNGVIV LVSAISPYAA IRQEVKHTIG DFLEVFVNAP LAVCEERDVK GLYAKARSGE IKGFTGIDDP YEPPTNPDVE CRTDLEELDE SVGKIWQKLV DLKYIEG |
预测分子量 | 19,6 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. |
以下是关于Cystatin C(CysC)重组蛋白的3篇代表性文献概览(内容为模拟示例):
1. **《High-level expression and purification of recombinant human cystatin C in Escherichia coli》**
*作者:Zhang Y, et al.*
**摘要**:研究通过大肠杆菌表达系统高效生产重组人Cystatin C,优化了诱导条件和纯化工艺,利用亲和层析获得高纯度蛋白,并证实其抑制半胱氨酸蛋白酶活性,为大规模制备提供方案。
2. **《Functional characterization of recombinant cystatin C produced in mammalian cell systems》**
*作者:Smith J, et al.*
**摘要**:比较哺乳动物细胞(如CHO细胞)与原核系统表达的重组CysC差异,发现哺乳动物表达的蛋白具有正确糖基化修饰,且体外稳定性及蛋白酶抑制活性更接近天然形式,提示其在临床诊断中的应用潜力。
3. **《Cystatin C as a biomarker for early renal impairment: validation of a recombinant protein-based ELISA assay》**
*作者:Lee H, et al.*
**摘要**:基于重组CysC开发新型ELISA检测方法,通过大样本临床验证证实其较血清肌酐能更敏感反映肾小球滤过率变化,支持其作为慢性肾病早期诊断标志物。
(注:以上文献信息为示例性质,实际引用请核对真实出版物。)
Cystatin C (CysC), a 13-kDa cysteine protease inhibitor, is a member of the cystatin superfamily involved in regulating proteolytic activity of cathepsins. Naturally produced by all nucleated cells, it plays critical roles in protein degradation, immune response modulation, and extracellular matrix remodeling. Unlike creatinine, CysC’s serum concentration is less influenced by age, gender, or muscle mass, making it a superior biomarker for estimating glomerular filtration rate (GFR) and diagnosing early-stage kidney dysfunction. Its clinical relevance has driven demand for standardized recombinant versions for research and diagnostic applications.
Recombinant CysC protein is typically produced using prokaryotic (e.g., *E. coli*) or eukaryotic expression systems (e.g., mammalian cells), with the former being cost-effective for bulk production and the latter offering post-translational modifications closer to native human CysC. The protein is purified via affinity chromatography, often leveraging tags like His-tag for streamlined isolation. Structural integrity and functional validation (e.g., cathepsin inhibition assays) are essential to ensure batch-to-batch consistency.
In biomedical research, recombinant CysC serves as a tool to study neurodegenerative diseases (e.g., Alzheimer’s), cancer progression, and cardiovascular disorders, where dysregulated protease activity is implicated. Therapeutically, engineered CysC variants are explored for neuroprotection and anti-metastatic therapies. Commercially, it is utilized in ELISA kits and calibrators to standardize CKD (chronic kidney disease) diagnostics. Recent advances in protein engineering, such as PEGylation, aim to enhance its stability and bioavailability for extended clinical applications. Ongoing studies focus on optimizing production yields and functional modifications to meet growing translational demands.
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