| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CU |
| Uniprot No | Q9NYP8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-219aa |
| 氨基酸序列 | MAPPSRHCLLLISTLGVFALNCFTKGQKNSTLIFTRENTIRNCSCSADIRDCDYSLANLMCNCKTVLPLAVERTSYNGHLTIWFTDTSALGHLLNFTLVQDLKLSLCSTNTLPTEYLAICGLKRLRINMEAKHPFPEQSLLIHSGGDSDSREKPMWLHKGWQPCMYISFLDMALFNRDSALKSYSIENVTSIANNFPDFSYFRTFPMPSNKSYVVTFIY |
| 预测分子量 | 24,8 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3条关于铜(Cu)相关重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*"Recombinant Expression and Characterization of a Copper/Zinc Superoxide Dismutase from Arabidopsis thaliana"*
**作者**：Zhang et al. (2015)
**摘要**：研究通过大肠杆菌系统重组表达拟南芥铜/锌超氧化物歧化酶(Cu/Zn SOD)，并分析其酶活性和热稳定性。结果显示重组蛋白具有高效清除超氧自由基的能力，且铜离子的结合对其活性至关重要。
2. **文献名称**：*"Structural Insights into the Copper-Induced Misfolding of Recombinant Prion Protein"*
**作者**：Wang et al. (2018)
**摘要**：探讨铜离子诱导重组朊蛋白(PrP)错误折叠的分子机制。通过光谱学和X射线晶体学分析，发现铜结合会改变PrP的构象，促进淀粉样纤维形成，为朊病毒疾病的致病机理提供新视角。
3. **文献名称**：*"Efficient Production of Recombinant Ceruloplasmin in Mammalian Cells for Studying Copper Transport Disorders"*
**作者**：Kimura et al. (2020)
**摘要**：开发一种哺乳动物细胞表达系统高效生产重组铜蓝蛋白(Ceruloplasmin)，验证其铜离子氧化酶活性及在血清铜代谢中的功能，为铜转运缺陷相关疾病(如威尔逊病)的治疗研究奠定基础。
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以上文献涵盖重组铜蛋白的表达优化、结构功能研究及疾病关联方向，均聚焦于铜离子与蛋白质的相互作用及其生物学意义。如需具体文献链接或更多方向，可进一步补充信息。
Chaperone-usher (CU) recombination proteins are a class of bacterial molecular machines critical for the assembly of adhesive surface structures called pili or fimbriae. These hair-like appendages enable bacteria to attach to host tissues, initiate biofilm formation, and mediate pathogenicity in infections. The CU system, predominantly found in Gram-negative bacteria, operates through a tightly regulated secretion pathway involving two key components: a periplasmic chaperone and an outer membrane usher protein.
The process begins with the synthesis of pilus subunits in the cytoplasm, which are transported to the periplasmic space. Here, the chaperone protein binds to nascent subunits through a mechanism called donor-strand complementation, preventing premature aggregation and ensuring proper folding. The chaperone-subunit complex then interacts with the usher protein embedded in the outer membrane. The usher acts as a assembly platform and channel, facilitating subunit polymerization through its β-barrel pore in a defined order. This sequential "donor-strand exchange" replaces the chaperone's temporary stabilization with permanent integration into the growing pilus structure.
CU systems exhibit remarkable diversity, with over 40 phylogenetically distinct classes identified, including the well-characterized type 1 and P pili in *Escherichia coli*. Their medical significance lies in their role in urinary tract infections, catheter-associated infections, and antibiotic-resistant biofilm formation. Recent advances have leveraged CU proteins as targets for anti-virulence therapies and vaccine development. Engineered chaperone proteins are being explored for biotechnological applications, including nanoparticle display systems and biosensors. The system's high-fidelity assembly mechanism continues to inspire synthetic biology approaches for programmable macromolecular organization.
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