| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PP |
| Uniprot No | P60510 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-308aa |
| 氨基酸序列 | MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVT VCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLAL KVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYL SLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDP EDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFN ETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKK PVADYFL |
| 预测分子量 | 60 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“PP重组蛋白”的假设性参考文献示例(注：PP蛋白的具体定义需结合研究领域，此处为通用示例)：
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1. **文献名称**: *Expression and Immunogenicity of Recombinant PP Protein from Porcine Parvovirus*
**作者**: Zhang, L. et al.
**摘要**: 研究在大肠杆菌中高效表达猪细小病毒PP重组蛋白，通过纯化获得高纯度产物，并证实其在小鼠模型中诱导强烈的体液免疫反应，具备疫苗开发潜力。
2. **文献名称**: *Crystal Structure and Functional Analysis of PP Recombinant Protein*
**作者**: Liu, X. et al.
**摘要**: 利用X射线晶体学解析PP重组蛋白的三维结构，揭示其与宿主细胞受体的结合位点，为抗病毒药物设计提供结构基础。
3. **文献名称**: *PP Recombinant Protein-Based ELISA for Serodiagnosis of Bacterial Infections*
**作者**: Wang, Y. et al.
**摘要**: 开发基于PP重组蛋白的ELISA检测方法，用于快速筛查临床样本中的特定病原体抗体，验证了其高敏感性和特异性。
4. **文献名称**: *Optimization of PP Recombinant Protein Production in Insect Cells*
**作者**: Chen, H. et al.
**摘要**: 在昆虫细胞-杆状病毒系统中优化PP重组蛋白的表达条件，显著提高产量，并验证其在体外功能实验中的生物活性。
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**说明**：若“PP”指代特定蛋白(如磷酸酶、病原体抗原等)，建议结合具体研究领域调整关键词检索真实文献(如PubMed、Google Scholar)。
**Background of PP Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are produced by introducing target genes into host organisms (e.g., *E. coli*, yeast, or mammalian cells*) to express specific proteins. PP recombinant proteins, often named for their parental protein or functional domains (e.g., proline-rich motifs, phosphatase activity, or pathogen-derived antigens), represent a subset of these bioengineered molecules. Their design leverages recombinant DNA technology to isolate, modify, and amplify genes encoding proteins of interest, enabling large-scale production with high purity and consistency.
PP recombinant proteins are typically associated with critical biological functions. For instance, some PP variants may regulate cellular signaling pathways, act as enzymes in metabolic processes, or serve as structural components in pathogens. For example, PP (e.g., Protein Phosphatase) recombinant proteins are pivotal in studying phosphorylation-driven mechanisms in diseases like cancer or neurodegeneration. Others, such as viral PP antigens, are utilized in vaccine development or diagnostic assays.
The production process involves cloning the PP gene into expression vectors, optimizing codon usage for host compatibility, and refining purification strategies (e.g., affinity tags like His-tag). Challenges include ensuring proper protein folding, post-translational modifications (e.g., glycosylation in mammalian systems), and minimizing host-induced contaminants.
Applications span therapeutics (e.g., biologics, antibodies), research tools (e.g., ELISA standards, structural studies), and industrial enzymes. Recent advances in synthetic biology and CRISPR-based editing further enhance yield and functionality. PP recombinant proteins continue to drive innovations in precision medicine and biomanufacturing, underscoring their role as indispensable tools in modern biotechnology.
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