| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPA2 |
| Uniprot No | P48052 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 115-419aa |
| 氨基酸序列 | SGNFNF GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG SSFENRPMNV LKFSTGGDKP AIWLDAGIHA REWVTQATAL WTANKIVSDY GKDPSITSIL DALDIFLLPV TNPDGYVFSQ TKNRMWRKTR SKVSGSLCVG VDPNRNWDAG FGGPGASSNP CSDSYHGPSA NSEVEVKSIV DFIKSHGKVK AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV GPICSVIYQA SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA EETWLGLKAI MEHVRDHPY |
| 预测分子量 | 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CPA2重组蛋白的模拟参考文献示例，供参考。建议通过学术数据库(如PubMed、Google Scholar)获取最新研究：
1. **文献名称**：*Expression and Characterization of Recombinant Human Carboxypeptidase A2 in E. coli*
**作者**：Smith J, et al.
**摘要**：本研究成功在大肠杆菌中表达了重组人CPA2.通过亲和层析纯化获得高纯度蛋白，并分析了其酶动力学参数，证实其与天然CPA2具有相似的底物特异性。
2. **文献名称**：*Role of Recombinant CPA2 in Pancreatic Cancer Cell Invasion*
**作者**：Zhang L, et al.
**摘要**：利用重组CPA2蛋白进行体外实验，发现其通过降解细胞外基质成分增强胰腺癌细胞的迁移和侵袭能力，提示CPA2在肿瘤转移中的潜在作用。
3. **文献名称**：*Structural Insights into Recombinant CPA2 via X-ray Crystallography*
**作者**：Brown K, et al.
**摘要**：通过X射线晶体学解析了重组CPA2的三维结构，揭示了其活性中心的金属离子结合模式，为设计特异性抑制剂提供了结构基础。
4. **文献名称**：*Optimization of Recombinant CPA2 Production in Pichia pastoris*
**作者**：Garcia R, et al.
**摘要**：在毕赤酵母系统中优化CPA2的表达条件，显著提高了蛋白产量，并验证了其酶活稳定性，为大规模工业应用奠定了基础。
**注意**：以上为模拟文献，实际研究中请查阅具体数据库获取真实数据。建议结合关键词“CPA2 recombinant protein”、“Carboxypeptidase A2 expression”进行检索。
CPA2 (carboxypeptidase A2) is a zinc-dependent metalloprotease primarily synthesized in the pancreas as an inactive precursor, procarboxypeptidase A2. This enzyme plays a critical role in protein digestion by cleaving C-terminal hydrophobic amino acids from dietary proteins, working in tandem with other digestive enzymes. CPA2 is structurally and functionally related to CPA1. but exhibits distinct substrate preferences and tissue expression patterns. Its selective activity makes it a valuable subject for studying enzyme specificity and digestive pathophysiology.
Recombinant CPA2 proteins are engineered using heterologous expression systems, typically E. coli or mammalian cell lines, to produce purified enzymes for research and industrial applications. The production process involves cloning the CPA2 gene into expression vectors, optimizing conditions for proper protein folding, and ensuring preservation of its catalytic zinc-binding motif. Advanced purification techniques like affinity chromatography are employed to achieve high-purity preparations.
Current research focuses on CPA2's potential clinical relevance, particularly its association with pancreatic disorders and cancer progression. Elevated CPA2 levels have been observed in pancreatic adenocarcinoma, suggesting potential as a diagnostic biomarker. In drug development, recombinant CPA2 serves as a tool for studying protease inhibitors and designing targeted therapies. Additionally, it facilitates structural biology studies through crystallographic analysis of enzyme-substrate interactions. The development of recombinant CPA2 has significantly enhanced our ability to investigate digestive enzyme mechanisms while minimizing the need for tissue-extracted proteins, improving experimental reproducibility and safety in biomedical research.
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