| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPA5 |
| Uniprot No | Q8WXQ8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 127-436aa |
| 氨基酸序列 | LERS TNSFSYSSYH TLEEIYSWID NFVMEHSDIV SKIQIGNSFE NQSILVLKFS TGGSRHPAIW IDTGIHSREW ITHATGIWTA NKIVSDYGKD RVLTDILNAM DIFIELVTNP DGFAFTHSMN RLWRKNKSIR PGIFCIGVDL NRNWKSGFGG NGSNSNPCSE TYHGPSPQSE PEVAAIVNFI TAHGNFKALI SIHSYSQMLM YPYGRLLEPV SNQRELYDLA KDAVEALYKV HGIEYIFGSI STTLYVASGI TVDWAYDSGI KYAFSFELRD TGQYGFLLPA TQIIPTAQET WMALRTIMEH TLNHPY |
| 预测分子量 | 49 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CPA5重组蛋白的3篇模拟参考文献示例(供参考，实际文献需通过学术数据库检索)：
1. **文献名称**：重组人羧肽酶A5(CPA5)的克隆表达及酶学性质研究
**作者**：李明等
**摘要**：本研究成功构建了人源CPA5基因的重组表达载体，通过大肠杆菌系统实现了CPA5的可溶性表达，并优化了纯化条件。酶活实验表明，重组CPA5对多种肽类底物具有水解活性，最适pH为7.5.且金属离子依赖性显著，为后续功能研究奠定基础。
2. **文献名称**：CPA5重组蛋白在肿瘤细胞侵袭中的作用机制
**作者**：Chen, X., et al.
**摘要**：通过体外重组表达CPA5蛋白，发现其能够降解细胞外基质中的特定多肽，促进肿瘤细胞迁移。进一步实验证实，抑制CPA5活性可降低结肠癌细胞侵袭能力，提示其可能成为癌症治疗的潜在靶点。
3. **文献名称**：Structural and Functional Characterization of Recombinant CPA5 in Zinc-Binding Mechanism
**作者**：Smith, J. & Tanaka, K.
**摘要**：采用X射线晶体学解析了重组CPA5的三维结构，揭示了其活性中心锌离子结合位点的关键氨基酸残基。突变实验证实，His196和Glu270对酶活性至关重要，为设计特异性抑制剂提供了结构基础。
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**提示**：以上为示例性内容，实际文献建议通过PubMed、Web of Science或Google Scholar检索关键词(如"CPA5 recombinant protein"、"carboxypeptidase A5 expression")获取。近年研究可能涉及CPA5在疾病中的调控机制或作为生物标志物的潜力。
**Background of Recombinant CPA5 Protein**
Carboxypeptidase A5 (CPA5) is a zinc-dependent metalloprotease belonging to the M14 family of carboxypeptidases. It plays a role in the selective cleavage of C-terminal amino acid residues from peptides and proteins, particularly those with hydrophobic or aromatic side chains. CPA5 is encoded by the *CPA5* gene and is primarily expressed in the digestive system, though emerging studies suggest its involvement in pathological processes such as cancer progression, inflammation, and neuropeptide processing.
Recombinant CPA5 protein is produced using genetic engineering techniques, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., mammalian or insect cell) systems to ensure proper folding and enzymatic activity. The recombinant form allows for controlled production of the enzyme, enabling detailed studies of its structure, substrate specificity, and regulatory mechanisms. Its purification typically involves affinity chromatography and ion-exchange methods to achieve high purity and functionality.
Research on recombinant CPA5 has gained momentum due to its potential biomedical applications. For instance, it is studied for its role in modulating bioactive peptides, including those involved in blood pressure regulation and pain signaling. In cancer biology, CPA5 may influence tumor microenvironment remodeling by processing extracellular matrix components or growth factors. Additionally, recombinant CPA5 serves as a tool for drug discovery, aiding in the development of inhibitors targeting metalloproteases for therapeutic interventions.
Despite progress, challenges remain in understanding its tissue-specific functions and interaction networks. Further studies using recombinant CPA5 could elucidate its physiological and pathological roles, paving the way for novel diagnostic or therapeutic strategies.
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