纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CPA6 |
Uniprot No | Q8N4T0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 130-437aa |
氨基酸序列 | SLSGYNYEVYHSLEEIQNWMHHLNKTHSGLIHMFSIGRSYEGRSLFILKLGRRSRLKRAVWIDCGIHAREWIGPAFCQWFVKEALLTYKSDPAMRKMLNHLYFYIMPVFNVDGYHFSWTNDRFWRKTRSRNSRFRCRGVDANRNWKVKWCDEGASMHPCDDTYCGPFPESEPEVKAVANFLRKHRKHIRAYLSFHAYAQMLLYPYSYKYATIPNFRCVESAAYKAVNALQSVYGVRYRYGPASTTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYFGFLLPEMLIKPTCTETMLAVKNITMHLLKKCP |
预测分子量 | 52.2 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CPA6重组蛋白的3篇示例参考文献(注:以下为模拟示例,实际文献需通过学术数据库查询确认):
1. **文献名称**:*"Recombinant Expression and Enzymatic Characterization of Human Carboxypeptidase A6 in Insect Cells"*
**作者**:Zhang Y, et al.
**摘要**:本研究利用杆状病毒-昆虫细胞系统成功表达了具有活性的重组人CPA6蛋白,并对其酶学性质进行了分析。结果显示,重组CPA6对疏水性羧基末端底物表现出特异性水解活性,最适pH为7.5.且依赖锌离子作为辅因子。
2. **文献名称**:*"Structural Insights into CPA6 Substrate Specificity through Crystallographic Analysis"*
**作者**:Smith JL, et al.
**摘要**:通过X射线晶体学解析了重组CPA6的三维结构(分辨率2.1Å),揭示了其底物结合口袋的独特构象。研究发现了关键氨基酸残基(如Arg145和Glu270)在底物识别中的作用,为设计选择性抑制剂提供了结构基础。
3. **文献名称**:*"CPA6 Mutations in Familial Epilepsy: Functional Rescue by Recombinant Wild-Type Protein"*
**作者**:Wang H, et al.
**摘要**:本研究在癫痫家系中鉴定了CPA6的功能缺失突变(如p.Arg287Trp)。通过体外表达突变体和野生型重组CPA6.证实突变导致酶活性显著降低,而外源添加野生型蛋白可部分恢复细胞模型中的神经肽加工缺陷。
**建议**:如需真实文献,请使用关键词“CPA6 recombinant”或“Carboxypeptidase A6 expression”在PubMed(https://pubmed.ncbi.nlm.nih.gov)或Google Scholar中检索,并筛选近年高被引研究。
Carboxypeptidase A6 (CPA6) is a zinc-dependent metalloprotease belonging to the M14 family of carboxypeptidases. It plays a role in proteolytic processing, particularly in cleaving C-terminal hydrophobic amino acids from peptides and proteins. CPA6 is distinct from other pancreatic carboxypeptidases (e.g., CPA1/CPA2) due to its tissue-specific expression, primarily in the brain, sensory organs, and during embryonic development. It has been implicated in neuropeptide processing, including substrates like neurotensin and kinins, suggesting its involvement in neuronal signaling and developmental pathways.
Recombinant CPA6 protein is engineered through heterologous expression systems (e.g., mammalian cells, insect cells, or *E. coli*) to study its enzymatic activity, structure, and biological roles. Purified recombinant CPA6 enables *in vitro* studies on substrate specificity, inhibitor screening, and mechanism analysis. Notably, mutations in the CPA6 gene are linked to human diseases such as temporal lobe epilepsy (TLE) and Duane syndrome, highlighting its clinical relevance. Structural studies using recombinant CPA6 have revealed conserved zinc-binding motifs (HEXXH) and substrate-binding pockets, providing insights into catalysis and potential therapeutic targeting.
Research on recombinant CPA6 also explores its extracellular matrix (ECM) interactions, particularly in modulating cell adhesion and tissue remodeling. Dysregulation of CPA6 has been observed in cancers, though its role remains unclear. Overall, recombinant CPA6 serves as a critical tool for deciphering its physiological functions and pathological associations, bridging basic enzymology with translational applications in neurology, oncology, and developmental biology.
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