| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NCAD |
| Uniprot No | P19022 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-906aa |
| 氨基酸序列 | MCRIAGALRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESAEVEEIVFPRQFSKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRIVSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDIIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD |
| 预测分子量 | 99,8 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篇与NCAD(N-Cadherin)重组蛋白相关的文献示例(注：文献为示例性内容，具体引用需核实原始文献)：
---
1. **文献名称**: *"Production and functional characterization of recombinant human N-cadherin extracellular domain"*
**作者**: Smith J, et al.
**摘要**: 研究报道了通过哺乳动物表达系统成功表达重组人N-Cadherin胞外域蛋白，验证其与β-catenin的结合能力，并证明其在体外抑制肿瘤细胞迁移的作用。
2. **文献名称**: *"Structural basis of N-cadherin dimerization revealed by recombinant protein crystallography"*
**作者**: Lee H, et al.
**摘要**: 利用重组N-Cadherin蛋白进行晶体结构解析，揭示了钙离子依赖的二聚化机制，为理解细胞间黏附的分子基础提供结构依据。
3. **文献名称**: *"Recombinant N-cadherin promotes neural crest cell migration in zebrafish embryos"*
**作者**: Chen R, et al.
**摘要**: 通过原核系统表达斑马鱼N-Cadherin重组蛋白，证明其可增强神经嵴细胞的定向迁移，并依赖Wnt信号通路调控。
---
如需具体文献，建议在PubMed或Web of Science中以关键词 **"recombinant N-Cadherin"** 或 **"N-Cadherin protein engineering"** 检索最新研究。
**Background of NCAD Recombinant Protein**
N-Cadherin (NCAD), a calcium-dependent cell adhesion molecule, plays a pivotal role in mediating cell-cell interactions during tissue morphogenesis, neuronal connectivity, and cancer progression. As a member of the classical cadherin family, NCAD is integral to maintaining structural integrity in tissues like the nervous system, heart, and muscles. Its extracellular domain facilitates homophilic binding, while the intracellular domain interacts with catenins to link the actin cytoskeleton, ensuring mechanical stability and signaling coordination.
Dysregulation of NCAD is implicated in pathological conditions, including tumor metastasis, where its overexpression promotes epithelial-to-mesenchymal transition (EMT), enhancing cancer cell invasiveness. Conversely, reduced NCAD levels correlate with neurodegenerative disorders, underscoring its dual role in health and disease.
Recombinant NCAD proteins are engineered *in vitro* using expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional domains or full-length proteins. These proteins retain key biological activities, enabling researchers to study cadherin-mediated adhesion, signaling pathways, and therapeutic targeting. Applications span drug discovery (e.g., anti-metastatic agents), tissue engineering (e.g., biomimetic scaffolds), and mechanistic studies in developmental biology.
The production of NCAD recombinant proteins often involves tag-fusion (e.g., Fc or His tags) for simplified purification and detection. Structural analyses (X-ray crystallography, cryo-EM) of recombinant NCAD have elucidated binding interfaces and calcium dependency, informing inhibitor design. Despite challenges in preserving post-translational modifications (e.g., glycosylation) in non-mammalian systems, advances in expression technologies continue to enhance the reliability of recombinant NCAD for both basic research and translational applications.
×
