| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NID |
| Uniprot No | P14543 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 927-1247aa |
| 氨基酸序列 | IHQGPAVPTAVIPLPPGTHLLFAQTGKIERLPLEGNTMRKTEAKAFLHVPAKVIIGLAFDCVDKMVYWTDITEPSIGRASLHGGEPTTIIRQDLGSPEGIAVDHLGRNIFWTDSNLDRIEVAKLDGTQRRVLFETDLVNPRGIVTDSVRGNLYWTDWNADNPKIETSYMDGTNRRILVQDDLGLPNGLTFDAFSSQLCWVDAGTNRAECLNPSQPSRRKALEGLQAPFAVTSYGKNLYFTDAKMNSVVALDLAISKETDAFQPHKQTALAGITTALSQCPQGHNYCSVNNGGCTHLCLATPGSRTCRCPDNTLGVDCIEQK |
| 预测分子量 | 42.0 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NID重组蛋白的3篇代表性文献(注：NID蛋白可能指不同领域的研究对象，此处假设为细胞外基质相关蛋白Nidogen/Enactin的缩写)：
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1. **文献名称**：*Recombinant expression and structural analysis of the Nidogen G1 domain*
**作者**：Kohfeldt, E., et al.
**摘要**：研究通过大肠杆菌系统重组表达Nidogen的G1结构域，并通过X射线晶体学解析其三维结构，揭示了其与层粘连蛋白相互作用的分子机制。
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2. **文献名称**：*Functional characterization of recombinant NID1 in tumor angiogenesis*
**作者**：Mok, S.C., et al.
**摘要**：利用哺乳动物细胞表达系统制备重组NID1蛋白，发现其通过调控VEGF信号通路抑制肿瘤血管生成，为癌症治疗提供了潜在靶点。
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3. **文献名称**：*High-yield production of Nidogen-2 in insect cells using baculovirus vectors*
**作者**：Hopf, M., et al.
**摘要**：开发了一种基于杆状病毒-昆虫细胞系统的Nidogen-2重组蛋白高效表达方法，并验证其在体外对基底膜组装的促进作用。
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注：若具体指其他NID相关蛋白(如神经分化相关蛋白)，建议补充背景信息以优化检索。以上文献为模拟示例，实际引用需通过学术数据库确认。
NID (Neuropilin and Immunoglobulin Domain-containing) recombinant proteins are engineered variants derived from a family of cell surface and extracellular matrix proteins that play critical roles in cellular adhesion, migration, and signaling. Initially identified as transmembrane glycoproteins, NID proteins are characterized by their unique structural domains: an N-terminal neuropilin-like domain, immunoglobulin (Ig) motifs, and a cytoplasmic tail involved in intracellular signaling. These proteins interact with integrins, growth factor receptors, and extracellular matrix components, modulating processes such as angiogenesis, tissue remodeling, and tumor progression.
The development of recombinant NID proteins emerged from the need to study their functional mechanisms in vitro and explore therapeutic applications. By expressing these proteins in heterologous systems (e.g., mammalian cells, bacteria), researchers obtain purified, bioactive forms to investigate ligand-receptor interactions, cell behavior, and downstream signaling pathways. For example, recombinant NID1 (a prominent member) has been used to study its role in stabilizing basement membranes and regulating endothelial cell motility.
In therapeutic contexts, NID recombinant proteins hold potential for cancer treatment, as they influence tumor microenvironment dynamics and metastatic pathways. They are also explored in regenerative medicine for scaffold-based tissue engineering, leveraging their ECM-binding properties. Additionally, engineered variants with modified domains help dissect structure-function relationships or develop targeted inhibitors. Challenges remain in maintaining proper post-translational modifications (e.g., glycosylation) during recombinant production, which are critical for functional fidelity. Current research focuses on optimizing expression systems and leveraging structural biology insights to expand their biomedical utility.
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