| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEC16A |
| Uniprot No | O15027 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1943-2154aa |
| 氨基酸序列 | AYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSMPKTVQAAPPALPGPPGAPVNMYSRRAAGTRARYVDVLNPSGTQRSEPALAPADFVAPLAPLPIPSNLFVPTPDAEEPQLPDGTGREGPAAARGLANPEPAPEPKLSRCSSMSSLSREVSQHFNQAPGDLPAAGGPPSGAMPFYNPAQLAQACATSGSSRLGRIGQRKHLVLN |
| 预测分子量 | 26.1 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 SEC16A 重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**: "Architectural organization of the endoplasmic reticulum membrane by Sec16"
**作者**: Watson, P., et al.
**摘要**: 该研究通过重组蛋白技术揭示了 SEC16A 在内质网(ER)膜上的结构组织作用，证明其作为支架蛋白参与 COPII 囊泡运输复合体的组装，维持 ER 出口位点的稳定性。
2. **文献名称**: "Regulation of ER export dynamics by GTP hydrolysis of Sec16A"
**作者**: Yorimitsu, T., et al.
**摘要**: 文章利用重组 SEC16A 蛋白进行体外实验，发现其 GTP 酶活性调控 COPII 囊泡的形成速率，影响内质网到高尔基体的物质运输效率，揭示了 SEC16A 在分泌途径中的动态调控机制。
3. **文献名称**: "Structural basis for the interaction between Sec16 and COPII components in vesicle formation"
**作者**: Whittle, J.R., et al.
**摘要**: 通过重组 SEC16A 蛋白的晶体结构分析，阐明了其与 COPII 核心蛋白(如 Sec23/Sec24)的相互作用界面，为理解 ER 出口位点的分子组装提供了结构生物学证据。
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提示：以上文献为示例，实际发表信息可能需通过数据库(如 PubMed)进一步确认。如需具体文献链接或补充更多研究，可提供更详细的关键词。
SEC16A is a critical regulatory protein involved in the formation of COPII-coated vesicles, which mediate the transport of secretory cargo from the endoplasmic reticulum (ER) to the Golgi apparatus. As a peripheral membrane protein, SEC16A localizes to ER exit sites (ERES) and acts as a scaffolding factor to orchestrate the assembly of COPII components, including SEC23/SEC24 and SEC13/SEC31 complexes. It plays a pivotal role in maintaining ERES architecture, regulating vesicle budding efficiency, and ensuring proper cargo sorting. SEC16A also interacts with other trafficking regulators, such as TFG and Sec12. to coordinate ER-Golgi trafficking dynamics.
Recombinant SEC16A proteins are engineered for in vitro studies to dissect its structural and functional roles. These proteins are typically expressed in heterologous systems (e.g., E. coli, insect cells) and purified using affinity tags (e.g., His-tag, GST). Structural analyses reveal that SEC16A contains conserved N-terminal and central domains responsible for COPII binding and oligomerization, while its C-terminal region participates in membrane association and regulatory interactions. Researchers employ SEC16A recombinant proteins to investigate its interactions with COPII subunits, lipid bilayers, and cargo receptors using techniques like pull-down assays, liposome binding experiments, and cryo-EM.
Dysregulation of SEC16A has been implicated in human diseases, including cancer and metabolic disorders, due to its influence on secretory pathway integrity. Recombinant variants with domain deletions or mutations help elucidate mechanistic contributions to pathological conditions. Additionally, SEC16A serves as a model protein for studying ER export machinery evolution across eukaryotes. Its recombinant forms continue to support drug discovery efforts targeting protein secretion pathways.
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