| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GOLGA7 |
| Uniprot No | Q7Z5G4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-137aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMRPQQAPVSGKVFIQRDYSSGTRCQFQ TKFPAELENRIDRQQFEETVRTLNNLYAEAEKLGGQSYLEGCLACLTAYT IFLCMETHYEKVLKKVSKYIQEQNEKIYAPQGLLLTDPIERGLRVIEITI YEDRGMSSGR |
| 预测分子量 | 18 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GOLGA7重组蛋白的3篇代表性文献的简要信息：
1. **文献名称**：*GOLGA7重组蛋白在丙型肝炎病毒复制中的功能研究*
**作者**：Li, Y., et al.
**摘要**：该研究通过表达GOLGA7重组蛋白，发现其与丙型肝炎病毒NS5A蛋白相互作用，调控病毒复制复合体的形成，揭示GOLGA7在病毒生命周期中的关键作用。
2. **文献名称**：*高尔基体蛋白GOLGA7调控EGFR运输的分子机制*
**作者**：Wang, X., & Zhang, J.
**摘要**：利用重组GOLGA7蛋白进行体外结合实验，证明其通过结合EGFR的胞内结构域，影响EGFR从高尔基体到细胞膜的运输，从而调节细胞信号转导。
3. **文献名称**：*GOLGA7重组蛋白的结构解析及其与Rab1的相互作用*
**作者**：Saito, K., et al.
**摘要**：通过X射线晶体学解析了GOLGA7重组蛋白的三维结构，并发现其N端结构域特异性结合Rab1 GTP酶，为阐明高尔基体-内质网囊泡运输机制提供结构基础。
注：以上为模拟文献示例，实际研究中请通过学术数据库(如PubMed/Web of Science)检索最新文献。
GOLGA7. also known as Golgin A7. is a member of the golgin family of proteins predominantly localized to the Golgi apparatus. These coiled-coil domain-containing proteins play critical roles in maintaining Golgi structure, vesicle trafficking, and membrane fusion processes. The human GOLGA7 gene encodes a 437-amino-acid protein characterized by its central coiled-coil regions and a C-terminal transmembrane domain, which anchors it to the Golgi membrane. It interacts with Rab GTPases and other trafficking machinery to regulate cargo sorting and organelle integrity.
Recombinant GOLGA7 protein is engineered through heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies. Its production typically involves cloning the coding sequence into expression vectors followed by affinity tag purification (e.g., His-tag). This recombinant form enables researchers to investigate GOLGA7's molecular interactions, particularly its role in Golgi-ER retrograde transport and glycosylation enzyme localization.
Emerging research links GOLGA7 to disease pathways. It shows altered expression in certain cancers, potentially influencing cell proliferation through dysregulation of secretory pathways. Notably, GOLGA7 forms a complex with RET receptor tyrosine kinase and TRIM27. modulating RET's cell surface expression – a pathway implicated in neural crest development and neuroendocrine tumors. In neurodegenerative contexts, disrupted Golgi function mediated by GOLGA7 abnormalities may contribute to protein misfolding cascades.
Studies using recombinant GOLGA7 have advanced understanding of Golgi matrix dynamics and its response to cellular stress. The protein's phosphorylation status during mitosis, regulated by CDK1/cyclin B, suggests involvement in Golgi disassembly-reassembly cycles. Current research leverages recombinant protein in structural studies, antibody development, and high-throughput screening for Golgi-related disorders. However, its full interactome and regulatory mechanisms remain active areas of investigation.
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