| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAPA |
| Uniprot No | Q9P0L0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-227aa |
| 氨基酸序列 | ASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSP |
| 预测分子量 | 32.3 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VAPA重组蛋白的假设性参考文献示例(非真实文献，仅作格式参考)：
1. **文献名称**：Structural characterization of recombinant VAPA and its role in ER-mitochondria contact sites
**作者**：Zhang Y et al. (2020)
**摘要**：通过重组VAPA蛋白的体外表达和X射线晶体学研究，揭示了VAPA MSP结构域与内质网-线粒体接触位点中脂质转移的分子机制，为膜接触调控提供了结构基础。
2. **文献名称**：VAPA recombinant protein interacts with hepatitis C virus NS5A and modulates viral replication
**作者**：Johnson R et al. (2019)
**摘要**：利用重组VAPA蛋白进行体外结合实验，证实其与丙肝病毒NS5A蛋白相互作用，调控病毒复制复合体的组装，提示VAPA可能成为抗病毒治疗的潜在靶点。
3. **文献名称**：Functional analysis of VAPA mutations in amyotrophic lateral sclerosis using recombinant protein models
**作者**：Smith JL et al. (2018)
**摘要**：通过重组VAPA突变体蛋白的功能研究，发现ALS相关突变破坏了VAPA与VAPB的异源二聚化能力，导致内质网应激通路异常，与神经元退行性病变相关。
4. **文献名称**：Recombinant VAPA facilitates lipid transfer in vitro and regulates cellular lipid homeostasis
**作者**：Lee H et al. (2021)
**摘要**：纯化重组VAPA蛋白证明其通过MSP结构域介导胆固醇和磷脂酰肌醇的转运，在体外脂质转移实验中明确了其在细胞脂代谢中的关键作用。
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**注意**：以上为模拟文献，实际研究中建议通过PubMed、Web of Science等平台检索关键词“VAPA recombinant protein”或结合具体研究领域(如神经科学、病毒学)筛选文献。
VAPA (Vesicle-associated membrane protein-associated protein A) is a ubiquitously expressed eukaryotic protein belonging to the VAP (VAP-A and VAP-B) family. It localizes to the endoplasmic reticulum (ER) and plays critical roles in intracellular membrane trafficking, lipid transfer, and inter-organelle communication. Structurally, VAPA contains a major sperm protein (MSP) domain at its N-terminus, which mediates interactions with proteins containing FFAT (two phenylalanines in an acidic tract) motifs, and a transmembrane domain anchoring it to the ER membrane.
Functionally, VAPA acts as a scaffold protein, facilitating membrane contact sites (MCSs) between the ER and other organelles (e.g., Golgi, endosomes, plasma membrane). These contacts enable lipid exchange and calcium signaling. VAPA interacts with lipid-transfer proteins like OSBP/ORP and STARD3. coordinating cholesterol/phospholipid distribution. Dysregulation of VAPA is linked to neurodegenerative diseases (e.g., ALS) and cancers, where altered lipid metabolism or ER stress pathways contribute to pathogenesis. Its involvement in viral replication (e.g., hepatitis C) further highlights therapeutic targeting potential.
Recombinant VAPA proteins are engineered using expression systems (E. coli, mammalian cells) for functional studies. Purified versions retain structural integrity to investigate binding partners, lipid transfer mechanisms, or drug interactions. Researchers utilize these proteins in pull-down assays, structural biology (X-ray crystallography), and high-throughput screens for therapeutic discovery. Tagged variants (His, GST) simplify purification and detection. As MCS regulators gain attention in cellular homeostasis, recombinant VAPA remains pivotal for deciphering organelle dynamics and disease mechanisms.
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