| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAPB |
| Uniprot No | O95292 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAKVEQVLSL EPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGI IDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAK PEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSS LDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISA LAPTGKEEGLST |
| 预测分子量 | 27 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VAPB重组蛋白的3篇代表性文献及其摘要概述：
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1. **文献名称**：*A mutation in VAPB causes familial amyotrophic lateral sclerosis*
**作者**：Nishimura AL 等
**摘要**：该研究首次报道了VAPB基因(VAMP-associated protein B)的突变与家族性肌萎缩侧索硬化症(ALS8)的关联。通过重组蛋白实验，发现突变体VAPB(如P56S)在内质网中异常聚集，导致内质网应激并干扰细胞内膜运输功能，揭示了其在神经退行性疾病中的潜在机制。
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2. **文献名称**：*Structure of VAPB and its role in MSP domain-mediated protein interactions*
**作者**：Prosser DC 等
**摘要**：本研究解析了VAPB重组蛋白的晶体结构，重点关注其保守的MSP(major sperm protein)结构域。实验表明，VAPB通过MSP结构域与含有FFAT基序的蛋白(如脂质转运蛋白)结合，调控脂质代谢和细胞器间膜接触，为VAPB的功能机制提供了结构基础。
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3. **文献名称**：*VAPB interacts with the mitochondrial protein PTPIP51 to regulate cellular homeostasis*
**作者**：De Vos KJ 等
**摘要**：通过重组VAPB蛋白的体外结合实验及细胞模型，发现VAPB与线粒体相关蛋白PTPIP51相互作用，介导内质网-线粒体间的钙离子信号传递和脂质交换。研究提示VAPB功能异常可能导致神经元线粒体功能障碍，与ALS等疾病的病理过程相关。
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**备注**：如需具体文献年份或期刊，可进一步补充(如Nishimura AL, 2004. *Nat Genet*;De Vos KJ, 2012. *Hum Mol Genet*)。
VAPB (vesicle-associated membrane protein-associated protein B) is a conserved endoplasmic reticulum (ER)-resident protein involved in maintaining ER structure, lipid transport, and inter-organelle communication. As a member of the VAP protein family, it contains a major sperm protein (MSP) domain at its N-terminus for binding FFAT (two phenylalanines in an acidic tract) motifs in partner proteins, and a transmembrane domain anchoring it to the ER membrane. VAPB facilitates the formation of membrane contact sites between the ER and other organelles, enabling lipid exchange and calcium signaling.
Mutations in the VAPB gene, particularly the proline-to-serine substitution at position 56 (P56S), are linked to neurodegenerative disorders like amyotrophic lateral sclerosis (ALS) and spinal muscular atrophy (SMA). The P56S mutation causes protein misfolding, leading to ER stress, aggregate formation, and impaired interactions with cellular partners such as ORP1 and CERT. These disruptions contribute to neuronal dysfunction and degeneration.
Recombinant VAPB protein, typically produced in bacterial or mammalian expression systems, is engineered with affinity tags (e.g., His-tag) for purification. It serves as a critical tool for studying VAPB’s molecular interactions, structural dynamics, and pathogenic mechanisms. Researchers use it to analyze binding partners, evaluate mutant protein aggregation, and screen therapeutic compounds targeting ER stress or protein misfolding. In disease modeling, recombinant VAPB helps establish cellular or animal models to explore ALS pathogenesis and test gene therapies or small molecules aimed at restoring proteostasis. Current studies focus on elucidating how VAPB dysregulation impacts lipid homeostasis and organelle crosstalk, offering insights into broader neurodegenerative processes.
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