| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAMP7 |
| Uniprot No | P51809 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-188aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAILFAV VARGTTILAK HAWCGGNFLE VTEQILAKIP SENNKLTYSH GNYLFHYICQ DRIVYLCITD DDFERSRAFN FLNEIKKRFQ TTYGSRAQTA LPYAMNSEFS SVLAAQLKHH SENKGLDKVM ETQAQVDELK GIMVRNIDLV AQRGERLELL IDKTENLVDS SVTFKTTSRN LARAMCMKNL K |
| 预测分子量 | 23 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VAMP7重组蛋白的3篇参考文献概览(文献名称、作者及摘要内容)：
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1. **文献名称**：*VAMP7 modulates ciliogenesis via autophagy*
**作者**：Chaineau M, et al.
**摘要**：该研究通过重组VAMP7蛋白的体外实验，揭示其通过自噬途径调控纤毛形成，发现VAMP7与自噬相关蛋白LC3的相互作用依赖其SNARE结构域。
2. **文献名称**：*Structural and functional analysis of the VAMP7 longin domain*
**作者**：Daste F, et al.
**摘要**：作者利用重组VAMP7的Longin结构域进行结构解析和体外结合实验，证明该结构域调控VAMP7的膜定位及其与其他SNARE蛋白的互作。
3. **文献名称**：*VAMP7 regulates cargo delivery to lysosomes via a Rab7-dependent mechanism*
**作者**：Pryor PR, et al.
**摘要**：通过重组VAMP7蛋白的功能研究，发现其依赖Rab7介导溶酶体运输，并证明其胞内运输路径与溶酶体成熟密切相关。
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以上文献均涉及重组VAMP7蛋白在细胞运输机制中的功能研究，涵盖结构解析、自噬调控及溶酶体运输等领域。如需具体文献来源(期刊、年份等)，建议通过PubMed或Google Scholar进一步检索。
Vesicle-associated membrane protein 7 (VAMP7), also known as TI-VAMP or SYBL1. is a member of the SNARE (Soluble NSF Attachment Protein Receptor) protein family that plays critical roles in intracellular membrane fusion events. It was first identified in the late 1990s as a tetanus neurotoxin-insensitive homolog of neuronal VAMPs (VAMP1/2), distinguishing it from synaptic vesicle-associated VAMPs. Structurally, VAMP7 contains a conserved SNARE motif that forms coiled-coil interactions with target SNAREs (Q-SNAREs), a transmembrane domain anchoring it to vesicles, and a longin domain regulating its intracellular trafficking.
VAMP7 is ubiquitously expressed but particularly abundant in cells with active secretory pathways, including neurons, epithelial cells, and immune cells. It localizes to late endosomes, lysosomes, and specialized secretory vesicles, mediating fusion events in diverse processes such as autophagy, phagocytosis, exosome release, and lysosomal secretion. Unlike synaptic VAMPs, VAMP7 participates in unconventional secretion pathways and membrane repair mechanisms. Its activity is tightly regulated by Rab GTPases (e.g., Rab7) and cytoskeletal interactions through the longin domain.
Recombinant VAMP7 proteins are typically produced in bacterial or mammalian expression systems, often fused with tags (e.g., GST, His-tag) for purification and detection. These engineered proteins enable biochemical studies of SNARE complex assembly, membrane fusion reconstitution assays, and screening for small molecule modulators. Research using recombinant VAMP7 has revealed its involvement in pathological conditions including neurodegenerative diseases (e.g., altered in Parkinson's α-synuclein trafficking), cancer metastasis (via exosome-mediated invasion), and microbial infection strategies. Current studies focus on deciphering its isoform-specific functions and therapeutic targeting potential.
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