| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP6V1F |
| Uniprot No | Q16864 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-119aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAGRGKL IAVIGDEDTV TGFLLGGIGE LNKNRHPNFL VVEKDTTINE IEDTFRQFLN RDDIGIILIN QYIAEMVRHA LDAHQQSIPA VLEIPSKEHP YDAAKDSILR RARGMFTAED LR |
| 预测分子量 | 16 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ATP6V1F重组蛋白的3篇参考文献示例(注：文献为虚构示例，实际研究中请核实真实文献)：
1. **文献名称**：*Structural and Functional Analysis of Recombinant ATP6V1F in V-ATPase Assembly*
**作者**：Chen, X., et al.
**摘要**：本研究通过重组表达人源ATP6V1F蛋白，结合冷冻电镜技术解析其三维结构，揭示了该亚基在V-ATP酶复合体组装中的关键作用，并发现其与ATP6V1E亚基的相互作用位点。
2. **文献名称**：*Expression and Purification of Recombinant ATP6V1F for Proton Transport Studies*
**作者**：Müller, S., et al.
**摘要**：开发了一种高效的真核表达系统(HEK293细胞)生产重组ATP6V1F蛋白，证实其在体外可恢复缺陷型V-ATP酶的质子泵活性，为酶功能研究提供工具。
3. **文献名称**：*ATP6V1F Dysfunction in Cancer: Recombinant Protein-Based Mechanistic Insights*
**作者**：Kim, H., et al.
**摘要**：通过重组ATP6V1F蛋白的体外功能实验，发现其表达水平降低导致溶酶体pH升高，促进肿瘤细胞侵袭，提示其作为癌症治疗靶点的潜力。
如需实际文献，建议在PubMed或Web of Science中检索关键词“ATP6V1F recombinant”或“V-ATPase subunit F expression”。
ATP6V1F is a subunit of the vacuolar-type H+-ATPase (V-ATPase), a multisubunit proton pump critical for cellular pH regulation. V-ATPases acidify intracellular compartments, such as lysosomes, endosomes, and secretory vesicles, enabling processes like protein degradation, membrane trafficking, and neurotransmitter release. They also localize to plasma membranes in specialized cells (e.g., osteoclasts, kidney intercalated cells) to modulate extracellular pH. Structurally, V-ATPases comprise two domains: the cytosolic V1 sector (ATP hydrolysis) and the membrane-embedded V0 sector (proton translocation). ATP6V1F, a 16 kDa protein, is part of the V1 domain’s peripheral stalk, contributing to structural stability and regulatory interactions between V1 and V0.
Recombinant ATP6V1F protein is produced using expression systems like *E. coli* or mammalian cells, often tagged for purification and detection. Its study helps elucidate V-ATPase assembly, function, and dysfunction linked to diseases. For instance, V-ATPase mutations are associated with renal tubular acidosis, neurodegenerative disorders, and cancer. In tumors, V-ATPase overexpression enhances microenvironment acidification, promoting invasion and chemoresistance. ATP6V1F’s role in these contexts remains underexplored, making recombinant protein tools valuable for mechanistic studies. Additionally, ATP6V1F may interact with viral proteins (e.g., HIV-1 Nef) to modulate host cell pathways, highlighting its relevance in virology. Research on ATP6V1F also aids in developing V-ATPase-targeted therapies, such as selective inhibitors for cancer or osteoporosis. Despite its auxiliary role, ATP6V1F’s conservation across eukaryotes underscores its functional importance in maintaining pH homeostasis and cellular health.
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