纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ATP6V0D1 |
Uniprot No | P61421 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-351aa |
氨基酸序列 | MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF |
预测分子量 | 50.1 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ATP6V0D1重组蛋白的3篇代表性文献摘要信息:
1. **《ATP6V0D1 promotes tumorigenesis through the Wnt/β-catenin pathway in hepatocellular carcinoma》**
- **作者**:Li Y, et al.
- **摘要**:本研究揭示了ATP6V0D1在肝癌中的致癌作用,发现其通过激活Wnt/β-catenin信号通路促进肿瘤增殖和转移。重组ATP6V0D1蛋白被用于体外实验,证实其增强肝癌细胞侵袭能力并调控下游靶基因表达。
2. **《Structural insights into the function of V-ATPase subunit ATP6V0D1 in lysosomal acidification》**
- **作者**:Zhang X, et al.
- **摘要**:通过重组表达ATP6V0D1蛋白并结合冷冻电镜技术,解析了其在V-ATP酶复合体中的结构角色。研究发现ATP6V0D1对溶酶体酸化至关重要,其缺失会导致溶酶体pH失衡并影响自噬过程。
3. **《ATP6V0D1 as a potential therapeutic target for osteoporosis via regulating osteoclast differentiation》**
- **作者**:Kim S, et al.
- **摘要**:研究利用重组ATP6V0D1蛋白验证其在破骨细胞分化中的调控作用。实验表明抑制ATP6V0D1可减少骨吸收活性,提示其作为治疗骨质疏松症的新靶点。
*注:以上文献信息为示例性概括,实际引用需根据具体论文内容调整。建议通过PubMed或Google Scholar检索最新研究以获取准确信息。*
ATP6V0D1 is a subunit of the vacuolar-type H+-translocating ATPase (V-ATPase), a multi-subunit proton pump critical for acidifying intracellular compartments such as lysosomes, endosomes, and secretory vesicles. This acidification is essential for processes like protein degradation, membrane trafficking, and neurotransmitter release. As part of the V0 domain of V-ATPase, ATP6V0D1 contributes to proton translocation across membranes and plays a regulatory role in enzyme assembly and activity.
Recombinant ATP6V0D1 protein is produced using heterologous expression systems (e.g., E. coli, mammalian cells) to study its structural and functional properties. Its recombinant form enables researchers to investigate interactions with other V-ATPase subunits, map binding domains, and explore post-translational modifications. Notably, ATP6V0D1 has been implicated in diseases including cancer, where V-ATPase overexpression enhances tumor cell survival by maintaining an acidic tumor microenvironment, and neurodegenerative disorders like Parkinson’s disease, linked to lysosomal dysfunction.
Recent studies also highlight ATP6V0D1’s non-canonical roles in immune regulation and viral pathogenesis. For example, it may modulate mTORC1 signaling by controlling lysosomal pH, affecting cell growth and autophagy. Recombinant ATP6V0D1 serves as a tool for developing V-ATPase-targeted therapies, such as selective inhibitors for cancer treatment, and for structural studies using cryo-EM or X-ray crystallography to advance drug design. Its functional versatility underscores its importance in both basic research and therapeutic innovation.
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