| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP6V1D |
| Uniprot No | Q9Y5K8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-247aa |
| 氨基酸序列 | MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSEKDL EQRRAAGEVL EPANLLAEEK DEDLLFE |
| 分子量 | 52.91 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 冻干粉 |
| 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3篇关于ATP6V1D的虚拟参考文献示例(文献为虚构，仅供格式参考)：
1. **"ATP6V1D regulates lysosomal acidification and promotes tumor cell invasion"**
*作者：Li X, et al.*
摘要：研究发现ATP6V1D通过维持溶酶体酸性环境，促进肿瘤细胞的胞外基质降解，增强乳腺癌细胞的迁移和侵袭能力。
2. **"ATP6V1D deficiency impairs autophagosome-lysosome fusion via pH imbalance"**
*作者：Wang Y, et al.*
摘要：通过CRISPR敲除ATP6V1D，发现其缺失导致溶酶体酸化异常，阻断自噬体-溶酶体融合，引发神经元细胞中蛋白质聚集和凋亡。
3. **"ATP6V1D interacts with mTOR signaling to modulate cellular metabolism"**
*作者：Chen J, et al.*
摘要：揭示ATP6V1D通过结合mTOR复合物调控细胞代谢重编程，其表达上调与结直肠癌患者化疗耐药性显著相关。
(注：以上内容为模拟生成，实际文献需通过PubMed/Google Scholar检索关键词"ATP6V1D"或"V-ATPase subunit D"获取。)
ATP6V1D, a key subunit of the vacuolar-type H+-ATPase (V-ATPase), is an essential component of this multi-subunit proton pump responsible for acidifying intracellular compartments such as lysosomes, endosomes, and secretory vesicles. V-ATPases are composed of two domains: the cytosolic V1 domain (ATP hydrolysis) and the membrane-bound V0 domain (proton translocation). ATP6V1D resides within the V1 sector (subunit D) and plays a structural and regulatory role in enzyme assembly, activity, and intracellular targeting. It facilitates coupling of ATP hydrolysis to proton transport, maintaining organelle pH gradients critical for protein degradation, membrane trafficking, and neurotransmitter release. Dysregulation of V-ATPases is linked to diseases like cancer, osteoporosis, and renal tubular acidosis. Recombinant human ATP6V1D, produced via heterologous expression systems, enables mechanistic studies of V-ATPase function, disease-related mutations, and potential therapeutic targeting. Its study provides insights into pH-dependent cellular processes and pathologies associated with lysosomal or secretory defects.
×
