| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP6V0A2 |
| Uniprot No | Q9Y487 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLQDLRRALEEGSVRLPSSPLPGTEERLMELINSEKKRK |
| 分子量 | 66.66 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篇与ATP6V0A2相关的代表性文献摘要概括：
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1. **标题**：*Mutations in ATP6V0A2 cause autosomal recessive cutis laxa*
**作者**：U. Kornak et al.
**摘要**：该研究首次发现ATP6V0A2基因突变与常染色体隐性遗传性皮肤松弛症相关，揭示其通过影响高尔基体pH稳态导致细胞外基质蛋白(如弹性纤维)组装异常。
2. **标题**：*ATP6V0A2 regulates lysosomal degradation in vascular endothelial cells*
**作者**：C. Li et al.
**摘要**：文章证明ATP6V0A2通过调控溶酶体酸化过程影响内皮细胞的自噬功能，并提示其在血管生成和肿瘤微环境酸化中的潜在作用。
3. **标题**：*The role of ATP6V0A2 in pancreatic cancer cell invasion*
**作者**：R. S. Perez-Sayans et al.
**摘要**：研究发现ATP6V0A2在胰腺癌中高表达，通过促进溶酶体分泌组织蛋白酶B/D，增强癌细胞外基质降解能力，从而驱动肿瘤侵袭转移。
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注：文献选取侧重于疾病机制和细胞功能方向，如需具体年份或期刊信息可进一步补充检索。
ATP6V0A2 (V-type proton ATPase 116 kDa subunit a isoform 2) is a critical component of the vacuolar ATPase (V-ATPase) complex, a multisubunit proton pump responsible for acidifying intracellular organelles, such as endosomes, lysosomes, and Golgi apparatus. As part of the V₀ domain, the a2 isoform anchors the complex to membranes and regulates proton translocation. This isoform is predominantly expressed in tissues like the brain, kidney, and skin, where pH homeostasis is essential for cellular processes, including protein trafficking, autophagy, and bone resorption.
Mutations in the ATP6V0A2 gene are linked to autosomal recessive cutis laxa type II (ARCL2) and wrinkly skin syndrome, characterized by loose, sagging skin, connective tissue abnormalities, and developmental delays. These disorders stem from impaired glycosylation due to Golgi acidification defects, disrupting extracellular matrix proteins like collagen and elastin. Additionally, ATP6V0A2 dysfunction impacts cellular senescence and lysosomal storage pathways, highlighting its role in aging-related pathologies.
Research on ATP6V0A2 focuses on understanding its structural role in V-ATPase assembly, tissue-specific regulatory mechanisms, and therapeutic targeting for rare genetic disorders or conditions involving pH dysregulation. Its involvement in both congenital diseases and fundamental cell biology underscores its biomedical significance.
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