| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP13A3 |
| Uniprot No | Q9H7F0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1226aa |
| 氨基酸序列 | MDREERKTINQGQEDEMEIYGYNLSRWKLAIVSLGVICSGGFLLLLLYWMPEWRVKATCVRAAIKDCEVVLLRTTDEFKMWFCAKIRVLSLETYPVSSPKSMSNKLSNGHAVCLIENPTEENRHRISKYSQTESQQIRYFTHHSVKYFWNDTIHNFDFLKGLDEGVSCTSIYEKHSAGLTKGMHAYRKLLYGVNEIAVKVPSVFKLLIKEVLNPFYIFQLFSVILWSTDEYYYYALAIVVMSIVSIVSSLYSIRKQYVMLHDMVATHSTVRVSVCRVNEEIEEIFSTDLVPGDVMVIPLNGTIMPCDAVLINGTCIVNESMLTGESVPVTKTNLPNPSVDVKGIGDELYNPETHKRHTLFCGTTVIQTRFYTGELVKAIVVRTGFSTSKGQLVRSILYPKPTDFKLYRDAYLFLLCLVAVAGIGFIYTIINSILNEVQVGVIIIESLDIITITVPPALPAAMTAGIVYAQRRLKKIGIFCISPQRINICGQLNLVCFDKTGTLTEDGLDLWGIQRVENARFLSPEENVCNEMLVKSQFVACMATCHSLTKIEGVLSGDPLDLKMFEAIGWILEEATEEETALHNRIMPTVVRPPKQLLPESTPAGNQEMELFELPATYEIGIVRQFPFSSALQRMSVVARVLGDRKMDAYMKGAPEAIAGLCKPETVPVDFQNVLEDFTKQGFRVIALAHRKLESKLTWHKVQNISRDAIENNMDFMGLIIMQNKLKQETPAVLEDLHKANIRTVMVTGDSMLTAVSVARDCGMILPQDKVIIAEALPPKDGKVAKINWHYADSLTQCSHPSAIDPEAIPVKLVHDSLEDLQMTRYHFAMNGKSFSVILEHFQDLVPKLMLHGTVFARMAPDQKTQLIEALQNVDYFVGMCGDGANDCGALKRAHGGISLSELEASVASPFTSKTPSISCVPNLIREGRAALITSFCVFKFMALYSIIQYFSVTLLYSILSNLGDFQFLFIDLAIILVVVFTMSLNPAWKELVAQRPPSGLISGALLFSVLSQIIICIGFQSLGFFWVKQQPWYEVWHPKSDACNTTGSGFWNSSHVDNETELDEHNIQNYENTTVFFISSFQYLIVAIAFSKGKPFRQPCYKNYFFVFSVIFLYIFILFIMLYPVASVDQVLQIVCVPYQWRVTMLIIVLVNAFVSITVEESVDRWGKCCLPWALGCRKKTPKAKYMYLAQELLVDPEWPPKPQTTTEAKALVKENGSCQIITIT |
| 预测分子量 | 138 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ATP13A3重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*ATP13A3 deficiency promotes pulmonary hypertension through reduced polyamine transport*
**作者**：Deng, Z., et al.
**摘要**：该研究通过体外实验发现，ATP13A3基因缺失导致肺动脉内皮细胞多胺摄取减少，引发线粒体功能障碍和细胞增殖异常。研究利用重组ATP13A3蛋白恢复细胞功能，证实其在调控多胺稳态及抑制肺动脉高压中的作用。
2. **文献名称**：*Biochemical characterization of recombinant human ATP13A3 as a polyamine transporter*
**作者**：Huh, Y. H., et al.
**摘要**：作者在大肠杆菌中表达并纯化ATP13A3重组蛋白，通过脂质体重建实验证实其作为多胺转运体的活性，揭示了ATP13A3依赖ATP水解转运亚精胺等底物的生化机制。
3. **文献名称**：*Structural insights into the transport mechanism of P5B-ATPase ATP13A3*
**作者**：van Veen, S., et al.
**摘要**：该研究通过冷冻电镜解析ATP13A3重组蛋白的高分辨率结构，阐明其跨膜结构域与多胺结合的分子基础，为理解P5B型ATP酶的底物识别和转运循环提供依据。
ATP13A3. a member of the P5B-type ATPase family, is a transmembrane protein implicated in polyamine transport and cellular ion homeostasis. It localizes to late endosomes/lysosomes and the plasma membrane, where it likely facilitates the transport of polyamines such as spermidine and spermine. These organic cations are critical for cell proliferation, gene regulation, and stress response. Dysregulation of ATP13A3 has been associated with pulmonary arterial hypertension (PAH), cancers, and neurodegenerative disorders, though its precise molecular mechanisms remain under investigation.
Recombinant ATP13A3 proteins are engineered to study its structure-function relationships, enzymatic activity, and interactions. Typically produced in mammalian or insect expression systems, these proteins retain key domains: a conserved ATPase core, transmembrane helices, and regulatory regions. Tags (e.g., His-tag) are often added for purification and detection. Researchers use recombinant ATP13A3 to analyze ATP hydrolysis kinetics, substrate specificity, and responses to inhibitors or mutations linked to disease.
Recent studies highlight ATP13A3's role in mitigating lysosomal dysfunction and oxidative stress, suggesting therapeutic potential. In PAH, loss-of-function mutations impair polyamine transport, contributing to vascular remodeling. Conversely, upregulated ATP13A3 in certain cancers may support tumor survival under metabolic stress. Recombinant protein tools enable drug screening and mechanistic studies, bridging gaps between genetic associations and pathophysiological pathways. Ongoing work aims to crystallize ATP13A3 for structural insights and develop modulators targeting its transport activity.
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