| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM33 |
| Uniprot No | P57088 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-247 aa |
| 活性数据 | MADTTPNGPQGAGAVQFMMTNKLDTAMWLSRLFTVYCSALFVLPLLGLHEAASFYQRALLANALTSALRLHQRLPHFQLSRAFLAQALLEDSCHYLLYSLIFVNSYPVTMSIFPVLLFSLLHAATYTKKVLDARGSNSLPLLRSVLDKLSANQQNILKFIACNEIFLMPATVFMLFSGQGSLLQPFIYYRFLTLRYSSRRNPYCRTLFNELRIVVEHIIMKPACPLFVRRLCLQSIAFISRLAPTVP |
| 分子量 | 54.4 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人TMEM33蛋白的3篇参考文献及其摘要的简明概述：
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1. **文献名称**: *Structural insights into human TMEM33 mediated ER membrane remodeling*
**作者**: Kors, S. et al.
**期刊**: *Nature Communications* (2023)
**摘要**: 通过冷冻电镜技术解析了人源TMEM33蛋白的结构，揭示其作为内质网(ER)膜重塑因子的作用机制。研究表明TMEM33通过调控膜曲率参与ER管状网络的形成，并可能与细胞器间膜接触位点的功能相关。
2. **文献名称**: *TMEM33 regulates cellular calcium homeostasis by modulating ER-mitochondria contacts*
**作者**: Shibata, Y. et al.
**期刊**: *Journal of Cell Biology* (2020)
**摘要**: 发现TMEM33通过与内质网-线粒体接触位点(MAMs)的互作调节钙离子稳态。敲低TMEM33导致线粒体钙摄取异常，影响细胞代谢与凋亡，提示其在疾病中可能的关键作用。
3. **文献名称**: *SARS-CoV-2 exploits cellular TMEM33 for viral entry and replication*
**作者**: Mathavarajah, S. et al.
**期刊**: *Cell Reports* (2021)
**摘要**: 揭示TMEM33在SARS-CoV-2感染中的关键角色，其通过结合病毒刺突蛋白促进病毒内吞及膜融合。抑制TMEM33显著降低病毒复制效率，为抗病毒治疗提供新靶点。
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**说明**：以上文献主要涵盖TMEM33的结构解析、细胞器互作机制及病理学功能，可根据需求进一步查阅原文。如需扩展，可关注其与自噬(如*PLOS Pathogens*相关研究)或癌症的关联领域。
TMEM33 (Transmembrane Protein 33) is a conserved eukaryotic transmembrane protein primarily localized to the endoplasmic reticulum (ER) membrane. It features multiple hydrophobic domains, suggesting a role in membrane structure or protein-protein interactions. Studies indicate TMEM33 is involved in regulating ER morphology and stress responses, potentially influencing autophagy and ER-associated degradation (ERAD). It interacts with proteins like SAR1B, a key component of the COPII vesicle coat, implicating it in ER-to-Golgi trafficking. TMEM33 also modulates membrane contact sites between the ER and other organelles, affecting lipid transfer and calcium signaling. Its dysregulation has been linked to diseases, including cancer and metabolic disorders. Recombinant human TMEM33 protein is commonly generated using heterologous expression systems (e.g., mammalian or insect cells) for structural and functional studies. Researchers use it to investigate its role in ER dynamics, cellular stress adaptation, and its potential as a therapeutic target. Recent cryo-EM studies have begun elucidating its 3D structure, advancing understanding of its mechanistic contributions to membrane biology and disease pathways.
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