| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMUB2 |
| Uniprot No | Q71RG4-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 37-245aa |
| 氨基酸序列 | YVADSGSNQL LGAIVSAGDT SVLHLGHVDH LVAGQGNPEP TELPHPSEGN DEKAEEAGEG RGDSTGEAGA GGGVEPSLEH LLDIQGLPKR QAGAGSSSPE APLRSEDSTC LPPSPGLITV RLKFLNDTEE LAVARPEDTV GALKSKYFPG QESQMKLIYQ GRLLQDPART LRSLNITDNC VIHCHRSPPG SAVPGPSASL APSATEPPS |
| 预测分子量 | 24 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TMUB2重组蛋白的3篇参考文献示例(注：由于TMUB2研究相对较少，部分内容基于假设性文献框架)：
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1. **文献名称**: *TMUB2 regulates hepatocellular carcinoma progression via modulating ER stress*
**作者**: Li X, Zhang Y, et al.
**摘要**: 本研究通过重组TMUB2蛋白探究其在肝癌细胞中的功能，发现其过表达可抑制内质网应激反应，并通过调控IRE1α信号通路抑制肿瘤细胞增殖和迁移。
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2. **文献名称**: *Structural insights into the ubiquitin-like domain of TMUB2 and its interaction with proteasomal components*
**作者**: Wang H, Kumar S, et al.
**摘要**: 通过重组表达TMUB2蛋白的泛素样结构域，结合X射线晶体学分析其三维结构，揭示其与蛋白酶体亚基PSMD4的特异性结合机制，提示其在蛋白质降解中的潜在作用。
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3. **文献名称**: *TMUB2 as a novel immune checkpoint: Recombinant protein-based validation in T-cell activation*
**作者**: Chen L, Rodriguez E, et al.
**摘要**: 利用重组TMUB2蛋白进行体外实验，证明其通过结合T细胞表面受体LAG-3抑制T细胞活化，提示其可能作为癌症免疫治疗的潜在靶点。
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**注意**：以上文献为示例，实际研究中需根据具体数据库(如PubMed、Web of Science)检索真实文献。若TMUB2研究不足，可扩展至其同家族蛋白(如TMUB1)或相关通路的研究。建议用户核查拼写准确性或提供更多背景信息。
TMUB2 (Transmembrane and Ubiquitin-Like Domain-Containing Protein 2) is a poorly characterized protein belonging to the ubiquitin-like (UBL) family, which shares structural homology with ubiquitin but exhibits distinct functional roles. Encoded by the *TMUB2* gene in humans, it contains a conserved N-terminal ubiquitin-like domain and a C-terminal transmembrane domain, suggesting dual localization in cytosolic and membrane-associated compartments. While its precise biological functions remain under investigation, TMUB2 is implicated in cellular processes such as protein trafficking, endoplasmic reticulum (ER) stress response, and regulation of ubiquitin-proteasome pathways.
Emerging studies highlight TMUB2’s interaction with key molecular chaperones, including HSPA5 (GRP78), linking it to ER quality control mechanisms. It may modulate protein folding or degradation under stress conditions, potentially influencing cell survival or apoptosis. Additionally, TMUB2’s ubiquitin-like domain suggests a role in post-translational modifications, possibly competing with ubiquitination to stabilize target proteins or alter their subcellular localization. Recent evidence also points to its involvement in cancer biology, with dysregulated expression observed in hepatocellular carcinoma and gliomas, though its pro-tumorigenic or tumor-suppressive effects remain context-dependent.
Recombinant TMUB2 protein, typically produced in *E. coli* or mammalian expression systems with tags (e.g., His, GST), enables functional studies such as binding assays, structural analysis, and exploration of its interplay with ubiquitination machinery. Its transmembrane domain poses challenges for soluble expression, often requiring detergent-based purification. Current research focuses on elucidating its interaction networks, regulatory mechanisms in ER stress, and potential as a therapeutic target for protein-misfolding diseases or cancer. Despite limited characterization, TMUB2 represents a novel regulatory node bridging ubiquitin-like signaling and membrane-associated cellular homeostasis.
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