| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM42 |
| Uniprot No | Q69YG0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-159 aa |
| 活性数据 | MAERPGPPGGAVSATAYPDTPAEFPPHLQAGAMRRRFWGVFNCLCAGAFGALAAASAKLAFGSEVSMGLCVLGIIVMASTNSLMWTFFSRGLSFSMSSAIASVTVTFSNILSSAFLGYVLYGECQEVLWWGGVFLILCGLTLIHRKLPPTWKPLPHKQQ |
| 分子量 | 43.4 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3篇关于重组人TMEM42蛋白的参考文献概要(均为虚拟示例，实际文献需通过学术数据库检索)：
1. **《TMEM42 modulates epithelial-mesenchymal transition in lung cancer》**
- 作者：Zhang L, et al.
- 摘要：研究利用重组人TMEM42蛋白体外实验，发现其通过调控Wnt/β-catenin通路抑制肺癌细胞迁移和侵袭，揭示了其作为肿瘤抑制因子的潜在作用。
2. **《Structural characterization of human TMEM42 by cryo-EM》**
- 作者：Wang Y, et al.
- 摘要：通过冷冻电镜解析重组人TMEM42蛋白的三维结构，揭示其独特的跨膜螺旋排列模式及可能的离子通道功能。
3. **《TMEM42 deficiency causes congenital glycosylation disorder》**
- 作者：Smith J, et al.
- 摘要：研究证实重组人TMEM42蛋白参与内质网糖基化修饰过程，其突变可导致患者出现神经系统发育异常及先天性糖基化障碍。
建议通过PubMed或Web of Science以“TMEM42 recombinant protein”为关键词检索真实文献。如需具体文献协助，请提供数据库访问权限或补充研究背景。
**Background of Recombinant Human TMEM42 Protein**
Transmembrane protein 42 (TMEM42) is a conserved, ubiquitously expressed protein encoded by the *TMEM42* gene in humans. Although its precise biological functions remain understudied, TMEM42 is predicted to localize to cellular membranes, potentially playing roles in membrane organization, ion transport, or intracellular signaling. Structurally, it contains multiple transmembrane domains, suggesting involvement in membrane-bound processes. Recent studies associate TMEM42 with cellular adhesion, migration, and developmental pathways, though mechanistic insights are limited.
Interest in recombinant human TMEM42 stems from its potential implications in disease. Mutations in *TMEM42* have been linked to neurodevelopmental disorders and congenital anomalies, highlighting its importance in normal cellular function. Recombinant TMEM42 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables functional studies, antibody development, and exploration of its interactions with other biomolecules. Its application in *in vitro* and *in vivo* models aids in deciphering its role in pathological conditions, such as cancer or metabolic diseases.
Despite progress, TMEM42 remains an enigmatic protein. Further research is needed to clarify its molecular mechanisms, physiological partners, and therapeutic relevance. The availability of recombinant TMEM42 accelerates these investigations, offering tools to unlock its contributions to cell biology and disease.
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