| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM27 |
| Uniprot No | Q9HBJ8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MLWLLFFLVTAIHAELCQPGAENAFKVRLSIRTALGDKAYAWDTNEEYLF KAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVE VQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVPIWIIIFGVI FCIIIVAIALLILSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDP LDMKGGHINDAFMTEDERLTPL |
| 预测分子量 | 52 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TMEM27重组蛋白的3篇模拟参考文献及其摘要概括(基于学术研究常见方向)：
---
1. **文献名称**: *TMEM27 is a novel regulator of β-cell surface identity and insulin secretion*
**作者**: Akpinar P, et al.
**摘要**: 本研究通过基因表达分析和功能实验，发现TMEM27作为跨膜蛋白在胰岛β细胞表面高表达，并调控胰岛素分泌。重组TMEM27蛋白的体外实验表明其通过稳定细胞间连接蛋白(如E-cadherin)增强β细胞功能，提示其与2型糖尿病病理相关。
2. **文献名称**: *Structural insights into the extracellular domain of TMEM27 and its interaction with collectrin*
**作者**: Zhang Y, et al.
**摘要**: 作者利用X射线晶体学解析了TMEM27胞外结构域的三维结构，发现其与collectrin(另一肾脏相关蛋白)具有相似结构域。重组TMEM27蛋白的结合实验显示其可能参与调节膜蛋白的稳定性，为研究其在肾脏和胰腺中的双重功能提供依据。
3. **文献名称**: *TMEM27 deficiency exacerbates metabolic stress in diabetic mouse models*
**作者**: Ito T, et al.
**摘要**: 通过构建TMEM27基因敲除小鼠模型，研究发现其在高脂饮食诱导下出现更严重的胰岛素抵抗和β细胞凋亡。重组TMEM27蛋白治疗可部分逆转代谢异常，表明其作为糖尿病潜在治疗靶点的价值。
---
**注**：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science检索真实文献(关键词：TMEM27 recombinant protein, β-cell, diabetes)。TMEM27的研究多集中于其在胰岛素分泌和肾脏功能中的调控作用，重组蛋白常用于结构、互作蛋白或治疗开发研究。
**Background of TMEM27 Recombinant Protein**
TMEM27 (Transmembrane Protein 27) is a cell surface protein predominantly expressed in pancreatic β-cells, where it plays a role in regulating β-cell function and mass. Initially identified as a type I transmembrane protein, TMEM27 consists of an extracellular domain, a single transmembrane helix, and a short cytoplasmic tail. Studies suggest it undergoes proteolytic cleavage by ADAM family proteases, releasing a soluble ectodomain into circulation. This soluble form has been proposed as a potential biomarker for β-cell mass in diabetes research.
TMEM27 is implicated in β-cell proliferation, survival, and insulin secretion. Knockdown or genetic ablation of TMEM27 in animal models results in reduced β-cell mass and impaired glucose tolerance, highlighting its importance in glucose homeostasis. Its extracellular domain may interact with unidentified ligands or receptors to modulate intracellular signaling pathways, though the precise mechanisms remain under investigation.
The recombinant TMEM27 protein, typically produced in mammalian or bacterial expression systems, retains the functional extracellular domain. This recombinant form is widely used in vitro and in vivo to study TMEM27’s biological roles, including its effects on β-cell dynamics and interactions with signaling molecules. Additionally, it serves as a critical tool for developing diagnostic assays to quantify soluble TMEM27 in clinical samples, aiding diabetes monitoring and research.
Emerging evidence also links TMEM27 to diabetic nephropathy, suggesting broader roles beyond pancreatic β-cells. Further research is needed to clarify its multifunctional nature and therapeutic potential in metabolic diseases.
×
