| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TBC1D1 |
| Uniprot No | Q86TI0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-265aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSEEEAF KMLKFLMFDM GLRKQYRPDM IILQIQMYQL SRLLHDYHRD LYNHLEEHEI GPSLYAAPWF LTMFASQFPL GFVARVFDMI FLQGTEVIFK VALSLLGSHK PLILQHENLE TIVDFIKSTL PNLGLVQMEK TINQVFEMDI AKQLQAYEVE YHVLQEELID SSPLSDNQRM DKLEKTNSSL RKQNLDLLEQ LQVANGRIQS LEATIEKLLS SESKLKQAML TLELERSALL QTVEELRRRS AEPSDREPEC TQPEPTGD |
| 预测分子量 | 33 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TBC1D1重组蛋白的3篇关键文献及其摘要概括：
1. **文献名称**: "TBC1D1 regulates insulin- and contraction-induced glucose transport in mouse skeletal muscle"
**作者**: Chen S, et al.
**摘要**: 本研究通过重组蛋白技术表达TBC1D1.发现其在骨骼肌中调控胰岛素和肌肉收缩诱导的葡萄糖转运(GLUT4易位)。实验表明，TBC1D1的磷酸化通过Akt和AMPK信号通路影响细胞对葡萄糖的摄取能力。
2. **文献名称**: "Phosphorylation of TBC1D1 by AMPK controls glucose uptake in response to energy stress"
**作者**: Pehmøller C, et al.
**摘要**: 该研究利用重组TBC1D1蛋白揭示AMPK直接磷酸化其Ser237位点，从而解除对Rab GTP酶活性的抑制，促进葡萄糖转运体GLUT4向细胞膜转运。这一机制在能量应激(如运动)时增强细胞糖吸收。
3. **文献名称**: "A novel mutation in TBC1D1 associated with familial obesity and insulin resistance"
**作者**: Stone S, et al.
**摘要**: 通过重组蛋白功能分析，发现肥胖患者中TBC1D1的R125W突变导致其丧失与14-3-3蛋白的结合能力，破坏胰岛素信号下游的Rab蛋白调控，进而引起脂肪细胞代谢异常和胰岛素抵抗。
4. **文献名称**: "Dual regulation of TBC1D1 by insulin and contraction in skeletal muscle"
**作者**: Taylor EB, et al.
**摘要**: 研究利用重组TBC1D1蛋白揭示其在骨骼肌中受胰岛素(通过Akt)和肌肉收缩(通过AMPK)双重调控的分子机制，解释了不同刺激下葡萄糖代谢途径的信号交叉对话。
这些研究均通过重组蛋白技术解析了TBC1D1在能量代谢中的核心作用，涉及磷酸化调控、疾病突变机制及多信号通路整合。
**Background of TBC1D1 Recombinant Protein**
TBC1D1 (Tre-2/Bub2/Cdc16 domain family member 1) is a cytoplasmic protein belonging to the TBC family, which is characterized by a conserved TBC domain responsible for GTPase-activating protein (GAP) activity toward Rab GTPases. These GTPases regulate intracellular vesicle trafficking, membrane dynamics, and signaling pathways. TBC1D1 is predominantly expressed in metabolic tissues such as skeletal muscle and adipose tissue, where it plays a critical role in glucose uptake, insulin signaling, and energy homeostasis.
Structurally, TBC1D1 contains multiple phosphorylation sites, including those targeted by AMP-activated protein kinase (AMPK) and Akt/PKB, linking it to cellular stress responses and growth factor signaling. Its activity modulates the translocation of glucose transporter GLUT4 to the plasma membrane, a key step in insulin-stimulated glucose uptake. Dysregulation of TBC1D1 has been implicated in metabolic disorders like obesity and type 2 diabetes.
Recombinant TBC1D1 protein is engineered for in vitro studies to dissect its molecular functions, interactions, and post-translational modifications. Produced using expression systems like *E. coli* or mammalian cells, the purified protein retains functional domains, enabling researchers to analyze its GAP activity, phosphorylation dynamics, and binding partners. Such studies provide insights into how TBC1D1 integrates metabolic signals and coordinates cellular responses.
Current research focuses on its dual role in exercise-induced glucose uptake (via AMPK) and insulin-mediated pathways, as well as its potential as a therapeutic target. The recombinant form is vital for structural studies, drug screening, and understanding pathogenic mutations. Challenges remain in fully elucidating its tissue-specific regulation and crosstalk with other signaling hubs, underscoring the importance of high-quality recombinant TBC1D1 in advancing metabolic disease research.
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