| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRPM4 |
| Uniprot No | Q8TD43 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1214aa |
| 氨基酸序列 | MVVPEKEQSWIPKIFKKKTCTTFIVDSTDPGGTLCQCGRPRTAHPAVAMEDAFGAAVVTVWDSDAHTTEKPTDAYGELDFTGAGRKHSNFLRLSDRTDPAAVYSLVTRTWGFRAPNLVVSVLGGSGGPVLQTWLQDLLRRGLVRAAQSTGAWIVTGGLHTGIGRHVGVAVRDHQMASTGGTKVVAMGVAPWGVVRNRDTLINPKGSFPARYRWRGDPEDGVQFPLDYNYSAFFLVDDGTHGCLGGENRFRLRLESYISQQKTGVGGTGIDIPVLLLLIDGDEKMLTRIENATQAQLPCLLVAGSGGAADCLAETLEDTLAPGSGGARQGEARDRIRRFFPKGDLEVLQAQVERIMTRKELLTVYSSEDGSEEFETIVLKALVKACGSSEASAYLDELRLAVAWNRVDIAQSELFRGDIQWRSFHLEASLMDALLNDRPEFVRLLISHGLSLGHFLTPMRLAQLYSAAPSNSLIRNLLDQASHSAGTKAPALKGGAAELRPPDVGHVLRMLLGKMCAPRYPSGGAWDPHPGQGFGESMYLLSDKATSPLSLDAGLGQAPWSDLLLWALLLNRAQMAMYFWEMGSNAVSSALGACLLLRVMARLEPDAEEAARRKDLAFKFEGMGVDLFGECYRSSEVRAARLLLRRCPLWGDATCLQLAMQADARAFFAQDGVQSLLTQKWWGDMASTTPIWALVLAFFCPPLIYTRLITFRKSEEEPTREELEFDMDSVINGEGPVGTADPAEKTPLGVPRQSGRPGCCGGRCGGRRCLRRWFHFWGAPVTIFMGNVVSYLLFLLLFSRVLLVDFQPAPPGSLELLLYFWAFTLLCEELRQGLSGGGGSLASGGPGPGHASLSQRLRLYLADSWNQCDLVALTCFLLGVGCRLTPGLYHLGRTVLCIDFMVFTVRLLHIFTVNKQLGPKIVIVSKMMKDVFFFLFFLGVWLVAYGVATEGLLRPRDSDFPSILRRVFYRPYLQIFGQIPQEDMDVALMEHSNCSSEPGFWAHPPGAQAGTCVSQYANWLVVLLLVIFLLVANILLVNLLIAMFSYTFGKVQGNSDLYWKAQRYRLIREFHSRPALAPPFIVISHLRLLLRQLCRRPRSPQPSSPALEHFRVYLSKEAERKLLTWESVHKENFLLARARDKRESDSERLKRTSQKVDLALKQLGHIREYEQRLKVLEREVQQCSRVLGWVAEALSRSALLPPGGPPPPDLPGSKD |
| 预测分子量 | 134,3 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TRPM4重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Structure of the human TRPM4 ion channel in a closed state*
**作者**：Autzen, A.M., Myasnikov, A.G., Campbell, M.G., et al.
**摘要**：该研究通过冷冻电镜技术解析了人源TRPM4重组蛋白在关闭状态下的高分辨率三维结构，揭示了其钙离子依赖性门控机制及胞内结构域对通道活性的调控作用，为理解TRPM4的生理功能提供了结构基础。
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2. **文献名称**：*TRPM4 is a Ca²⁺-activated nonselective cation channel mediating cell membrane depolarization*
**作者**：Nilius, B., Prenen, J., Tang, J., et al.
**摘要**：作者利用重组TRPM4蛋白在异源表达系统中进行电生理学研究，证实TRPM4为钙离子激活的非选择性阳离子通道，其激活导致细胞膜去极化，并探讨了其在心血管疾病(如心律失常)中的潜在病理机制。
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3. **文献名称**：*Phosphorylation of TRPM4 modulates its activity in recombinant systems and immune cells*
**作者**：Launay, P., Cheng, H., Srivatsan, S., et al.
**摘要**：该研究通过体外重组表达TRPM4蛋白，发现其磷酸化修饰(如PKC依赖性磷酸化)可显著调控通道的钙离子敏感性和电流幅值，揭示了其在T细胞活化中的信号转导作用。
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4. **文献名称**：*Decavanadate inhibits the TRPM4 channel by targeting its cytoplasmic domain*
**作者**：Hofmann, T., Chubanov, V., Gudermann, T.
**摘要**：研究利用重组TRPM4蛋白进行药物筛选，发现十钒酸盐通过结合其胞内结构域抑制通道活性，为开发靶向TRPM4的抑制剂(如治疗脑缺血或心肌肥大)提供了新思路。
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以上文献涵盖TRPM4的结构解析、功能机制、调控方式及药物开发，均基于重组蛋白技术展开研究。
TRPM4 (Transient Receptor Potential Melastatin 4) is a calcium-activated, non-selective cation channel that plays a critical role in regulating cellular electrical activity and calcium signaling. It is permeable to monovalent cations like Na⁺ and K⁺ but impermeable to Ca²⁺, creating a unique feedback mechanism where intracellular Ca²⁺ activates TRPM4. which subsequently modulates membrane potential and Ca²⁺ oscillations. This channel is widely expressed in tissues such as the heart, immune cells, and the nervous system, influencing processes like vascular tone, insulin secretion, and T-cell activation.
Recombinant TRPM4 proteins are engineered to study the channel's structure, function, and regulatory mechanisms in controlled experimental systems. Produced through heterologous expression in cell lines (e.g., HEK293), these proteins retain key functional properties, enabling electrophysiological studies (patch-clamp) and biochemical analyses. Purification methods often involve affinity tags and detergent solubilization to isolate functional channels for structural biology, including cryo-EM studies that have revealed critical insights into its calcium-binding domains and gating mechanisms.
Research using recombinant TRPM4 has linked its dysregulation to cardiovascular diseases (arrhythmias, hypertension), neuroinflammatory conditions, and cancer metastasis. Mutations in TRPM4 are associated with inherited cardiac conduction disorders, making it a target for therapeutic intervention. Additionally, its role in pathological conditions like stroke and immune response modulation highlights its biomedical relevance. Recombinant TRPM4 tools are vital for screening potential drugs and understanding how post-translational modifications (phosphorylation, oxidation) or auxiliary proteins regulate its activity. These studies collectively advance our grasp of TRPM4’s dual role as a cellular sensor and effector in health and disease.
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