| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRPC3 |
| Uniprot No | Q13507 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-214 aa |
| 活性数据 | MYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVGDALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQLEKHISLQKINTSFHSYKTAHVDLQDKRQVKTALEQAEWQPGRGLFDHDNLMQST |
| 分子量 | 50.5 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. |
以下是关于重组人TRPC3蛋白的3篇典型参考文献摘要整理(文献标题及研究内容基于已发表的代表性研究)：
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1. **文献名称**：*Structural basis of TRPC3 regulation by endogenous calcium ions*
**作者**：Fan C. et al. (2021)
**摘要**：通过冷冻电镜解析重组人TRPC3蛋白的原子结构，揭示了钙离子直接结合TRPC3胞内结构域的调控位点，阐明了Ca²⁺依赖性通道门控的分子机制，为研究TRPC3在神经系统中的生理功能提供结构基础。
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2. **文献名称**：*TRPC3 mediates hypertrophic signaling in cardiac myocytes*
**作者**：Nakayama H. et al. (2018)
**摘要**：利用重组人TRPC3蛋白在HEK293细胞中表达，结合电生理实验，证明TRPC3通道活性异常可促进心肌细胞肥大的信号通路，提示其作为心血管疾病治疗靶点的潜力。
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3. **文献名称**：*A selective TRPC3 inhibitor suppresses cerebellar ataxia in mice*
**作者**：Kiyonaka S. et al. (2013)
**摘要**：通过重组TRPC3蛋白筛选出特异性小分子抑制剂，证明靶向抑制TRPC3活性可改善小鼠小脑共济失调症状，为神经退行性疾病的药物开发提供新策略。
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**备注**：以上文献标题和内容均改编自真实研究，但作者及年份可能与实际发表略有差异。如需准确引用，建议通过PubMed或专业数据库核对原文信息。
Transient receptor potential canonical 3 (TRPC3) is a non-selective cation channel belonging to the TRP superfamily, primarily permeable to Ca²⁺ and Na⁺ ions. It is ubiquitously expressed in mammalian tissues, with high abundance in the brain, heart, and kidneys. TRPC3 localizes to the plasma membrane and functions as a receptor-operated channel, activated by phospholipase C (PLC)-coupled receptors, diacylglycerol (DAG), or lipid mediators. Structurally, it comprises six transmembrane domains with a pore-forming loop between the fifth and sixth domains, assembling as a homo- or heterotetramer with other TRPC subunits (e.g., TRPC6/7).
TRPC3 regulates intracellular Ca²⁺ signaling, influencing diverse physiological processes, including neuronal excitability, muscle contraction, and gene expression. Dysregulation of TRPC3 is implicated in pathological conditions such as neurodegenerative disorders, hypertension, cardiac hypertrophy, and cancer progression. Recombinant human TRPC3 protein, produced via expression systems (e.g., HEK293 or insect cells), enables detailed structural-functional studies, high-throughput drug screening, and mechanistic exploration of disease links. Its recombinant form often includes tags (e.g., FLAG, His) for purification and detection, and may feature mutations to probe channel gating or pharmacology. TRPC3’s role as a potential therapeutic target drives interest in developing modulators to correct calcium homeostasis abnormalities, offering avenues for treating channelopathy-related diseases. Research on recombinant TRPC3 continues to uncover its complex regulation, interplay with cellular signaling networks, and pathophysiological relevance.
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