| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HVCN1 |
| Uniprot No | Q96D96 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-273aa |
| 氨基酸序列 | MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPTPVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAELILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVVSFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAAKIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN |
| 预测分子量 | 31,6 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HVCN1重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际引用需核实准确性)：
---
1. **文献名称**：*"HVCN1 voltage-sensing mechanism and proton permeation in immune cells"*
**作者**：Tombola F. et al. (2008)
**摘要**：通过重组表达HVCN1蛋白，结合电生理学与结构分析，揭示了其电压依赖性门控机制及在免疫细胞中的质子传导功能，为调控免疫反应提供分子基础。
2. **文献名称**：*"Recombinant HVCN1 channels modulate ROS production in phagocytes"*
**作者**：Capasso M. et al. (2010)
**摘要**：研究利用重组HVCN1蛋白在HEK293细胞中表达，证明其在吞噬细胞活性氧(ROS)生成中的关键作用，并验证了pH依赖性调控机制。
3. **文献名称**：*"Structural insights into HVCN1 proton channel assembly and function"*
**作者**：Ramsey S. et al. (2006)
**摘要**：通过重组HVCN1的晶体结构解析，阐明了其跨膜结构域与质子选择性滤器的分子特征，揭示了其在癌症微环境酸化中的潜在作用。
---
**注**：以上为示例文献，实际研究中需根据具体需求检索真实数据库(如PubMed、ScienceDirect)获取准确信息。若需进一步协助查找真实文献，请提供更多背景信息。
HVCN1 (Hydrogen Voltage-Gated Channel 1) is a proton-selective ion channel encoded by the *HCVN1* gene, primarily involved in regulating intracellular pH and membrane potential. Discovered in the early 2000s, it is expressed in immune cells (e.g., B lymphocytes, macrophages), sperm, and certain cancer cells. HVCN1 facilitates proton extrusion, counteracting cytoplasmic acidification during processes like phagocytosis, respiratory burst, or sperm capacitation. Its voltage-dependent gating and unique structure—featuring a conserved voltage-sensing domain and a selective pore—distinguish it from other ion channels. Dysregulation of HVCN1 is linked to immune disorders, neurodegeneration, and cancer progression, where its activity promotes tumor microenvironment acidification and metastasis.
Recombinant HVCN1 protein is produced via heterologous expression systems (e.g., HEK293 or *E. coli*), enabling studies on its biophysical properties, structure-function relationships, and therapeutic targeting. Purified recombinant HVCN1 retains native channel activity, allowing in vitro electrophysiological assays (patch-clamp) or proton flux measurements in lipid bilayers. Researchers use it to investigate inhibitors/activators for drug development, particularly in autoimmune diseases or cancers. Additionally, it serves as an antigen for antibody production or in structural biology (cryo-EM) to resolve conformational states. Its role in modulating ROS production in immune cells further underscores its relevance in inflammation research. Overall, recombinant HVCN1 is a critical tool for deciphering proton channel biology and translating findings into clinical applications.
×
