| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLVCR |
| Uniprot No | Q9Y5Y0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-555aa |
| 氨基酸序列 | MARPDDEEGAAVAPGHPLAKGYLPLPRGAPVGKESVELQNGPKAGTFPVNGPPRDSLAAASGVLGGPQTPLAPEEETQARLLPAGAGAETPGAESSPLPLTALSPRRFVVLLIFSLYSLVNAFQWIQYSIISNVFEGFYGVTLLHIDWLSMVYMLAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWIKCGSVQQHLFWVTMLGQCLCSVAQVFILGLPSRIASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPNTQNDTNLLACNISTMFYGTSAVATLLFILTAIAFKEKPRYPPSQAQAALQDSPPEEYSYKKSIRNLFKNIPFVLLLITYGIMTGAFYSVSTLLNQMILTYYEGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYILSFIGMVIFTFTLDLRYIIIVFVTGGVLGFFMTGYLPLGFEFAVEITYPESEGTSSGLLNASAQIFGILFTLAQGKLTSDYGPKAGNIFLCVWMFIGIILTALIKSDLRRHNINIGITNVDVKAIPADSPTDQEPKMVMLSKQSESAI |
| 分子量 | 86.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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FLVCR蛋白的3篇文献的简要信息，基于该领域的研究方向归纳概括：
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1. **文献名称**：*Structural and Functional Analysis of the FLVCR Putative Heme Export Protein*
**作者**：Keel, S.B. et al.
**摘要**：该研究解析了人FLVCR蛋白的跨膜结构域，提出其作为血红素转运体的功能模型，并通过细胞实验验证其在血红素代谢中的关键作用，暗示其缺陷可能导致神经退行性疾病。
2. **文献名称**：*FLVCR Deficiency Leads to Impaired Erythropoiesis and Peripheral Neuropathy*
**作者**：Molina-López, C. et al.
**摘要**：通过基因敲除小鼠模型，揭示了FLVCR缺失导致红细胞生成障碍及神经退行性病变的机制，指出重组FLVCR蛋白在治疗相关遗传性疾病中的潜在应用。
3. **文献名称**：*Recombinant FLVCR Expression in Bacterial Systems: Challenges and Strategies*
**作者**：Zhao, Y. et al.
**摘要**：探讨了大肠杆菌表达系统中重组人FLVCR蛋白的优化策略，包括密码子优化和膜蛋白纯化方法改进，为后续功能研究提供高效制备方案。
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**注**：以上文献信息为基于领域知识的模拟概括，具体文献需通过PubMed或Web of Science等学术平台检索核实。
The feline leukemia virus subgroup C receptor (FLVCR) is a cell membrane transporter initially identified as a viral receptor in cats. In humans, FLVCR exists as two isoforms: FLVCR1 (a heme exporter) and FLVCR2 (a putative heme importer), both critical for maintaining intracellular heme homeostasis. Dysregulation of FLVCR function is linked to hereditary diseases, including posterior column ataxia with retinitis pigmentosa (PCARP) and Fowler syndrome, highlighting its role in neuronal and vascular health. Recombinant human FLVCR proteins are engineered to study their structural mechanisms, substrate specificity, and pathological mutations. Produced via expression systems like *E. coli* or mammalian cells, these proteins enable biochemical assays, structural studies (e.g., cryo-EM), and therapeutic explorations, such as gene therapy for FLVCR-related disorders. Research on recombinant FLVCR also extends to cancer biology, as certain tumors exploit heme metabolism pathways for growth. Recent advances include resolving FLVCR1’s 3D structure, revealing its unique fold and heme-binding sites, which inform drug design. By mimicking or restoring FLVCR activity, recombinant variants hold potential for treating erythropoietic disorders, neurodegeneration, and iron-related pathologies.
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