| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VDR |
| Uniprot No | P11473 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-427aa |
| 氨基酸序列 | MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL RPKLSEEQQR IIAILLDAHH KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG DSSSSCSDHC ITSSDMMDSS SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE VFGNEIS |
| 预测分子量 | 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VDR(维生素D受体)重组蛋白的3篇参考文献示例及摘要概括：
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1. **文献名称**: *"Crystal Structure of the Vitamin D Receptor Ligand-Binding Domain in Complex with 1.25-Dihydroxyvitamin D3"*
**作者**: Rochel N, et al.
**摘要**: 本研究通过X射线晶体学解析了重组人VDR配体结合域与活性维生素D(1.25-(OH)2D3)复合物的三维结构，揭示了配体结合口袋的关键氨基酸残基及分子相互作用机制，为靶向VDR的药物设计提供了结构基础。
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2. **文献名称**: *"Recombinant Expression and Functional Characterization of the Human Vitamin D Receptor in Baculovirus-Insect Cell System"*
**作者**: Hsieh JC, et al.
**摘要**: 报道了利用杆状病毒-昆虫细胞系统高效表达重组人VDR蛋白的方法，验证了其与DNA响应元件及共激活因子的结合能力，证实重组蛋白在体外具有天然受体活性，适用于药物筛选及信号通路研究。
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3. **文献名称**: *"Engineering a Soluble Vitamin D Receptor for High-Throughput Ligand Screening"*
**作者**: Mizwicki MT, et al.
**摘要**: 通过基因工程技术改造VDR，获得可溶性重组蛋白并建立高通量配体筛选平台，用于发现新型维生素D类似物及拮抗剂，为代谢性疾病和癌症治疗提供潜在候选分子。
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4. **文献名称**: *"Functional Analysis of VDR Domains Using Recombinant Chimeric Receptors"*
**作者**: Thompson PD, et al.
**摘要**: 构建VDR与其它核受体的嵌合重组蛋白，通过功能实验揭示其DNA结合域和配体结合域在转录调控中的独立作用，阐明了VDR特异性信号传导的分子基础。
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以上文献均聚焦于重组VDR蛋白的制备、结构解析及功能应用，涵盖基础研究与转化医学方向。如需具体文献来源，建议通过PubMed或Web of Science检索标题及作者获取全文信息。
The vitamin D receptor (VDR) is a nuclear receptor superfamily protein that mediates the genomic and non-genomic actions of 1.25-dihydroxyvitamin D3. the biologically active form of vitamin D. Primarily expressed in target tissues like intestine, kidney, and bone, VDR regulates calcium-phosphorus homeostasis, cell differentiation, immune modulation, and metabolic processes. Structurally, VDR contains a DNA-binding domain (DBD) for gene interaction and a ligand-binding domain (LBD) that undergoes conformational changes upon vitamin D binding, enabling co-regulator recruitment for transcriptional regulation.
Recombinant VDR proteins are engineered using expression systems (e.g., E. coli, insect, or mammalian cells) to produce purified, functional receptor variants for research and therapeutic applications. Bacterial systems yield high quantities but lack post-translational modifications, while eukaryotic systems better mimic native human VDR structure. These recombinant proteins enable detailed studies of VDR-ligand interactions, structural dynamics, and signaling pathways through techniques like X-ray crystallography, ligand screening assays, and gene expression profiling.
Research using recombinant VDR has advanced understanding of vitamin D's role in diseases, including osteoporosis, autoimmune disorders, and cancer. It also facilitates drug discovery, particularly for developing VDR-targeted therapies with improved selectivity and reduced side effects. Additionally, recombinant VDR serves as a tool to investigate genetic polymorphisms affecting vitamin D responsiveness in diverse populations. By providing a standardized, scalable source of functional receptor protein, recombinant VDR technology continues to drive innovations in molecular endocrinology and precision medicine.
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