| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VD3 |
| Uniprot No | O15528 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-508aa |
| 氨基酸序列 | MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSRLHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCRQRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPPALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPHWLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFREELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPSATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPAQFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQPEPGAAPVRPKTRTVLVPERSINLQFLDR |
| 预测分子量 | 56,5 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. |
以下是关于维生素D3(VD3)相关重组蛋白研究的参考文献示例(注：以下文献信息为模拟示例，实际引用请核对真实文献)：
---
1. **文献名称**: *"Recombinant Expression and Functional Characterization of Human CYP27B1 in Escherichia coli"*
**作者**: Smith J, et al.
**摘要**: 本研究利用大肠杆菌系统重组表达了人源CYP27B1(25-羟基维生素D3 1-α羟化酶)，验证了其催化25-羟基维生素D3转化为活性形式1.25-二羟基维生素D3的功能，为体外研究维生素D代谢机制提供了工具。
---
2. **文献名称**: *"Structural Analysis of the Vitamin D Receptor Ligand-Binding Domain by Recombinant Protein Crystallography"*
**作者**: Tanaka K, et al.
**摘要**: 通过重组技术表达并纯化了维生素D受体(VDR)的配体结合域，利用X射线晶体学解析了其与1.25-二羟基维生素D3的复合物结构，揭示了VD3与受体结合的关键分子机制。
---
3. **文献名称**: *"High-Yield Production of Recombinant Vitamin D-Binding Protein in Mammalian Cells and Its Role in Immune Modulation"*
**作者**: Chen L, et al.
**摘要**: 在哺乳动物细胞中高效表达了重组维生素D结合蛋白(DBP)，证实其可通过调节巨噬细胞活性增强维生素D3的抗炎作用，为免疫相关疾病的治疗提供了潜在靶点。
---
4. **文献名称**: *"Engineering a Thermostable Recombinant CYP2R1 for Vitamin D3 25-Hydroxylation in Industrial Applications"*
**作者**: Müller R, et al.
**摘要**: 通过蛋白质工程技术改造了重组CYP2R1(维生素D3 25-羟化酶)，提高了其热稳定性及催化效率，为工业化生产活性维生素D3代谢产物奠定了基础。
---
**注**：以上文献为示例，实际研究中建议通过PubMed、Web of Science等数据库检索关键词如“recombinant vitamin D3 protein”“CYP27B1 expression”“VDR structure”等获取真实文献。
**Background of VD3 Recombinant Protein**
Vitamin D3 (cholecalciferol) is a fat-soluble secosteroid essential for calcium homeostasis, bone metabolism, and immune regulation. Its biologically active form, 1.25-dihydroxyvitamin D3 (calcitriol), exerts effects by binding to the vitamin D receptor (VDR), a nuclear transcription factor regulating gene expression. Recombinant VD3-related proteins, such as the VDR or vitamin D-binding protein (DBP), are engineered using biotechnological platforms to study these pathways or develop therapeutics.
The production of VD3 recombinant proteins typically involves cloning target genes (e.g., *VDR* or *DBP*) into expression vectors, followed by transfection into host systems like *E. coli*, yeast, or mammalian cells. Post-expression, purification techniques (e.g., affinity chromatography) ensure high purity and functionality. Recombinant VDR, for instance, retains its ability to dimerize with retinoid X receptor (RXR) and bind DNA response elements, enabling research into vitamin D-dependent gene regulation. Similarly, recombinant DBP aids in studying vitamin D metabolite transport and immune modulation.
Applications span basic research, drug discovery, and diagnostics. Recombinant proteins are used to elucidate molecular mechanisms in diseases linked to vitamin D deficiency (e.g., osteoporosis, autoimmune disorders) or VDR dysfunction. They also serve as tools for high-throughput screening of VD3 analogs or DBP-targeted therapies. Additionally, recombinant enzymes like CYP27B1 (responsible for calcitriol synthesis) are leveraged to produce active vitamin D metabolites in vitro.
Advantages include batch consistency, scalability, and reduced ethical concerns compared to animal-derived proteins. Challenges remain in mimicking post-translational modifications in prokaryotic systems, often necessitating eukaryotic hosts. Overall, VD3 recombinant proteins are pivotal in advancing understanding of vitamin D biology and translational applications.
×
