| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | VD2 |
| Uniprot No | G8Z974 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1077aa |
| 氨基酸序列 | MRILLLSWLLFSSYFAIFLGISNLVLVSGQCRNDQKQLLLDLNLTSSSDLFIYPIPLGKLMKWNQAMECCSWDGVSCDGGGHVIGLDLSNRAISSSIDGSSSLFRLQHLQRLNLASNQFMTAFPAGFDKLENLSYLNLSNAGFTGQIPAKIPRLTRLITLDLSTDPFLSGEPLKLEKPNLEMLVQNLTRLRFLYLDGVNISAMGNEWCRALSPLTELQVLSMSNCYLSGPIHSSLSKLQSLSVICLDYNNLSASVPQFFAEFPNLTSLSLRSTGLNGRLPDEIFQIPTLQTLDLSYNMLLKGSFPNFPLNASLQALALSSTKFGGQIPESLDNLGQLTRIELAGCNFSGPIPKAVEKLTQLVSLDFSNNNFSGPIPSFSSSRNLTNLSLAHNKLVGTIHSTDWSSLSKLEDADLGDNKLSGTIPPTLFGIPSLQRLDLSHNQFNGSIGDFHDKASSLLNTLDLSNNKLKGQFPTPLFELRGLEILHLSSNNFSGLIPMNAFQNLGNLLSLDLSHNRLSIDATATNISLLSFPTFTGLGLASCNLTEFPGFLKNQSSLMYLDLSNNHIHGKIPDWIWKPIDLLRLNLSDNFLVGFERPVKNITSSVQIIDLHVNQLQGEIPIPTLDATYLDYSDNNFSSVLPAHIGDSLQRVSFFSISNNNIHGSIPPSICSSTSLRVLDLSNNSLSGPIPQCLFQMSGSLGVLDLRQNNLSGIISDTFSKSCKLQTLKLDQNRLEGKVPKSLGNCKMLEVLDIGNNQINDSFPWHLKNIAKLHVLVLRSNKFNGHIDCSGNNGGWSMLQIFDLASNNFSGKLHLTCLGTWDAMQHNPYSNLLELKHLHFVDSGSGGGTRYQDAITITTKGLELELVKILPVFTSIDISWNNFEGPIPEVIGKFKELHGLNFSHNAFTGPIPSSFGNLRELESLDLSSNSLRGEIPLQLANLNFLSCLNVSNNKLVGPIPTSTQLQSFPEASFENNAGLCGPPLKTKCGLPPGKEDSPSDSETGSIIHWNHLSIEIGFTFGLGIIIVPLIYWKRWRIWYFERIDLALSRLFPHLGRETKKHGRRAKQNQRGGPSNDWD |
| 预测分子量 | 118 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VD2重组蛋白的模拟参考文献示例(注：内容为虚构，仅供格式参考)：
1. **文献名称**: "Expression and Purification of Recombinant Vitamin D2-Binding Protein in E. coli"
**作者**: Zhang L, et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达重组维生素D2结合蛋白(VD2-BP)的方法，通过优化密码子使用和纯化步骤获得高纯度蛋白，并验证其与维生素D2的特异性结合能力，为相关诊断试剂开发奠定基础。
2. **文献名称**: "Structural Characterization of Recombinant VD2 Receptor and Its Role in Calcium Homeostasis"
**作者**: Gupta R, et al.
**摘要**: 通过X射线晶体学解析了重组VD2受体的三维结构，揭示其与维生素D2结合的活性位点，并证明该蛋白在调节肠道钙吸收中的关键作用，为代谢性疾病治疗提供新靶点。
3. **文献名称**: "Development of a VD2-Specific ELISA Using Recombinant Antigen"
**作者**: Tanaka K, et al.
**摘要**: 利用重组VD2蛋白作为包被抗原，建立了一种高灵敏度的ELISA检测方法，可特异性检测血清中的维生素D2水平，临床验证显示其与质谱法结果高度一致，适用于大规模筛查。
4. **文献名称**: "Comparative Analysis of Recombinant VD2 and VD3 Binding Affinity to Nuclear Receptors"
**作者**: Müller S, et al.
**摘要**: 研究比较了重组维生素D2和D3蛋白与核受体VDR的结合动力学，发现VD2亲和力较VD3低约30%，解释了二者在生物活性上的差异，为维生素D类似物设计提供依据。
**提示**：如需真实文献，建议在PubMed或Web of Science以“recombinant vitamin D2 protein”或“VD2-binding protein expression”为关键词检索，并筛选近年高被引研究。
**Background of VD2 Recombinant Protein**
Vitamin D2 (ergocalciferol) is a secosteroid critical for calcium homeostasis, bone health, and immune modulation. Unlike vitamin D3 (cholecalciferol), which is synthesized in human skin upon UV exposure, vitamin D2 is derived primarily from plant and fungal sources. Both forms require hepatic and renal hydroxylation to become biologically active (1.25-dihydroxyvitamin D). However, vitamin D2 has historically been used in fortified foods and supplements, particularly in regions where dietary sources or sunlight exposure are limited.
Recombinant protein technology enables the production of VD2-associated proteins, such as vitamin D-binding proteins (DBP) or enzymes involved in its metabolism (e.g., CYP24A1 or CYP27B1). These proteins are synthesized using genetically modified host systems (e.g., *E. coli*, yeast, or mammalian cells*), ensuring high purity and scalability. VD2 recombinant proteins are instrumental in studying vitamin D metabolism, receptor interactions (VDR), and its role in diseases like rickets, osteoporosis, and autoimmune disorders.
Recent advances focus on optimizing recombinant VD2-related proteins for therapeutic applications, including targeted delivery systems or as biomarkers to assess vitamin D status. Challenges remain in mimicking post-translational modifications critical for functionality, driving the preference for eukaryotic expression systems. Overall, VD2 recombinant proteins bridge gaps in both clinical research and biotherapeutic development, offering tools to address global vitamin D deficiency and related pathologies.
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