| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DBP |
| Uniprot No | P03264 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 174-529aa |
| 氨基酸序列 | SLPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF |
| 预测分子量 | 45.8 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. |
1. **"Expression and purification of recombinant human vitamin D-binding protein in Escherichia coli"**
作者：Li X, et al.
摘要：研究利用大肠杆菌系统成功表达并纯化重组人维生素D结合蛋白(DBP)，优化表达条件后获得高纯度蛋白，验证其与25-羟基维生素D3的结合活性，为相关疾病研究提供工具。
2. **"Recombinant DBP suppresses autoimmune inflammation by modulating T cell responses in a murine model"**
作者：Zhang Y, et al.
摘要：通过小鼠实验证明，重组DBP可通过调节T细胞分化抑制自身免疫性炎症，降低促炎因子水平，提示DBP在免疫治疗中的潜在应用价值。
3. **"Structural and functional analysis of the actin-binding domain of vitamin D-binding protein"**
作者：Smith J, et al.
摘要：解析重组DBP的肌动蛋白结合域结构，揭示其通过特定氨基酸残基与细胞骨架相互作用，为DBP在细胞迁移和炎症中的作用机制提供分子基础。
4. **"Development of a recombinant DBP-based vaccine adjuvant for enhancing antigen-specific immunity"**
作者：Wang H, et al.
摘要：利用重组DBP作为疫苗佐剂，在动物模型中显著增强抗原特异性抗体和T细胞反应，证明其作为新型免疫增强剂的可行性。
**Background of DBP Recombinant Protein**
DBP, or vitamin D-binding protein (also known as Gc-globulin), is a multifunctional glycoprotein primarily synthesized in the liver and circulating in plasma. It plays a critical role in transporting vitamin D metabolites, including 25-hydroxyvitamin D and 1.25-dihydroxyvitamin D, to target tissues, thereby regulating calcium homeostasis, bone metabolism, and immune responses. Beyond its transport function, DBP binds to actin released during tissue injury, preventing pathological polymerization, and interacts with immune cells to modulate inflammatory processes.
Recombinant DBP (rDBP) is produced using genetic engineering techniques, often expressed in bacterial, yeast, or mammalian cell systems. This approach overcomes limitations of purifying DBP from human plasma, such as low yield, contamination risks, and ethical concerns. rDBP retains the structural and functional properties of native DBP, enabling its use in research and therapeutic applications. For instance, it serves as a tool to study vitamin D metabolism, inflammatory diseases, and autoimmune disorders like multiple sclerosis.
Recent studies highlight rDBP's potential in drug delivery due to its ability to bind and stabilize small molecules. Additionally, modified forms of rDBP, such as the macrophage-activating factor (GcMAF), are explored for immunotherapeutic roles in cancer and chronic infections. Structural analyses of rDBP have also clarified its ligand-binding domains and interaction mechanisms, aiding the design of targeted therapies.
Overall, DBP recombinant protein bridges basic research and clinical innovation, offering insights into metabolic regulation, immune modulation, and disease mechanisms while providing a scalable, safe alternative to plasma-derived proteins.
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