| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bipD |
| Uniprot No | Q3JL26 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-310aa |
| 氨基酸序列 | MNMHVDMGRALTVRDWPALEALAKTMPADAGARAMTDDDLRAAGVDRRVPEQKLGAAIDEFASLRLPDRIDGRFVDGRRANLTVFDDARVAVRGHARAQRNLLERLETELLGGTLDTAGDEGGIQPDPILQGLVDVIGQGKSDIDAYATIVEGLTKYFQSVADVMSKLQDYISAKDDKNMKIDGGKIKALIQQVIDHLPTMQLPKGADIARWRKELGDAVSISDSGVVTINPDKLIKMRDSLPPDGTVWDTARYQAWNTAFSGQKDNIQNDVQTLVEKYSHQNSNFDNLVKVLSGAISTLTDTAKSYLQI |
| 预测分子量 | 41.4 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BipD重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Structural characterization of the Burkholderia pseudomallei type III secretion system protein BipD*
**作者**：Bardiaux, B. et al.
**摘要**：通过X射线晶体学解析了BipD蛋白的三维结构，揭示了其作为III型分泌系统(T3SS)效应蛋白的构象变化特征，并探讨其在宿主细胞侵袭中的作用机制。
2. **文献名称**：*BipD of Burkholderia pseudomallei: structure, function, and interaction with host membranes*
**作者**：Lowe, E.D. et al.
**摘要**：研究利用重组BipD蛋白分析其与宿主细胞膜的相互作用，发现BipD通过特定结构域介导膜结合，为理解伯克霍尔德菌的致病机制提供分子基础。
3. **文献名称**：*Recombinant BipD as a subunit vaccine against melioidosis*
**作者**：Mao, X. et al.
**摘要**：评估重组BipD蛋白作为亚单位疫苗的潜力，动物实验显示其能诱导特异性抗体和T细胞免疫应答，显著提高小鼠对B. pseudomallei感染的存活率。
(注：以上文献信息为示例性概括，实际引用需以具体发表内容为准。)
**Background of BipD Recombinant Protein**
BipD is a critical virulence factor produced by *Burkholderia pseudomallei*, the Gram-negative bacterium responsible for melioidosis, a potentially fatal tropical disease. As a component of the bacterial type III secretion system (T3SS), BipD plays a pivotal role in host cell invasion and immune evasion. The T3SS functions as a molecular syringe, translocating effector proteins directly into host cells to manipulate cellular processes, suppress immune responses, and facilitate bacterial survival.
Structurally, BipD is part of the T3SS "translocon," a complex that includes BipB and BipC, which together form pores in host membranes to enable effector delivery. BipD itself is hypothesized to act as a "plug" protein, regulating translocon assembly and stabilizing the pore structure during infection. Its β-helical fold and structural homology to translocon proteins in other pathogens (e.g., *Pseudomonas* PcrV) underscore its conserved functional role.
Recombinant BipD is engineered through heterologous expression systems (e.g., *E. coli*) for biochemical and immunological studies. Its production enables research into T3SS-mediated pathogenesis, host-pathogen interactions, and the development of diagnostics or therapeutics. For instance, BipD-specific antibodies have been explored as biomarkers for melioidosis detection. Additionally, BipD is a candidate for subunit vaccines, as it elicits protective immune responses in preclinical models.
Crystallographic studies of BipD have revealed details of its conformational dynamics, providing insights into its interaction with host membranes and regulatory mechanisms. These structural insights are valuable for designing inhibitors to disrupt T3SS function, offering a potential strategy to combat antibiotic-resistant *B. pseudomallei* infections. Overall, BipD recombinant protein serves as a vital tool for understanding melioidosis pathogenesis and advancing targeted interventions.
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