| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | burs |
| Uniprot No | Q9VD83 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-173aa |
| 氨基酸序列 | MLRHLLRHENNKVFVLILLYCVLVSILKLCTAQPDSSVAATDNDITHLGDDCQVTPVIHVLQYPGCVPKPIPSFACVGRCASYIQVSGSKIWQMERSCMCCQESGEREAAVSLFCPKVKPGERKFKKVLTKAPLECMCRPCTSIEESGIIPQEIAGYSDEGPLNNHFRRIALQ |
| 预测分子量 | 19,2 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Burs重组蛋白(Bursicon相关研究)的示例参考文献(注：文献为示例性概括，非真实发表论文)：
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1. **标题**：*Recombinant Bursicon Protein Regulates Cuticle Sclerotization in Drosophila melanogaster*
**作者**：Smith A, et al.
**摘要**：研究利用大肠杆菌系统成功表达重组Bursicon蛋白，证实其通过激活cAMP信号通路调控果蝇表皮硬化过程，为昆虫发育分子机制提供新证据。
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2. **标题**：*Functional Characterization of Bursicon Receptor in Tribolium castaneum Using Recombinant Proteins*
**作者**：Li Y, Wang H.
**摘要**：通过昆虫细胞表达系统获得重组Bursicon及其受体(DLGR2)，证明其在赤拟谷盗(Tribolium)蜕皮后体壁扩展中的关键作用，并揭示受体-配体互作机制。
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3. **标题**：*Bursicon-Based Biopesticide Development: Expression and Bioactivity Assay*
**作者**：Chen X, et al.
**摘要**：开发植物表达系统生产重组Bursicon蛋白，验证其干扰害虫表皮发育的能力，为新型绿色农药的研发提供潜在靶点。
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4. **标题**：*Structural Analysis of Recombinant Bursicon Heterodimer by Cryo-EM*
**作者**：Zhang R, et al.
**摘要**：利用冷冻电镜解析Bursicon异源二聚体(Burs-α/Burs-β)的三维结构，揭示其与受体结合的活性位点，为设计靶向抑制剂奠定基础。
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**注**：以上文献为示例，实际研究需查询具体数据库(如PubMed、Web of Science)。Bursicon为昆虫神经肽激素，主要调控蜕皮后表皮硬化及行为变化。
Bursicon is a neurohormone critical in insect development, primarily involved in regulating post-ecdysial processes such as cuticle hardening (sclerotization) and wing expansion. It was first identified in the 1960s through studies on blowflies, but its molecular characterization emerged later. Bursicon is a heterodimeric cystine knot protein, composed of two subunits: bursicon α (burs α) and bursicon β (burs β), which are covalently linked via disulfide bonds. Both subunits belong to the cystine knot family, sharing structural similarities with vertebrate glycoprotein hormones like TGF-β.
The gene encoding bursicon was cloned in the early 2000s, revealing its evolutionary conservation across arthropods. Recombinant bursicon proteins are typically produced using heterologous expression systems, such as *E. coli* or insect cell lines, enabling functional studies. These recombinant forms retain biological activity, mimicking native bursicon's ability to bind to its receptor, a leucine-rich repeat-containing G protein-coupled receptor (LGR2 or rickets in *Drosophila*), and activate intracellular cAMP signaling pathways.
Research on recombinant bursicon has clarified its role beyond cuticle maturation, including involvement in neural plasticity, immune responses, and stress tolerance. Its application in pest control strategies is also explored, as disrupting bursicon signaling could impair insect development. However, challenges remain in understanding tissue-specific effects and interspecies functional variations. Overall, recombinant bursicon serves as a vital tool for dissecting molting-related mechanisms and developing targeted insect management approaches.
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