| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | dgcQ |
| Uniprot No | P76330 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 381-564aa |
| 氨基酸序列 | RRMVSNMYVLQSSLQWQAWHDTLTRLYNRGALFEKARPLAKLCQTHQHPFSVIQVDLDHFKAINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVILPGASLTEAAEVAERIRLKLNEKEMLIAKSTTIRISASLGVSSSEETGDYDFEQLQSLADRRLYLAKQAGRNRVFASDNA |
| 预测分子量 | 47.5 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dgcQ重组蛋白的3篇参考文献示例(注：内容为虚构，仅作格式参考)：
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1. **文献名称**: *Structural and functional analysis of the dgcQ-encoded diguanylate cyclase in Pseudomonas aeruginosa*
**作者**: Smith, J.R. et al.
**摘要**: 本研究解析了铜绿假单胞菌中dgcQ基因编码的双鸟苷酸环化酶(DGC)的晶体结构，揭示了其催化结构域的关键活性位点，并通过体外实验证明该酶参与调控细菌生物膜形成及运动性。
2. **文献名称**: *Heterologous expression and enzymatic characterization of recombinant DgcQ in E. coli*
**作者**: Zhang, L. et al.
**摘要**: 文章报道了dgcQ基因在大肠杆菌中的重组表达及纯化策略，测定了重组DgcQ蛋白的酶动力学参数(Km=2.3 μM，kcat=8.7 s⁻¹)，并证实其催化生成第二信使c-di-GMP的能力。
3. **文献名称**: *DgcQ-mediated c-di-GMP signaling regulates virulence in Vibrio cholerae*
**作者**: Gupta, S. et al.
**摘要**: 通过敲除和回补实验，发现霍乱弧菌DgcQ通过调控c-di-GMP水平影响毒素分泌和宿主细胞黏附，为开发针对细菌致病的抑制剂提供了潜在靶点。
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(注：以上文献信息为模拟生成，实际研究中请通过PubMed/Google Scholar等平台检索真实文献。)
**Background of dgcQ Recombinant Protein**
The dgcQ recombinant protein is derived from bacterial diguanylate cyclases (DGCs), a class of enzymes critical for synthesizing the secondary messenger cyclic di-GMP (c-di-GMP). C-di-GMP is a ubiquitous signaling molecule in bacteria that regulates key physiological processes, including biofilm formation, virulence, motility, and cell cycle progression. DGCs catalyze the synthesis of c-di-GMP from two GTP molecules via their conserved GGDEF domain. The dgcQ gene, often found in pathogenic and environmental bacteria, encodes one such DGC implicated in adapting bacterial behavior to environmental cues.
Recombinant dgcQ protein is produced through genetic engineering, where the dgcQ gene is cloned into expression vectors (e.g., plasmids) and expressed in heterologous hosts like *E. coli*. This allows large-scale purification of the protein for functional and structural studies. Researchers utilize recombinant dgcQ to investigate its enzymatic activity, regulatory mechanisms, and interactions with other cellular components. Its role in modulating c-di-GMP levels makes it a target for understanding bacterial pathogenicity and developing antimicrobial strategies.
Studies on dgcQ have revealed its potential as a biotechnological tool. For instance, engineered variants of DGCs are explored for synthetic biology applications, such as constructing biosensors or controlling biofilm dynamics in industrial fermentations. Additionally, structural analysis of dgcQ provides insights into the conformational changes required for catalysis, aiding in the design of inhibitors to disrupt c-di-GMP signaling in infectious bacteria.
Overall, dgcQ recombinant protein serves as a vital resource for both basic research and applied microbiology, bridging gaps between bacterial signaling pathways and practical interventions in medicine and biotechnology.
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