| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | lldD |
| Uniprot No | A8A670 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-396aa |
| 氨基酸序列 | MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQGLGKELPAALAPMAKGNAA |
| 预测分子量 | 46.7kDa |
| 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3篇与 **lldD重组蛋白** 相关的文献示例(内容基于假设性研究场景，供参考)：
---
1. **文献名称**: *"Cloning, Expression, and Functional Characterization of the lldD Gene Encoding a Key Enzyme in Lactate Utilization in Escherichia coli"*
**作者**: Johnson, A. et al.
**摘要**: 本研究克隆并表达了来自大肠杆菌的lldD基因，编码依赖FAD的乳酸脱氢酶(lldD)。重组蛋白在E. coli中成功表达，并通过体外酶活实验证实其催化L-乳酸氧化为丙酮酸的功能，为研究细菌碳代谢途径提供依据。
2. **文献名称**: *"Efficient Purification and Biochemical Analysis of Recombinant lldD Protein for Industrial Applications"*
**作者**: Smith, R. & Patel, K.
**摘要**: 报道了一种基于His标签亲和层析的lldD重组蛋白高效纯化方法，并分析了其最适反应pH、温度及金属离子依赖性。结果显示，纯化的lldD在微好氧条件下活性最高，适用于生物技术中乳酸废料的转化。
3. **文献名称**: *"Structural Insights into the Catalytic Mechanism of lldD Dehydrogenase through X-ray Crystallography"*
**作者**: Chen, L. et al.
**摘要**: 通过X射线晶体学解析了lldD蛋白的三维结构(分辨率2.1 Å)，揭示了其FAD结合域和底物结合口袋的关键残基，为理性改造lldD以提升工业催化效率提供了结构基础。
---
**注**：以上文献为模拟示例，实际文献需通过数据库(如PubMed、Web of Science)检索。如需真实文献，可提供更具体的研究方向或关键词进一步筛选。
**Background of LldD Recombinant Protein**
The *lldD* gene encodes L-lactate dehydrogenase (LldD), a membrane-bound enzyme critical in microbial metabolic pathways, particularly in organisms like *Escherichia coli*. It catalyzes the oxidation of L-lactate to pyruvate, coupled with the transfer of electrons to the respiratory chain via flavin mononucleotide (FMN). This reaction is vital under aerobic conditions, enabling bacteria to utilize lactate as a carbon source for energy production.
Recombinant LldD protein is produced through heterologous expression systems, such as *E. coli* or yeast, to study its structure, function, and potential applications. Its recombinant form is often engineered with affinity tags (e.g., His-tag) for simplified purification. Research on LldD has gained traction due to its role in metabolic engineering and industrial biotechnology. For instance, modifying lactate utilization pathways via LldD can enhance microbial production of biofuels, organic acids (e.g., propionate, pyruvate), or pharmaceutical precursors.
Additionally, LldD’s involvement in redox balance makes it a target for optimizing synthetic biology chassis strains, improving their efficiency in anaerobic or microaerobic fermentations. Structural studies of recombinant LldD, including X-ray crystallography, have revealed insights into its FMN-binding domain and catalytic mechanism, guiding protein engineering efforts to enhance stability or activity.
Beyond industrial applications, LldD is studied in pathogenic bacteria (e.g., *Pseudomonas aeruginosa*) as a potential antimicrobial target, since lactate metabolism contributes to their survival in host environments. Overall, recombinant LldD serves as a versatile tool in both basic research and applied biotechnology, bridging gaps between microbial physiology, enzymology, and sustainable bioproduction.
×
