| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ldcC |
| Uniprot No | P52095 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-713aa |
| 氨基酸序列 | MNIIAIMGPHGVFYKDEPIKELESALVAQGFQIIWPQNSVDLLKFIEHNPRICGVIFDWDEYSLDLCSDINQLNEYLPLYAFINTHSTMDVSVQDMRMALWFFEYALGQAEDIAIRMRQYTDEYLDNITPPFTKALFTYVKERKYTFCTPGHMGGTAYQKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGAEQSYIVTNGTSTSNKIVGMYAAPSGSTLLIDRNCHKSLAHLLMMNDVVPVWLKPTRNALGILGGIPRREFTRDSIEEKVAATTQAQWPVHAVITNSTYDGLLYNTDWIKQTLDVPSIHFDSAWVPYTHFHPIYQGKSGMSGERVAGKVIFETQSTHKMLAALSQASLIHIKGEYDEEAFNEAFMMHTTTSPSYPIVASVETAAAMLRGNPGKRLINRSVERALHFRKEVQRLREESDGWFFDIWQPPQVDEAECWPVAPGEQWHGFNDADADHMFLDPVKVTILTPGMDEQGNMSEEGIPAALVAKFLDERGIVVEKTGPYNLLFLFSIGIDKTKAMGLLRGLTEFKRSYDLNLRIKNMLPDLYAEDPDFYRNMRIQDLAQGIHKLIRKHDLPGLMLRAFDTLPEMIMTPHQAWQRQIKGEVETIALEQLVGRVSANMILPYPPGVPLLMPGEMLTKESRTVLDFLLMLCSVGQHYPGFETDIHGAKQDEDGVYRVRVLKMAG |
| 预测分子量 | 82.6 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 **ldcC重组蛋白** 的参考文献示例(内容基于典型研究主题的合理推测，实际文献需进一步验证)：
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1. **文献名称**: *"Functional Characterization of Recombinant LdcC in Acid Stress Response of Escherichia coli"*
**作者**: Sakurai, K. et al. (2015)
**摘要**: 研究通过重组表达大肠杆菌ldcC基因，证明其编码的赖氨酸脱羧酶在酸性条件下催化赖氨酸转化为尸胺，帮助细菌抵御低pH环境，并分析了酶活性调控机制。
2. **文献名称**: *"Crystal Structure and Substrate Specificity of LdcC: Insights into Bacterial Decarboxylase Mechanisms"*
**作者**: Schmidt, T. & Müller, V. (2018)
**摘要**: 通过X射线晶体学解析重组LdcC蛋白的三维结构，揭示其底物结合位点和催化残基，探讨了与其他细菌脱羧酶的功能差异及进化关系。
3. **文献名称**: *"Metabolic Engineering of E. coli Using Recombinant LdcC for Enhanced Cadaverine Production"*
**作者**: Lee, J. et al. (2020)
**摘要**: 利用重组LdcC优化大肠杆菌代谢通路，提高尸胺(工业化学品前体)的生物合成效率，评估了其在规模化发酵中的应用潜力。
4. **文献名称**: *"Regulatory Network of LdcC in Bacterial Polyamine Homeostasis"*
**作者**: Browning, D.F. et al. (2022)
**摘要**: 研究ldcC转录调控机制及其在细菌多胺平衡中的作用，发现重组LdcC表达受σ因子RpoS调控，并影响生物膜形成和毒力。
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**注**：以上文献为示例性内容，实际引用时需通过学术数据库(如PubMed、Web of Science)检索真实文献。如需具体文章，可提供更详细的研究背景或关键词进一步筛选。
**Background of LdcC Recombinant Protein**
The LdcC protein, a lysine decarboxylase encoded by the *ldcC* gene in *Escherichia coli*, plays a critical role in bacterial acid stress resistance. It catalyzes the decarboxylation of lysine into cadaverine, a polyamine that helps maintain intracellular pH homeostasis under acidic conditions. Unlike its inducible counterpart, LdcI, which is regulated by the acid response system, LdcC is constitutively expressed and contributes to baseline stress tolerance.
Recombinant LdcC refers to the protein produced through heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for functional and structural studies. Its recombinant production has facilitated detailed characterization of its enzymatic mechanisms, including dependency on pyridoxal-5'-phosphate (PLP) as a cofactor and its oligomeric structure. Studies reveal that LdcC forms a homohexamer, critical for its catalytic activity and stability.
Research on LdcC has broader implications. In biotechnology, it is explored for cadaverine biosynthesis, a precursor for bio-based polyamides (nylon alternatives) and pharmaceuticals. Additionally, understanding LdcC’s role in bacterial survival informs strategies to combat pathogenic strains reliant on similar acid resistance mechanisms. Structural insights from recombinant LdcC also aid in designing inhibitors targeting decarboxylase enzymes in infectious bacteria.
Overall, LdcC recombinant protein serves as a model for studying microbial stress adaptation and a tool for sustainable chemical production, bridging fundamental microbiology and industrial applications.
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