| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pucL |
| Uniprot No | O32141 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-494aa |
| 氨基酸序列 | MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA |
| 预测分子量 | 64.0 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 **pucL重组蛋白** 的3篇参考文献(基于模拟生成，非真实文献，仅供参考格式)：
---
1. **文献名称**: *Cloning and expression of the pucL gene encoding a light-harvesting complex subunit in Rhodobacter sphaeroides*
**作者**: Tadros, M.H., Waterkamp, K.
**摘要**: 研究报道了光合细菌 *Rhodobacter sphaeroides* 中 **pucL** 基因的克隆与重组表达，发现该基因编码的蛋白参与光合作用外周捕光复合体(LH2)的组装，重组蛋白在异源宿主中成功表达并保留光谱特性。
---
2. **文献名称**: *Functional analysis of the pucL protein in the regulation of bacterial photosynthesis*
**作者**: Drews, G., et al.
**摘要**: 通过构建 **pucL** 基因缺失突变体及重组蛋白回补实验，证明PucL蛋白对光合膜结构的稳定性及光能捕获效率具有关键作用，其重组形式可部分恢复突变体的光合缺陷。
---
3. **文献名称**: *Structural characterization of recombinant PucL protein from purple nonsulfur bacteria*
**作者**: Zsebo, K.M., Youvan, D.C.
**摘要**: 利用X射线晶体学解析了重组PucL蛋白的三维结构，揭示了其与细菌光合作用中色素分子结合的位点，为设计人工光能转化系统提供结构基础。
---
如需真实文献，建议在 **PubMed** 或 **Web of Science** 中以关键词“pucL recombinant protein”或“pucL gene function”检索。
PucL is a light-harvesting protein component primarily studied in photosynthetic bacteria, notably within the *Rhodobacter* genus, such as *Rhodobacter sphaeroides* and *Rhodobacter capsulatus*. It plays a critical role in the assembly and stability of the peripheral light-harvesting complex II (LHII), which is responsible for capturing solar energy and transferring it to the reaction center for conversion into chemical energy. The *pucL* gene is part of the *puc* operon, which encodes multiple polypeptides (e.g., PucA, PucB) that form the LHII complex’s structural framework. Unlike the core light-harvesting complex I (LHI), LHII absorbs longer wavelengths of light, expanding the organism’s spectral range for energy absorption in low-light conditions. PucL is essential for proper LHII oligomerization and integration into the bacterial photosynthetic membrane, though its exact mechanistic role—whether in pigment binding, membrane anchoring, or complex stabilization—remains under investigation.
Recombinant PucL production typically involves heterologous expression in *Escherichia coli*, where the protein is cloned into plasmid vectors under inducible promoters (e.g., T7 or araBAD). Affinity tags (e.g., His-tag) facilitate purification via chromatography. Challenges include ensuring proper folding and post-translational modifications, as PucL is a membrane-associated protein requiring lipid interactions for functionality. Researchers often employ detergent solubilization or cell-free systems to mimic native membrane environments. Studies on recombinant PucL aim to elucidate its structural dynamics using techniques like cryo-EM or X-ray crystallography, as well as its interactions with bacteriochlorophylls and carotenoids. Beyond basic research, engineered PucL variants hold potential in bioenergy (e.g., enhancing artificial photosynthesis) and biotechnology (e.g., biosensors). However, functional reconstitution of LHII *in vitro* remains technically demanding, necessitating further optimization of expression and purification protocols. Understanding PucL’s role advances synthetic biology efforts to design hybrid photosynthetic systems and improve solar energy harvesting efficiency.
×
