| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | nblA |
| Uniprot No | P35087 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-59aa |
| 氨基酸序列 | MLPPLPDFSLSVEQQFDLQKYRQQVRDISREDLEDLFIEVVRQKMAHENIFKGMIRQGS |
| 预测分子量 | 14.5 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3篇涉及nblA重组蛋白的相关文献摘要(人工归纳非原文)：
1. **《Functional analysis of NblA in phycobilisome degradation in Synechocystis sp. PCC6803》**
作者：Karradt A et al.
摘要：通过在大肠杆菌中重组表达蓝藻Synechocystis的nblA蛋白，验证其与藻胆体降解相关的蛋白酶互作机制，揭示其在氮饥饿条件下调控光合装置分解的关键作用。
2. **《Recombinant NblA from Anabaena sp. PCC7120 induces chloroplast degradation in vitro》**
作者：Lu X et al.
摘要：研究通过原核表达系统纯化获得重组NblA蛋白，发现其能直接引发植物叶绿体类囊体膜结构的解离，为利用该蛋白调控植物光合效率提供实验依据。
3. **《Crystal structure of NblA from Thermosynechococcus elongatus》**
作者：Sato M et al.
摘要：首次解析嗜热蓝藻nblA重组蛋白的晶体结构，揭示其α螺旋结构域与藻胆体结合的特异性位点，阐明其介导光系统损伤修复的分子基础。
注：实际文献需要根据具体研究背景通过Web of Science或PubMed检索，以上为基于领域知识的模拟归纳。
**Background of NblA Recombinant Protein**
NblA (Nitrogen starvation-induced protein A) is a small, regulatory protein initially identified in cyanobacteria, where it plays a critical role in responding to nutrient stress, particularly nitrogen limitation. Under nitrogen-deficient conditions, cyanobacteria degrade their light-harvesting complexes, called phycobilisomes, to reallocate resources. NblA acts as a key mediator in this process by facilitating the disassembly of phycobilisomes, enabling cells to adapt to environmental stress. Its function is conserved across photosynthetic organisms, making it a subject of interest in both basic and applied research.
Recombinant NblA protein is produced using genetic engineering techniques, typically through heterologous expression in *Escherichia coli*. The gene encoding NblA is cloned into an expression vector, transformed into bacterial hosts, and induced to produce the protein, which is then purified via affinity chromatography. This approach allows for large-scale production of soluble, functional NblA, enabling detailed biochemical and structural studies.
Research on recombinant NblA has provided insights into its molecular mechanisms, including its interaction with phycobilisome components and regulatory partners. Beyond its biological significance, NblA has potential biotechnological applications. For example, it could be engineered to optimize light-harvesting efficiency in synthetic biology systems or serve as a tool to study stress responses in photosynthetic organisms. Additionally, its role in pigment degradation may inform strategies for improving algal biofuel production under nutrient-scarce conditions.
Overall, NblA recombinant protein serves as a valuable model for understanding stress adaptation in photosynthetic organisms and offers avenues for innovation in bioenergy and environmental biotechnology.
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