| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIPB |
| Uniprot No | Q9Y234 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-373aa |
| 氨基酸序列 | MLIPFSMKNCFQLLCNCQVPAAGFKKTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGKPILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTLLCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQIDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFIDIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNSKWNILCEKIKGIM |
| 预测分子量 | 42,4 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LIPB(脂酰转移酶)重组蛋白研究的模拟参考文献示例(非真实文献，供格式参考)：
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1. **文献名称**: *Cloning and Functional Characterization of LIPB in Escherichia coli*
**作者**: Smith J, et al.
**摘要**: 本研究通过基因克隆技术在大肠杆菌中表达重组LIPB蛋白，并验证其脂酰转移酶活性。结果表明，重组LIPB可催化脂肪酸与载体蛋白的酰化反应，为脂代谢研究提供工具。
2. **文献名称**: *Structural Analysis of Recombinant LIPB Using X-ray Crystallography*
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析了重组LIPB的三维结构，揭示其活性位点的关键氨基酸残基，为酶活性的分子机制及抑制剂设计奠定基础。
3. **文献名称**: *Optimization of LIPB Expression in Pichia pastoris for Industrial Applications*
**作者**: Wang Y, et al.
**摘要**: 在毕赤酵母系统中优化LIPB重组蛋白的分泌表达，提升酶产量及稳定性，探索其在工业生物催化中的潜在应用。
4. **文献名称**: *Role of LIPB in Bacterial Lipid Metabolism: Insights from Knockout Mutants*
**作者**: Gonzalez R, et al.
**摘要**: 通过构建LIPB基因缺失菌株，发现LIPB缺失导致细菌脂肪酸合成异常，证实其在脂代谢途径中的关键作用。
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**说明**：以上文献为模拟内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。若需具体领域文献，建议提供更详细的关键词或研究背景。
**Background of LIPB Recombinant Protein**
LIPB, a recombinant protein, is primarily associated with bacterial lipid metabolism and pathogenicity. It belongs to the lipase/esterase family, enzymes critical for hydrolyzing lipids into free fatty acids and glycerol, which serve as energy sources or signaling molecules. In pathogenic bacteria, such as *Mycobacterium tuberculosis* or *Staphylococcus aureus*, LIPB homologs are often linked to virulence, enabling the breakdown of host cell membranes or modulating immune responses.
The recombinant form of LIPB is engineered through genetic cloning, where the *lipB* gene is inserted into expression vectors (e.g., *E. coli* or yeast systems) to produce purified protein for research. This approach allows scalable production and functional studies without requiring native pathogen cultivation. Structurally, LIPB typically features a conserved alpha/beta-hydrolase fold and a catalytic triad (Ser-Asp-His) common to lipases, though its substrate specificity may vary across species.
Research on LIPB focuses on its role in bacterial survival and infection mechanisms. For instance, in *M. tuberculosis*, LipB (Rv0183) participates in the biosynthesis of phthiocerol dimycocerosates (PDIMs), complex lipids essential for cell wall integrity and evasion of host immunity. Inhibiting LIPB activity has been proposed as a therapeutic strategy to weaken bacterial resilience. Additionally, recombinant LIPB is utilized in immunological studies to develop diagnostics or vaccines, leveraging its antigenic properties.
Despite its potential, challenges remain in understanding its regulation, interaction with host systems, and applicability as a drug target. Advances in structural biology and proteomics continue to refine its functional characterization, highlighting LIPB as a molecule of interest in both basic microbiology and translational medicine.
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