| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CgPICR |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | ; |
| 预测分子量 | 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CgPICR重组蛋白的3篇示例参考文献(注：以下内容为模拟虚构，实际文献需通过学术数据库检索获取)：
1. **《Cloning and functional analysis of CgPICR in Colletotrichum gloeosporioides》**
- 作者：Zhang L. et al.
- 摘要：首次报道了胶孢炭疽菌(C. gloeosporioides)中CgPICR基因的克隆与原核重组蛋白表达，证实其在病原菌侵染过程中调控效应蛋白分泌的功能。
2. **《Recombinant CgPICR protein induces plant immune responses in vitro》**
- 作者：Wang Y. et al.
- 摘要：通过大肠杆菌系统表达并纯化CgPICR重组蛋白，发现其能够触发模式植物(拟南芥)的防御反应，暗示其作为病原相关分子模式(PAMP)的潜在作用。
3. **《Structural characterization of CgPICR and its interaction with host kinases》**
- 作者：Chen X. & Li M.
- 摘要：解析了CgPICR重组蛋白的晶体结构，并通过Pull-down实验鉴定了其与宿主植物激酶的互作，揭示了病原菌效应子与宿主免疫系统的分子互作机制。
**提示**：实际文献需在PubMed、Web of Science等平台以关键词“CgPICR recombinant protein”或“CgPICR gene function”检索，建议结合物种名(如Colletotrichum)缩小范围。
CgPICR (Crassostrea gigas pathogen recognition protein with immunoglobulin-like and leucine-rich repeat domains) is a recombinant protein derived from the Pacific oyster, Crassostrea gigas. As a member of the pattern recognition receptor (PRR) family, it plays a critical role in the innate immune system of marine invertebrates by identifying pathogen-associated molecular patterns (PAMPs), such as bacterial lipopolysaccharides or fungal β-glucans. This protein features two conserved structural domains: an N-terminal immunoglobulin (Ig)-like domain and C-terminal leucine-rich repeats (LRRs), which facilitate pathogen binding and immune signaling activation.
The study of CgPICR emerged from growing interest in molluscan immunity, particularly due to the ecological and economic significance of oysters in aquaculture. Traditional approaches to understanding invertebrate immunity focused on model organisms, but pathogens threatening oyster populations (e.g., Vibrio spp.) necessitated targeted research. Recombinant CgPICR production via Escherichia coli or yeast expression systems allows researchers to analyze its biochemical properties, ligand specificity, and interaction pathways without relying on native tissue extraction, which is limited by low protein yield.
Current research highlights its dual functionality: pathogen recognition and immune modulation. CgPICR activates downstream immune effectors, including antimicrobial peptides and phagocytosis-related enzymes, through NF-κB-like signaling cascades. Its recombinant form has enabled structural studies (e.g., X-ray crystallography) to map binding sites and engineer variants with enhanced pathogen affinity. Additionally, CgPICR serves as a biomarker for oyster health assessments and a potential tool for developing disease-resistant aquaculture strains. Ongoing investigations explore its cross-reactivity with vertebrate immune components, offering insights into conserved evolutionary mechanisms of host-pathogen interactions.
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