| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRRG2 |
| Uniprot No | O14669 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-86aa |
| 氨基酸序列 | MRGHPSLLLL YMALTTCLDT SPSEETDQEV FLGPPEAQSF LSSHTRIPRA NHWDLELLTP GNLERECLEE RCSWEEAREY FEDNTL |
| 预测分子量 | 36 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PRRG2重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**: "Proline-rich Gla protein 2 (PRRG2) is a transmembrane proprotein convertase substrate"
**作者**: Kulczycka A, et al.
**摘要**: 该研究首次报道了PRRG2重组蛋白在哺乳动物细胞中的表达与加工，证实其作为跨膜蛋白可被前蛋白转化酶切割，并参与细胞外基质相关信号通路的调控。
2. **文献名称**: "Structural and functional characterization of recombinant PRRG2 extracellular domain"
**作者**: Zhang Y, et al.
**摘要**: 通过昆虫表达系统制备PRRG2胞外域重组蛋白，解析其晶体结构，揭示了其钙离子结合位点及与整合素相互作用的潜在机制，为研究其细胞黏附功能提供依据。
3. **文献名称**: "PRRG2 promotes tumor angiogenesis through VEGF signaling pathway"
**作者**: Li H, et al.
**摘要**: 利用重组PRRG2蛋白进行体外实验，证明其通过激活VEGFR2磷酸化促进内皮细胞迁移和血管生成，提示其在肿瘤微环境中的促血管生成作用。
注：上述文献为示例性内容，实际研究中建议通过PubMed或Web of Science以关键词"PRRG2 recombinant"或"PRRG2 expression"检索最新文献。若研究领域较新，可扩展检索至相关家族蛋白(如PRRG1/PRRG4)的功能研究。
PRRG2 (Proline Rich and Gla domain 2) is a transmembrane protein belonging to the proline-rich γ-carboxyglutamic acid (Gla) protein family, characterized by its unique structural domains and potential roles in cellular signaling. Encoded by the PRRG2 gene, this protein contains an extracellular proline-rich domain, a transmembrane region, and a cytoplasmic tail with tyrosine phosphorylation sites. Its N-terminal Gla domain, dependent on vitamin K-mediated γ-carboxylation, enables calcium-binding activity, suggesting involvement in calcium-dependent processes. PRRG2 is evolutionarily conserved across vertebrates, with homologs identified in mice (Prrg2) and zebrafish, reflecting its biological significance.
Functionally, PRRG2 is implicated in cell adhesion, migration, and signal transduction pathways. It interacts with Src family kinases through cytoplasmic tyrosine residues, potentially modulating intracellular signaling cascades. Emerging studies link PRRG2 to vascular biology and cancer progression, where its expression patterns show tissue-specific regulation. In endothelial cells, PRRG2 may influence vascular development, while in cancers like breast and colorectal carcinoma, altered PRRG2 expression correlates with tumor aggressiveness and metastasis, though its precise mechanistic role remains under investigation.
Recombinant PRRG2 proteins are engineered using expression systems (e.g., mammalian, insect, or bacterial cells) to study structure-function relationships. These purified proteins enable biochemical characterization, antibody development, and functional assays exploring ligand-receptor interactions. Research applications include elucidating PRRG2's role in pathological angiogenesis, tumor microenvironment modulation, and its potential as a diagnostic biomarker or therapeutic target. Current challenges involve resolving its endogenous ligands and clarifying contradictory findings about its pro- versus anti-tumor effects in different cancer contexts.
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