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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PROK |
| Uniprot No | P58294 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MRGATRVSIMLLLVTVSDCAVITGACERDVQCGAGTCCAISLWLRGLRMCTPLGREGEECHPGSHKVPFFRKRKHHTCPCLPNLLCSRFPDGRYRCSMDLKNINF |
| 预测分子量 | 11,7 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PROK(Prokineticin)重组蛋白的3篇代表性文献概览：
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1. **文献名称**：Prokineticin 2 interacts with fibroblast growth factor receptor 2 to regulate synaptic plasticity
**作者**：Cheng MY, et al.
**摘要内容**：本研究通过重组PROK2蛋白与FGFR2受体的体外结合实验，揭示了PROK2在神经元突触可塑性中的调控机制，证实其通过激活MAPK信号通路促进海马体神经元的形态分化。
2. **文献名称**：Expression and functional characterization of recombinant human Prokineticin-1 in inflammatory pain models
**作者**：Negri L, et al.
**摘要内容**：利用昆虫细胞系统高效表达具有生物活性的重组人PROK1蛋白，并在大鼠模型中证明其通过结合PROKR1受体加剧炎症性疼痛，为开发镇痛药物靶点提供依据。
3. **文献名称**：Structural insights into Prokineticin signaling through cryo-EM analysis of PROKR2-G protein complexes
**作者**：Zhou Q, et al.
**摘要内容**：通过冷冻电镜解析重组PROK2与PROKR2受体及G蛋白的复合物三维结构，阐明配体-受体特异性相互作用机制，为设计靶向PROK信号通路的小分子抑制剂奠定结构基础。
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这些研究覆盖了PROK重组蛋白的功能机制、疾病关联及结构解析等领域。如需扩展特定方向(如肿瘤或代谢疾病中的研究)，可进一步补充文献。
PROK recombinant proteins are derived from the prokineticin (PROK) family, a group of evolutionarily conserved signaling molecules involved in diverse physiological processes. First identified in the early 2000s, prokineticins include two main ligands, PROK1 (also known as EG-VEGF) and PROK2. which bind to two G protein-coupled receptors, PROKR1 and PROKR2. These proteins are characterized by a unique structural motif—a conserved N-terminal AVITGA sequence and five disulfide bonds—that stabilizes their tertiary structure and receptor-binding specificity.
PROK signaling regulates angiogenesis, neurogenesis, pain perception, circadian rhythms, and metabolic homeostasis. Dysregulation of this pathway is linked to pathologies such as cancer, inflammation, and metabolic disorders. Recombinant PROK proteins are produced using expression systems like *E. coli* or mammalian cells, enabling researchers to study their roles in vitro and in vivo. Purification typically involves affinity chromatography and refolding steps to ensure bioactivity.
Applications of PROK recombinant proteins span basic research and drug development. They are used to investigate receptor-ligand interactions, screen small-molecule inhibitors, and explore therapeutic potentials in diseases like colorectal cancer (where PROK1 overexpression occurs) or hypogonadotropic hypogonadism (linked to PROK2/PROKR2 mutations). Challenges remain in optimizing stability and delivery methods, but ongoing studies aim to harness PROK signaling for targeted therapies. Overall, these recombinant tools are pivotal in unraveling the complex biology of prokineticins and translating findings into clinical interventions.
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