纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PIP |
Uniprot No | P12273 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 28-146aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSQDNTRKIIIKNFDIPKSVRPNDEVTAV LAVQTELKECMVVKTYLISSIPLQGAFNYKYTACLCDDNPKTFYWDFYTN RTVQIAAVVDVIRELGICPDDAAVIPIKNNRFYTIEILKVE |
预测分子量 | 16 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PIP(Phosphatidylinositol Phosphate)重组蛋白研究的3篇代表性文献摘要(注:以下内容为模拟虚构,仅作示例参考):
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1. **文献名称**:*Recombinant PIP5K1A regulates membrane dynamics in cancer cell migration*
**作者**:Chen L, et al.
**摘要**:研究通过大肠杆菌表达系统成功纯化重组人PIP5K1A蛋白(磷脂酰肌醇-4-磷酸5-激酶),并证明其通过催化PIP2生成参与细胞膜重塑,促进乳腺癌细胞侵袭迁移,为靶向PIP信号通路治疗癌症提供依据。
2. **文献名称**:*Structural and functional analysis of plant PIP2 aquaporins under drought stress*
**作者**:Wang Y, et al.
**摘要**:利用昆虫细胞体系重组表达拟南芥PIP2水通道蛋白,解析其晶体结构,发现干旱胁迫下PIP2通过构象变化增强水分运输效率,揭示了植物抗旱分子机制。
3. **文献名称**:*High-yield production of bioactive PIP3 phosphatase via yeast expression*
**作者**:Garcia-Ruiz E, et al.
**摘要**:开发酿酒酵母表达系统高效生产重组人PTEN蛋白(PIP3磷酸酶),验证其酶活性和对AKT信号通路的抑制作用,为肿瘤药物筛选提供稳定蛋白来源。
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*注:实际文献需通过PubMed/Google Scholar检索关键词"recombinant PIP protein"或结合具体PIP亚型(如PIP2/PIP3/PIP5K等)进行筛选。*
**Background of PIP Recombinant Proteins**
PIP (Prostatic Inflammatory Protein) recombinant proteins are engineered versions of naturally occurring proteins associated with prostate physiology and pathology. Originally identified for their role in prostate inflammation and infection, PIPs belong to the antimicrobial peptide family and exhibit immunomodulatory properties. Their expression is often dysregulated in prostate diseases, including prostatitis and prostate cancer, making them potential biomarkers or therapeutic targets.
Structurally, PIPs are small, secreted proteins characterized by conserved domains that enable interactions with immune cells or microbial membranes. Recombinant PIPs are produced using biotechnological methods, such as *E. coli* or mammalian expression systems, to ensure proper folding and post-translational modifications. This allows large-scale production for research and clinical applications.
Functionally, PIP recombinant proteins are studied for their dual roles in innate immunity and disease progression. They demonstrate antimicrobial activity against pathogens like *E. coli* and *Pseudomonas aeruginosa*, common culprits in urinary tract infections. Conversely, chronic overexpression of certain PIP isoforms has been linked to tumor microenvironment modulation, potentially promoting prostate cancer cell survival or metastasis.
In research, PIP recombinant proteins are utilized to dissect signaling pathways in inflammation and cancer, screen drug candidates, or develop diagnostic assays. Clinically, they hold promise as therapeutic agents for resistant infections or as vaccine components. However, challenges remain in optimizing stability, delivery, and minimizing off-target effects.
Overall, PIP recombinant proteins bridge basic science and translational medicine, offering insights into prostate biology while paving the way for novel diagnostics and therapies in urology and oncology.
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