纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GFAP |
Uniprot No | P14136 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-432aa |
氨基酸序列 | MERRRITSAARRSYVSSGEMMVGGLAPGRRLGPGTRLSLARMPPPLPTRVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM |
预测分子量 | 57.3 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GFAP重组蛋白的3篇参考文献及简要摘要:
1. **文献名称**: "Production and characterization of recombinant human GFAP protein for antibody detection in autoimmune diseases"
**作者**: Smith J, et al.
**摘要**: 该研究通过大肠杆菌表达系统制备了重组人GFAP蛋白,并验证其用于检测患者血清中抗GFAP自身抗体的有效性,为自身免疫性星形胶质细胞病的诊断提供工具。
2. **文献名称**: "Structural insights into GFAP filament assembly using recombinant protein fragments"
**作者**: Chen L, et al.
**摘要**: 利用重组GFAP片段解析其纤维组装机制,发现特定结构域突变(如R79C)会导致异常聚集,解释了亚历山大病中GFAP异常沉积的分子基础。
3. **文献名称**: "Recombinant GFAP-based ELISA for monitoring astrocyte activation in neurodegenerative models"
**作者**: Wang Y, et al.
**摘要**: 开发基于重组GFAP的ELISA检测方法,定量分析阿尔茨海默病小鼠模型中星形胶质细胞活化水平,证实GFAP表达与神经炎症程度正相关。
*注:以上文献信息为示例性质,实际引用需以具体论文内容为准。建议通过PubMed或Web of Science检索关键词“recombinant GFAP”获取最新研究。*
Glial Fibrillary Acidic Protein (GFAP) is a type III intermediate filament protein predominantly expressed in astrocytes, the star-shaped glial cells of the central nervous system (CNS). As a key structural component, GFAP maintains cellular integrity, supports mechanical strength, and regulates astrocyte motility and signaling. Its expression is often upregulated in response to CNS injuries, neurodegenerative diseases (e.g., Alzheimer’s), and glial tumors, making it a biomarker for astrocyte activation and pathological states.
Recombinant GFAP proteins are engineered using genetic cloning techniques, where the GFAP gene is inserted into expression vectors (e.g., bacterial, mammalian, or insect cell systems) to produce purified protein for research and therapeutic applications. This approach enables scalable production of GFAP with high purity and consistency, overcoming limitations of isolating the protein directly from tissues. Recombinant variants may include tags (e.g., His-tag) for easier purification or specific mutations to study disease-linked isoforms, such as those associated with Alexander disease, a rare neurodegenerative disorder caused by GFAP mutations.
In research, recombinant GFAP aids in studying astrocyte biology, neuroinflammation, and blood-brain barrier dynamics. It is used to develop diagnostic tools (e.g., ELISA kits for detecting GFAP in cerebrospinal fluid or serum) and to screen therapeutics targeting astrocyte dysfunction. However, challenges persist in replicating post-translational modifications (e.g., phosphorylation) critical for GFAP’s native function, necessitating careful selection of expression systems. Despite these hurdles, recombinant GFAP remains vital for advancing neuroscience and precision medicine.
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