| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPBP1 |
| Uniprot No | Q86WP2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 293-473aa |
| 氨基酸序列 | MRTDKKSEFLKALKRDRVEEEHEDESRAGSEKDDDSFNLHNSNSTHQERDINRNFDENEIPQENGNASVISQQIIRSSTFPQTDVLSSSLEAEHRLLKEMGWQEDSENDETCAPLTEDEMREFQVISEQLQKNGLRKNGILKNGLICDFKFGPWKNSTFKPTTENDDTETSSSDTSDDDDV |
| 预测分子量 | 36.8 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. |
以下是基于GPBP1重组蛋白研究的模拟参考文献示例(实际文献需通过学术数据库检索获取)：
1. **《Recombinant GPBP1 expression and kinase activity analysis in autoimmune disorders》**
- 作者：Chen L, et al.
- 摘要：研究利用大肠杆菌系统表达并纯化His标签的GPBP1重组蛋白，验证其激酶活性，发现其通过磷酸化特定底物参与系统性红斑狼疮(SLE)的发病机制。
2. **《Structural characterization of GPBP1 and its interaction with collagen IV》**
- 作者：Gupta R, et al.
- 摘要：通过哺乳动物细胞表达系统获得GPBP1重组蛋白，结合X射线晶体学解析其三维结构，揭示其与胶原IV的结合域，为靶向治疗Alport综合征提供结构依据。
3. **《GPBP1 recombinant protein promotes tumor angiogenesis in vitro》**
- 作者：Wang Y, et al.
- 摘要：构建GPBP1真核重组蛋白，发现其通过激活VEGF信号通路促进内皮细胞迁移和血管生成，提示其在结直肠癌转移中的潜在作用。
4. **《High-yield purification and functional screening of GPBP1 mutants》**
- 作者：Kim S, et al.
- 摘要：优化昆虫杆状病毒系统的GPBP1重组蛋白表达条件，开发高通量筛选方法鉴定影响蛋白稳定性的突变体，助力药物靶点开发。
---
**说明**：以上为模拟内容，实际研究中建议通过PubMed、Web of Science等平台检索关键词(如“GPBP1 recombinant protein”、“GPBP1 kinase”)，重点关注其分子功能、疾病关联及重组制备技术的研究。真实文献可能涉及更多实验细节，如Western blot验证、动物模型验证等。
**Background of GPBP1 Recombinant Protein**
GPBP1 (Glycogen Phosphorylase Brain Isoform 1) is a critical enzyme in glycogen metabolism, primarily expressed in the brain and involved in the regulation of energy homeostasis. It catalyzes the rate-limiting step of glycogen breakdown, releasing glucose-1-phosphate to meet cellular energy demands, particularly in neurons during high activity or stress. GPBP1 is one of three tissue-specific isoforms of glycogen phosphorylase, with its expression tightly linked to neural and glial functions. Dysregulation of GPBP1 has been implicated in neurological disorders, such as epilepsy and neurodegenerative diseases, as well as metabolic conditions, highlighting its physiological and pathological significance.
Recombinant GPBP1 protein is engineered using biotechnological approaches, often through heterologous expression in bacterial (e.g., *E. coli*) or mammalian cell systems. This allows large-scale production of the purified protein while retaining enzymatic activity. The recombinant form typically includes affinity tags (e.g., His-tag) to facilitate purification and detection. Structural studies using recombinant GPBP1 have provided insights into its catalytic mechanism, allosteric regulation, and interactions with inhibitors or modulators.
Applications of GPBP1 recombinant protein span *in vitro* assays to screen potential therapeutics targeting glycogen metabolism, antibody development for diagnostic purposes, and mechanistic studies of brain-specific energy dysregulation. Its use also extends to modeling diseases like Lafora epilepsy, where aberrant glycogen accumulation occurs. By enabling precise biochemical and functional analyses, recombinant GPBP1 serves as a vital tool for advancing research into metabolic and neurological disorders, with potential implications for drug discovery and therapeutic strategies.
(Word count: 249)
×
