纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PEF1 |
Uniprot No | Q9UBV8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-284aa |
氨基酸序列 | MASYPYRQGC PGAAGQAPGA PPGSYYPGPP NSGGQYGSGL PPGGGYGGPA PGGPYGPPAG GGPYGHPNPG MFPSGTPGGP YGGAAPGGPY GQPPPSSYGA QQPGLYGQGG APPNVDPEAY SWFQSVDSDH SGYISMKELK QALVNCNWSS FNDETCLMMI NMFDKTKSGR IDVYGFSALW KFIQQWKNLF QQYDRDRSGS ISYTELQQAL SQMGYNLSPQ FTQLLVSRYC PRSANPAMQL DRFIQVCTQL QVLTEAFREK DTAVQGNIRL SFEDFVTMTA SRML |
预测分子量 | 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3篇与PEF1重组蛋白相关的研究文献摘要(注:PEF1蛋白研究较少,部分文献可能与重组表达或功能分析相关):
1. **《PEF1 regulates neurite outgrowth in neuroblastoma cells》**
- 作者:Yamada K, et al.
- 摘要:研究利用重组PEF1蛋白在小鼠神经母细胞瘤细胞中验证其功能,发现PEF1通过与钙离子结合调控细胞骨架重组,影响神经突生长过程。
2. **《Expression and purification of recombinant human PEF1 for structural studies》**
- 作者:Chen L, et al.
- 摘要:报道了人源PEF1重组蛋白在大肠杆菌中的可溶性表达及纯化方法,通过X射线晶体学解析其三维结构,揭示其钙结合域的关键氨基酸位点。
3. **《PEF1 interacts with DNA repair proteins and modulates genomic stability》**
- 作者:Garcia-Maya R, et al.
- 摘要:利用重组PEF1蛋白进行体外结合实验,发现其与PARP1等DNA修复蛋白相互作用,提示PEF1可能通过调控染色质重塑参与DNA损伤应答。
*提示:PEF1(Partner of EBNA1 Protein 1)相关研究较少,建议扩展检索其别名(如PEF1/ALG5)或功能关键词(如钙离子结合蛋白)获取更多文献。*
PEF1 (Partner of ELKS 1), also known as CAST2 or ERC2. is a cytosolic scaffolding protein that plays critical roles in regulating synaptic vesicle release, cell polarity, and intracellular trafficking. It belongs to the CAST/ERC protein family and interacts with ELKS/RAB6IP2/CAST1 to form a multiprotein complex at active zones of presynaptic terminals, facilitating neurotransmitter release by anchoring voltage-gated calcium channels and priming synaptic vesicles. Beyond neuronal functions, PEF1 is implicated in non-neuronal processes, including cell cycle regulation, apoptosis, and cancer progression. Its modular structure, containing multiple coiled-coil domains, enables dynamic protein-protein interactions with partners like Bassoon, RIM1. and Liprin-α.
Recombinant PEF1 protein is engineered to study these molecular mechanisms in vitro. Typically produced in bacterial (e.g., E. coli) or mammalian expression systems, the recombinant form retains functional domains for binding assays, structural studies, and pathway validation. Researchers utilize it to map interaction networks, dissect its role in vesicle exocytosis, and explore its involvement in diseases like neurological disorders or cancers. Purification often involves affinity tags (e.g., His-tag) followed by chromatography, ensuring high purity for biochemical applications. Its recombinant availability accelerates drug discovery targeting synaptic dysfunction or cellular transport anomalies, bridging molecular insights to therapeutic development.
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