纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PRMT8 |
Uniprot No | Q9NR22 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 61-394 aa |
活性数据 | MSKLLNPEEMTSRDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMYHNKHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECSSISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWWENVYGFDMTCIRDVAMKEPLVDIVDPKQVVTNACLIKEVDIYTVKTEELSFTSAFCLQIQRNDYVHALVTYFNIEFTKCHKKMGFSTAPDAPYTHWKQTVFYLEDYLTVRRGEEIYGTISMKPNAKNVRDLDFTVDLDFKGQLCETSVSNDYKMR |
分子量 | 45.2 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. |
以下是关于重组人PRMT8蛋白的参考文献示例(部分为构造文献,实际引用时需核实):
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1. **Lacoste, N. et al.** (2012).
**"A conserved N-terminal motif regulates the activity of PRMT8. a type II arginine methyltransferase"**
*摘要*:研究揭示了PRMT8的结构特征及其N端自抑制结构域对酶活性的调控作用,利用重组蛋白阐明了其与PRMT家族其他成员的功能差异。
2. **Dillon, M.B. et al.** (2013).
**"Functional characterization of recombinant human PRMT8 reveals neuronal-specific substrate selectivity"**
*摘要*:通过体外酶活实验,发现重组PRMT8优先甲基化神经元相关蛋白(如HNRNP-K),并依赖磷脂结合激活,提示其在神经发育中的作用。
3. **Hamey, J.J. & Wilkins, M.R.** (2016).
**"PRMT8 Catalyzes Arginine Methylation of the ELAVL Family of RNA-Binding Proteins"**
*摘要*:利用重组PRMT8鉴定其与RNA结合蛋白(如HuR)的互作,揭示其通过精氨酸甲基化调控RNA代谢及神经元信号通路。
4. **Lee, K. et al.** (2020).
**"Expression and inhibitor screening of human PRMT8 in cancer cell models"**
*摘要*:报道了重组PRMT8在大肠杆菌中的高效表达及纯化方法,并通过高通量筛选发现新型小分子抑制剂,为靶向治疗提供依据。
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**注意**:以上文献及摘要内容部分为示例性构造,实际研究需查阅具体数据库(如PubMed、Google Scholar)确认。推荐以下关键词检索:`PRMT8 recombinant expression`, `PRMT8 substrate specificity`, `PRMT8 structure-function`。
Protein arginine methyltransferase 8 (PRMT8) is a member of the PRMT enzyme family that catalyzes the post-translational methylation of arginine residues in proteins. As a type I PRMT, it primarily generates ω-NG-monomethylarginine (MMA) and asymmetric ω-NG,NG-dimethylarginine (ADMA), influencing protein function, localization, and interactions. PRMT8 is uniquely expressed in mammals and shows predominant localization in the central nervous system (CNS), particularly enriched in neurons of the brain cortex, hippocampus, and cerebellum. Its expression peaks during early development, suggesting roles in neurogenesis, synaptic plasticity, and cognitive processes. Structurally, PRMT8 contains a conserved catalytic core shared among PRMTs but differs by an N-terminal myristoylation motif, enabling membrane association and distinct substrate targeting. Studies implicate PRMT8 in neuronal signaling pathways, including regulating dendritic spine morphology, neurotransmitter receptor trafficking, and synaptic protein methylation (e.g., CELF2. FMRP). Knockout mouse models exhibit behavioral abnormalities, such as impaired motor coordination and anxiety-like phenotypes, linking PRMT8 dysfunction to neurodevelopmental or psychiatric disorders. Emerging evidence also connects its dysregulation to glioblastoma and neuropathic pain. Despite progress, PRMT8’s precise substrates and CNS-specific regulatory mechanisms remain under exploration, highlighting its potential as a therapeutic target in neurological diseases.
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