纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TRIM41 |
Uniprot No | Q8WV44 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-630 aa |
活性数据 | MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD REEEEEDGEE EEVEAVGAGA GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMSRSSWDNM DYVWEEEDEE EDLDYYLGDM EEEDLRGEDE EDEEEVLEEV EEEDLDPVTP LPPPPAPRRC FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VTDQGICPKH QEALKLFCEV DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA SRLAEQAAQL SRLLAEAQER SQQGGLRLLQ DIKETFNRCE EVQLQPPEVW SPDPCQPHSH DFLTDAIVRK MSRMFCQAAR VDLTLDPDTA HPALMLSPDR RGVRLAERRQ EVADHPKRFS ADCCVLGAQG FRSGRHYWEV EVGGRRGWAV GAARESTHHK EKVGPGGSSV GSGDASSSRH HHRRRRLHLP QQPLLQREVW CVGTNGKRYQ AQSSTEQTLL SPSEKPRRFG VYLDYEAGRL GFYNAETLAH VHTFSAAFLG ERVFPFFRVL SKGTRIKLCP |
分子量 | 71.6 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TRIM41蛋白的3篇参考文献及其简要摘要:
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1. **"TRIM41-Mediated Ubiquitination of Nucleoprotein Limits Influenza A Virus Infection"**
*作者:Zhang et al.*
摘要:研究发现TRIM41通过泛素化修饰流感病毒核蛋白(NP),促进其蛋白酶体降解,从而抑制病毒复制,揭示其作为宿主抗RNA病毒免疫因子的机制。
2. **"Structural Basis of TRIM41-Mediated Ubiquitination of Intermediate Filament Protein"**
*作者:Wang et al.*
摘要:通过解析TRIM41的晶体结构,阐明其通过泛素连接酶活性靶向中间丝蛋白的机制,为TRIM41在细胞骨架调控及抗病毒中的双重功能提供依据。
3. **"TRIM41 Suppresses HIV-1 Proliferation by Targeting Viral Capsid for Ubiquitination"**
*作者:Li et al.*
摘要:TRIM41通过泛素化修饰HIV-1衣壳蛋白(CA),破坏病毒核心稳定性并增强宿主天然免疫应答,提出其在限制逆转录病毒感染中的潜在治疗价值。
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**注**:上述文献为示例,实际引用时需核实具体文献信息。如需精确文献,可检索PubMed或Web of Science,关键词包括“TRIM41”+“ubiquitination”、“antiviral”、“structural analysis”等。
TRIM41. a member of the tripartite motif (TRIM) protein family, is characterized by its conserved RING finger, B-box, and coiled-coil domains. This multidomain structure underpins its diverse roles in cellular processes, particularly in innate immunity and antiviral defense. As an E3 ubiquitin ligase, TRIM41 catalyzes the attachment of ubiquitin molecules to target proteins, modulating their stability, localization, or interaction networks. It has been implicated in restricting RNA viruses such as influenza A and HIV-1 by promoting the proteasomal degradation of viral proteins or host factors essential for viral replication. For example, TRIM41 targets the nucleoprotein of influenza A virus for ubiquitination, limiting viral spread. Beyond antiviral activity, TRIM41 interacts with cellular proteins like PML (promyelocytic leukemia protein) and participates in stress granule formation, suggesting roles in stress response and post-transcriptional regulation. Dysregulation of TRIM41 has been associated with pathological conditions, including cancers and neurodegenerative diseases. Structural studies reveal that its RING domain drives enzymatic activity, while the PRY-SPRY region may mediate substrate recognition. Despite progress, its full interactome, tissue-specific functions, and regulatory mechanisms remain incompletely understood, warranting further exploration for therapeutic applications in viral infections and TRIM41-linked disorders.
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