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Recombinant Human TRIM25 Protein

  • 中文名: 重组人(TRIM25)蛋白
  • 别    名: E3 ubiquitin/ISG15 ligase TRIM25; EFP; Estrogen responsive finger Protein; Estrogen-responsive finger Protein; RING finger Protein 147; RNF 147; RNF147; TRI25; TRI25_HUMAN; TRIM 25; Trim25; Tripartite motif containing 25; Tripartite motif containing Prote
货号: PAX2000-12145
Price: ¥询价
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TRIM25
Uniprot NoQ14258
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-630 aa
活性数据MAELCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGSPYLC PQCRAVYQAR PQLHKNTVLC NVVEQFLQAD LAREPPADVW TPPARASAPS PNAQVACDHC LKEAAVKTCL VCMASFCQEH LQPHFDSPAF QDHPLQPPVR DLLRRKCSQH NRLREFFCPE HSECICHICL VEHKTCSPAS LSQASADLEA TLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ LQQEYTEMKA LLDASETTST RKIKEEEKRV NSKFDTIYQI LLKKKSEIQT LKEEIEQSLT KRDEFEFLEK ASKLRGISTK PVYIPEVELN HKLIKGIHQS TIDLKNELKQ CIGRLQEPTP SSGDPGEHDP ASTHKSTRPV KKVSKEEKKS KKPPPVPALP SKLPTFGAPE QLVDLKQAGL EAAAKATSSH PNSTSLKAKV LETFLAKSRP ELLEYYIKVI LDYNTAHNKV ALSECYTVAS VAEMPQNYRP HPQRFTYCSQ VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES RLGRNSASWC VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADKVHLM YKFRVDFTEA LYPAFWVFSA GATLSICSPK
分子量70.9 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.


参考文献

1. **"TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity"** by Gack, M.U. et al. (2007)

*摘要*:该研究揭示了TRIM25通过泛素化RIG-I的CARD结构域激活抗病毒信号通路(如IRF3),增强I型干扰素应答,在RNA病毒免疫中起关键作用。

2. **"Zika virus evades interferon-mediated restriction through NS2A-mediated degradation of TRIM25"** by Yuan, L. et al. (2015)

*摘要*:研究证明寨卡病毒蛋白NS2A通过诱导TRIM25降解,抑制RIG-I介导的抗病毒信号通路,阐明病毒逃逸宿主先天免疫的机制。

3. **"TRIM25 promotes the cell survival and growth of hepatocellular carcinoma through targeting p53 for ubiquitination"** by Zhang, Y. et al. (2016)

*摘要*:发现TRIM25通过泛素化降解肿瘤抑制因子p53.促进肝癌细胞的存活与增殖,提示其在癌症发生中的潜在作用。

4. **"Structural basis for ubiquitin-mediated antiviral signal activation by TRIM25"** by Sanchez, J.G. et al. (2014)

*摘要*:解析了TRIM25的RING结构域与泛素结合的结构机制,阐明其通过协同自泛素化激活RIG-I信号通路的分子基础。


背景信息

TRIM25 (tripartite motif-containing protein 25) is a member of the TRIM family, a group of proteins characterized by a conserved N-terminal motif comprising RING, B-box, and coiled-coil domains. Primarily located in the cytoplasm, TRIM25 functions as an E3 ubiquitin ligase, mediating post-translational protein modifications through ubiquitination. It plays a critical role in innate immunity, particularly in antiviral defense. A well-studied function involves its interaction with retinoic acid-inducible gene I (RIG-I), where TRIM25 catalyzes K63-linked ubiquitination of RIG-I, enabling its activation and subsequent signaling to induce type I interferon production during RNA virus infections, such as influenza and SARS-CoV-2.

Beyond immunity, TRIM25 regulates diverse cellular processes, including apoptosis, cell proliferation, and RNA metabolism. It binds RNA directly, influencing the stability or activity of viral and cellular RNAs. Dysregulation of TRIM25 is implicated in diseases; for instance, it acts as an oncogene in some cancers (e.g., breast cancer) by promoting estrogen receptor signaling or destabilizing tumor suppressors. Conversely, reduced TRIM25 expression correlates with impaired antiviral responses. Its dual roles in health and disease, structural versatility, and involvement in ubiquitin-dependent and -independent pathways make TRIM25 a compelling target for therapeutic research. Recent studies also explore its interactions with non-coding RNAs and potential roles in autoimmune disorders, underscoring its multifaceted biological significance.


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