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Recombinant Human TRIM23 Protein

  • 中文名: 重组人(TRIM23)蛋白
  • 别    名: ADP ribosylation factor domain Protein 1; ADP-ribosylation factor domain-containing Protein 1; ARF domain Protein 1; ARFD1; E3 ubiquitin-Protein ligase TRIM23; GTP binding Protein ARD 1; GTP-binding Protein ARD-1; N-acetyltransferase ARD1 human homolog of
货号: PAX2000-12144
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TRIM23
Uniprot NoP36406
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-574 aa
活性数据MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA
分子量64.0 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

以下是3篇关于TRIM23蛋白的关键文献摘要概述:

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1. **文献名称**:*TRIM23 mediates virus-induced autophagy via activation of TBK1*

**作者**:Sparrer KMJ et al.

**摘要**:该研究发现TRIM23通过其泛素连接酶活性促进TANK结合激酶1(TBK1)的激活,进而启动抗病毒自噬反应,揭示其在先天免疫中协调自噬与抗病毒信号的作用机制。

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2. **文献名称**:*TRIM23 regulates angiogenesis through NF-κB and mTOR signaling in endothelial cells*

**作者**:Hatakeyama S et al.

**摘要**:研究证明TRIM23通过泛素化修饰调控内皮细胞中NF-κB和mTOR通路,影响血管生成,提示其在肿瘤微环境血管异常中的潜在治疗靶点价值。

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3. **文献名称**:*The E3 ligase TRIM23 links innate immune signalling to RNA virus infection by targeting MAVS*

**作者**:Zhao W et al.

**摘要**:本文阐明了TRIM23通过调控线粒体抗病毒信号蛋白(MAVS)的泛素化修饰,增强宿主对RNA病毒(如丙肝病毒)的免疫应答,揭示其在抗病毒信号通路中的关键调控角色。

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4. **文献名称**:*TRIM23 acts as a tumor suppressor in glioblastoma by regulating cell proliferation and apoptosis*

**作者**:Li Y et al.

**摘要**:该研究指出TRIM23在胶质母细胞瘤中通过抑制PI3K/AKT通路降低细胞增殖并诱导凋亡,其表达下调与患者不良预后相关,提示其作为抑癌基因的潜在机制。

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每篇文献涉及TRIM23的不同功能(自噬、血管生成、抗病毒、肿瘤抑制),覆盖细胞生物学及疾病关联方向。具体全文建议通过PubMed/Google Scholar检索标题获取。


背景信息

TRIM23 (Tripartite motif-containing protein 23), also known as ARD1 or ARF-binding protein, is a member of the TRIM protein family characterized by a conserved tripartite motif: a RING domain, one or two B-box domains, and a coiled-coil region. Unlike many TRIM proteins, TRIM23 uniquely harbors an additional ADP-ribosylation factor (ARF) domain at its C-terminus, enabling dual functionality as both an E3 ubiquitin ligase and a GTPase. This structural duality allows TRIM23 to engage in diverse cellular processes, including innate immunity, autophagy, and vesicular trafficking.

Initially identified for its role in regulating ARF-mediated signaling, TRIM23 has since been implicated in antiviral defense, particularly against RNA viruses like HSV-1. by modulating interferon pathways and promoting autophagic degradation of pathogens. It also participates in neuronal differentiation and cell cycle regulation through interactions with proteins such as p53 and PML bodies. Subcellularly, TRIM23 localizes to cytoplasmic puncta and membrane compartments, dynamically associating with Golgi structures.

Dysregulation of TRIM23 has been linked to neurodevelopmental disorders, cancers, and immune dysfunctions. Its E3 ligase activity facilitates ubiquitination of substrates, influencing protein stability and signaling cascades, while its GTPase domain contributes to membrane remodeling. Ongoing research aims to elucidate its tissue-specific roles and therapeutic potential in inflammatory and degenerative diseases.


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