纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TRIM48 |
Uniprot No | Q8IWZ4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-208 aa |
活性数据 | MNSGISQVFQ RELTCPICMN YFIDPVTIDC GHSFCRPCFY LNWQDIPILT QCFECIKTIQ QRNLKTNIRL KKMASLARKA SLWLFLSSEE QMCGIHRETK KMFCEVDRSL LCLLCSSSQE HRYHRHCPAE WAAEEHWEKL LKKMQSLWEK ACENQRNLNV ETTRISHWKA FGDILYRSES VLLHMPQPLN LALRAGPITG LRDRLNQF |
分子量 | 26.4 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. |
目前针对TRIM48蛋白的研究文献较少,可能该编号存在拼写误差(如TRIM28/TRIM24研究较多)。以下是依据TRIM家族蛋白研究模式的**推测性示例**,供参考:
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1. **文献名称**:TRIM48 regulates cell proliferation via ubiquitination of p53
**作者**:Chen L, et al.
**摘要**:研究发现TRIM48通过E3泛素连接酶活性介导p53蛋白的泛素化降解,抑制肿瘤细胞凋亡并促进结肠癌细胞增殖。这为癌症治疗提供了潜在靶点。
2. **文献名称**:Structural basis of TRIM48 in antiviral immunity
**作者**:Zhang Y, et al.
**摘要**:解析了TRIM48的三维结构,证明其通过RING结构域介导的泛素化通路增强Ⅰ型干扰素表达,抑制流感病毒复制。
3. **文献名称**:TRIM48 deficiency promotes neuronal differentiation
**作者**:Wang Q, et al.
**摘要**:在小鼠模型中,TRIM48敲除导致神经干细胞分化异常,证明其通过调控Notch信号通路影响神经发育。
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**注意**:以上内容为假设性描述,目前公开发表的文献数据库中未明确收录TRIM48的详细信息。建议核对编号准确性(如TRIM24/TRIM28等)或查阅最新预印本平台(如bioRxiv)。
TRIM48. a member of the tripartite motif (TRIM) protein family, is a relatively understudied protein implicated in diverse cellular processes. TRIM proteins typically contain a conserved N-terminal structure: a RING finger domain, one or two B-box domains, and a coiled-coil region, which collectively facilitate protein-protein interactions, ubiquitination, and regulatory functions. TRIM48 is encoded by the TRIM48 gene located on human chromosome 2 and is expressed in multiple tissues, though its physiological role remains unclear.
Functionally, TRIM48 is hypothesized to act as an E3 ubiquitin ligase, tagging target proteins for degradation via the ubiquitin-proteasome system. Emerging studies suggest potential involvement in cellular stress responses, nucleic acid sensing, and innate immunity pathways, similar to other TRIM family members like TRIM5 or TRIM25. However, experimental evidence supporting these roles is limited. Its C-terminal region may include a PRY/SPRY domain, which could mediate specific substrate recognition or macromolecular interactions.
Research on recombinant human TRIM48 (produced via heterologous expression systems) aims to unravel its structural features, enzymatic activity, and interaction networks. Challenges include elucidating its exact substrates, signaling partners, and relevance to diseases such as cancer or viral infections. Current knowledge gaps highlight the need for further biochemical and cellular studies to define TRIM48's biological significance and therapeutic potential.
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