The TRIM (Tripartite Motif) family of proteins encompasses a diverse group of E3 ubiquitin ligases that are critically involved in various cellular processes, including intracellular signaling pathways, apoptosis, cell cycle regulation, and innate immunity. Characterized by the presence of a RING domain, one or two B-box domains, and a coiled-coil region, TRIM proteins function by facilitating the ubiquitination of target substrates, thereby marking them for degradation by the proteasome or altering their subcellular localization and activity. This ubiquitination process is essential for the regulated turnover of proteins, modulating signal transduction pathways and maintaining cellular homeostasis. The specificity and versatility of TRIM proteins allow them to play pivotal roles in antiviral defense, where they recognize and target viral proteins for degradation, and in the regulation of transcription factors and signaling molecules, influencing cell growth, differentiation, and response to stress.
The activation of TRIM proteins involves several layers of regulation, including post-translational modifications, subcellular localization, and protein-protein interactions. Phosphorylation, SUMOylation, and neddylation are among the post-translational modifications that can affect the E3 ligase activity of TRIM proteins, either by enhancing their ability to ubiquitinate substrates or by stabilizing the TRIM proteins themselves. The localization of TRIM proteins within the cell can also regulate their activity; for example, nuclear or cytoplasmic localization can determine the range of substrates available for ubiquitination. Furthermore, interactions with specific co-factors or substrates can modulate the activity of TRIM proteins, enabling them to respond dynamically to cellular signals and stress conditions. This intricate regulatory network ensures that TRIM proteins are activated in a context-dependent manner, allowing for precise control over protein ubiquitination and degradation pathways that are critical for cellular function and the immune response.
产品名称 | CAS # | 产品编号 | 数量 | 价格 | 应用 | 排名 |
---|---|---|---|---|---|---|
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
佛司可林能激活腺苷酸环化酶,提高细胞内的 cAMP 水平。升高的 cAMP 会激活 PKA,然后使 TRIM 磷酸化,从而有可能增强其 E3 泛素连接酶的活性。 | ||||||
IBMX | 28822-58-4 | sc-201188 sc-201188B sc-201188A | 200 mg 500 mg 1 g | $159.00 $315.00 $598.00 | 34 | |
IBMX是一种非特异性磷酸二酯酶抑制剂,可导致细胞内cAMP增加和PKA激活。激活的PKA可通过磷酸化间接增强TRIM的活性。 | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $40.00 $129.00 $210.00 $490.00 $929.00 | 119 | |
PMA是一种强效的PKC激活剂,可以调节PKC下游的信号通路。PKC介导的磷酸化通路可能会通过翻译后修饰增强TRIM的功能活性。 | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
EGCG 是一种具有抗氧化特性的激酶抑制剂。通过抑制某些激酶,EGCG 可减少竞争性信号传递,从而可能导致 TRIM 相关途径的活性增加。 | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
离子霉素是一种钙离子载体,可增加细胞内钙离子浓度,激活钙离子依赖性蛋白激酶,从而可能通过磷酸化增强TRIM的活性。 | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
冈田酸是蛋白磷酸酶PP1和PP2A的强效抑制剂,可导致细胞内磷酸化水平升高,并可能通过磷酸化依赖机制增强TRIM活性。 | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin 通过抑制 SERCA 泵破坏钙稳态,导致细胞膜钙增加,从而激活钙依赖性激酶,间接增强 TRIM 的活性。 | ||||||
D-erythro-Sphingosine-1-phosphate | 26993-30-6 | sc-201383 sc-201383D sc-201383A sc-201383B sc-201383C | 1 mg 2 mg 5 mg 10 mg 25 mg | $162.00 $316.00 $559.00 $889.00 $1693.00 | 7 | |
S1P 与其受体结合,激活细胞内信号级联,包括可能导致 TRIM 翻译后修饰和激活的信号级联。 |