人 TRIML1 抗体对
01AB01862
Tripartite motif family like 1 (TRIML1) is a nuclear protein belonging to the TRIM/RING E3 ligase family. It is characterized by a conserved N-terminal RING finger, B-box, and coiled-coil domains, which are indicative of E3 ubiquitin-protein ligase activity and zinc-binding capabilities. Although its specific substrates are not yet fully defined, functional studies suggest that TRIML1 is involved in early embryogenesis, particularly during the progression of the blastocyst stage and overall pre-implantation biology. Expression of TRIML1 is notably enriched in the testis and during early developmental phases. While it shares structural similarities with other TRIM family members involved in various cellular processes, its precise physiological roles and regulatory mechanisms continue to be elucidated.
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技术参数
- 靶点基因名
- TRIML1
- 基因别名
- RNF209
- 蛋白别名
- tripartite motif family like 1; TRIML1
- UniProt
- Q8N9V2
- 物种
- Human
产品详情
- 靶点名称
- TRIML1
- 蛋白名称
- tripartite motif family like 1
- 蛋白别名
- Probable E3 ubiquitin-protein ligase TRIML1; RING finger protein 209; RING-type E3 ubiquitin transferase TRIML1; Tripartite motif family-like protein 1
- 靶点基因名
- TRIML1
- 基因别名
- RNF209
- UniProt
- Q8N9V2
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Tripartite motif family like 1 (TRIML1) is a nuclear protein belonging to the TRIM/RING E3 ligase family. It is characterized by a conserved N-terminal RING finger, B-box, and coiled-coil domains, which are indicative of E3 ubiquitin-protein ligase activity and zinc-binding capabilities. Although its specific substrates are not yet fully defined, functional studies suggest that TRIML1 is involved in early embryogenesis, particularly during the progression of the blastocyst stage and overall pre-implantation biology. Expression of TRIML1 is notably enriched in the testis and during early developmental phases. While it shares structural similarities with other TRIM family members involved in various cellular processes, its precise physiological roles and regulatory mechanisms continue to be elucidated.