TRAIP, Human, 重组蛋白 (His)
产品名称: TRAIP, Human, 重组蛋白 (His)
英文名称: TRAIP Protein, Human, Recombinant (His)
产品编号: TMPH-01270
产品价格: 20 μg
产品产地: 美国
品牌商标: TargetMol
更新时间: 2024-05-23T17:34:14
使用范围: null
规格 | 价格 |
1800.00 |
- 联系人 : 邵雪香
- 地址 : 上海市静安区江场三路238号8楼
- 邮编 : 200436
- 所在区域 : 上海
- 电话 : 150****4094 点击查看
- 传真 : 点击查看
- 邮箱 : sales@targetmol.com
- 二维码 : 点击查看
E3 ubiquitin ligase required to protect genome stability in response to replication stress. Acts as a key regulator of interstrand cross-link repair, which takes place when both strands of duplex DNA are covalently tethered together, thereby blocking replication and transcription. Controls the choice between the two pathways of replication-coupled interstrand-cross-link repair by mediating ubiquitination of MCM7 subunit of the CMG helicase complex. Short ubiquitin chains on MCM7 promote recruitment of DNA glycosylase NEIL3. If the interstrand cross-link cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on MCM7, promoting the unloading of the CMG helicase complex by the VCP/p97 ATPase, enabling the Fanconi anemia DNA repair pathway. Only catalyzes ubiquitination of MCM7 when forks converge. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: promotes ubiquitination of DPCs, leading to their degradation by the proteasome. Has also been proposed to play a role in promoting translesion synthesis by mediating the assembly of 'Lys-63'-linked poly-ubiquitin chains on the Y-family polymerase POLN in order to facilitate bypass of DNA lesions and preserve genomic integrity. The function in translesion synthesis is however controversial. Acts as a regulator of the spindle assembly checkpoint. Also acts as a negative regulator of innate immune signaling by inhibiting activation of NF-kappa-B mediated by TNF. Negatively regulates TLR3/4- and RIG-I-mediated IRF3 activation and subsequent IFNB1 production and cellular antiviral response by promoting 'Lys-48'-linked polyubiquitination of TNK1 leading to its proteasomal degradation.