Anti-Human TRIM7 Antibody Pair

Product Description: Tripartite motif containing 7 (TRIM7) is an E3 ubiquitin ligase belonging to the TRIM protein family, characterized by a conserved RBCC motif comprising a RING finger, B-box domains, and a coiled-coil region, along with a variable C-terminal B30.2 domain that determines substrate specificity. TRIM7 localizes to both the nucleus and cytoplasm and mediates ubiquitination-dependent degradation of diverse protein substrates, thereby regulating multiple biological processes such as protein turnover, immune responses, and cellular signaling. Structurally, the crystal structure of its B30.2 domain has provided insights into its interaction with glycogenin-1, linking TRIM7 to glycogen biosynthesis. Functionally, TRIM7 plays paradoxical roles in infection by either promoting host defense or facilitating viral pathogenesis, and in cancer, it can act as both a tumor suppressor and promoter by influencing metastasis, apoptosis, and tumor immunity. Clinically, TRIM7 has been implicated as a potential biomarker and therapeutic target in diseases such as idiopathic pulmonary fibrosis and atherosclerosis. Protein Function: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration (PubMed:25851810, PubMed:32853985, PubMed:34062120). Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and NSP8 proteins (PubMed:34062120, PubMed:35982226). Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation (PubMed:35867826, PubMed:35893676, PubMed:35982226). Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (PubMed:25851810). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (By similarity). Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation (PubMed:32126128). Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1 (PubMed:32853985). Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation (PubMed:36067704) , (Microbial infection) Promotes Zika virus replication by mediating envelope protein E ubiquitination [The Uniprot Consortium]