Anti-MARCH5 / Membrane-associated RING finger protein 5

In 1X PBS, pH 7.4, with 0.09% sodium azide. Membrane-associated RING finger protein 5 (MARCH5), also known as MARCHF5, is involved in cellular processes that are essential for maintaining the homeostasis and integrity of the cell. It possesses a RING finger domain that allows it to function as an E3 ubiquitin ligase, mediating the ubiquitination and subsequent degradation of specific target proteins. One of the key functions of MARCH5 is its role in regulating the turnover of mitochondrial proteins. Studies have shown that MARCH5 targets a variety of mitochondrial proteins for ubiquitination, leading to their degradation by the proteasome. This process helps to maintain the quality control of mitochondria and ensures the proper functioning of these vital organelles. Furthermore, MARCH5 has been implicated in various cellular processes, including apoptosis, autophagy, and immune response. By targeting specific proteins for degradation, MARCH5 can regulate the signaling pathways that govern these processes, influencing cell survival, proliferation, and immunity. MARCH5 has also been linked to the development of certain diseases, such as Parkinson's disease and cancer. Dysregulation of MARCH5 expression or activity has been observed in these conditions. Protein function: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission and as an important regulator of immune response (PubMed:16874301, PubMed:17606867, PubMed:26246171, PubMed:31881323). Plays a crucial role in maintaining mitochondrial homeostasis by regulating the dynamics of mitochondria through the ubiquitination of key proteins involved in fission and fusion such as FIS1, DNM1L and MFN1 (PubMed:16874301, PubMed:17606867). Acts as a critical determinant of mitotic apoptosis through both MCL1- dependent and -independent pathways. Turns off persistent immune signaling by degrading oligomeric complexes of retinoic acid-inducible gene I/DDX58 and mitochondrial antiviral- signaling protein/MAVS formed upon RNA virus infection (PubMed:26246171, PubMed:31881323). Promotes STING-mediated type-I interferon production via 'Lys-63'-linked ubiquitination of STING1 thereby preserving its activity and preventing the formation of inactive STING1 polymers (PubMed:37916870). Plays also an essential role in the formation of PEX3-containing vesicles in the de novo biogenesis of peroxisomes from mitochondria (PubMed:39423820, PubMed:39423819). Acts as a regulator of NLRP3 inflammasome activation on the mitochondria by mediating the 'Lys-27'-linked polyubiquitination of NLRP3, positively regulating the NLRP3-NEK7 complex formation and NLRP3 oligomerization (PubMed:37575012). [The UniProt Consortium]