|Application ||WB, E|
|Other Accession||Q4R7G8, NP_078820.2|
|Calculated MW||39800 Da|
|Antigen Region||272-301 aa|
|Other Names||Mitochondrial ubiquitin ligase activator of NFKB 1, 632-, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, Growth inhibition and death E3 ligase, Mitochondrial-anchored protein ligase, MAPL, Putative NF-kappa-B-activating protein 266, RING finger protein 218, MUL1, C1orf166, GIDE, MAPL, MULAN, RNF218|
|Target/Specificity||This MUL1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 272-301 amino acids from the C-terminal region of human MUL1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MUL1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||C1orf166, GIDE, MAPL, MULAN, RNF218|
|Function||Exhibits weak E3 ubiquitin-protein ligase activity (PubMed:18591963, PubMed:19407830, PubMed:22410793). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:18591963, PubMed:19407830, PubMed:22410793). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (PubMed:22410793). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830). Plays a role in the control of mitochondrial morphology by promoting mitchondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395). Likely to promote mitchondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May also be involved in the sumoylation of the membrane fission protein DNM1L (PubMed:18207745, PubMed:19407830). Inhibits cell growth (PubMed:18591963, PubMed:22410793). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (PubMed:23399697). Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (PubMed:23399697). Can mediate DDX58 sumoylation and disrupt its polyubiquitination (PubMed:23399697).|
|Cellular Location||Mitochondrion outer membrane; Multi-pass membrane protein. Peroxisome. Note=Transported in mitochondrion- derived vesicles from the mitochondrion to the peroxisome|
|Tissue Location||Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.|
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Provided below are standard protocols that you may find useful for product applications.
E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Laure, L., et al. FEBS J. 277(20):4322-4337(2010)
Braschi, E., et al. EMBO Rep. 10(7):748-754(2009)
Venkatesan, K., et al. Nat. Methods 6(1):83-90(2009)
Zhang, B., et al. Cell Res. 18(9):900-910(2008)
Zhang, H., et al. Biochem. Biophys. Res. Commun. 366(4):898-904(2008)
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