|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. 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. 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. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.|
|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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