The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Protein concentration is above or equal to 0.05 mg/ml.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 8.00 Constituents: 0.31% Glutathione, 0.79% Tris HCl
Chromosome 1 open reading frame 166
E3 SUMO-protein ligase MUL1
E3 ubiquitin ligase
E3 ubiquitin protein ligase MUL1
E3 ubiquitin-protein ligase MUL1
Growth inhibition and death E3 ligase
Mitochondrial anchored protein ligase
mitochondrial E3 ubiquitin ligase 1
mitochondrial E3 ubiquitin protein ligase 1
Mitochondrial ubiquitin ligase activator of NFKB 1
Mitochondrial-anchored protein ligase
Putative NF kappa B activating protein 266
Putative NF-kappa-B-activating protein 266
RING finger protein 218
Exhibits weak E3 ubiquitin-protein ligase activity, but preferentially acts as a SUMO E3 ligase at physiological concentrations. 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.
Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.
Protein modification; protein ubiquitination. Protein modification; protein sumoylation.
Contains 1 RING-type zinc finger.
The zinc finger domain is required for E3 ligase activity.
Mitochondrion outer membrane. Peroxisome. Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome.