Background:

The zinc finger domain is required for E3 ligase activity.,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.,pathway:Protein modification; protein ubiquitination.,Contains 1 RING-type zinc finger.,subcellular location:Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome.,subunit:Homooligomer. Interacts with MAP3K7/TAK1.,tissue specificity:Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.,

Classification:

Primary antibody

Alternative names:

Mitochondrial ubiquitin ligase activator of NFKB 1 ;EC 6.3.2.-;E3 SUMO-protein ligase MUL1;E3 ubiquitin-protein ligase MUL1;Growth inhibition and death E3 ligase;Mitochondrial-anchored protein

Species reactivity:

Human, Mouse

Host:

Rabbit

Isotype:

IgG

Immunogen:

Synthesized peptide derived from part region of human protein

Concentration:

1 mg/ml

Molecular weight:

Applications:

WB, ELISA

Storage:

-20°C for 1 year

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