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anti-Human MUL1 Antibodies:
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Human Polyclonal MUL1 Primary Antibody for WB - ABIN4892072
Cilenti, Ambivero, Ward, Alnemri, Germain, Zervos: Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy. in Biochimica et biophysica acta 2014
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Cow (Bovine) Polyclonal MUL1 Primary Antibody for WB - ABIN2774782
Zhang, Denhard, Zhou, Liu, Lan: 0610009K11Rik, a testis-specific and germ cell nuclear receptor-interacting protein. in Biochemical and biophysical research communications 2008
Show all 2 Pubmed References
HSPA5 negatively regulates lysosomal activity through ubiquitination of MUL1 in head and neck cancer
Data demonstrate a clear role for MAPL and mitochondrial SUMOylation in the activation of RIG-I, a modification essential for the mitochondrial antiviral signaling response.
MULAN regulates NF-kappaappaB activation to protect cells from endoplasmic reticulum stress-induced apoptosis.
MUL1 ubiquitinates ULK1 and regulates selenite-induced mitophagy
Cigarette smoke-induced MUL1 elevation mediates Akt ubiquitination/degradation, potentially leading to pulmonary endothelial cell death and functional impairment.
Hades (MUL1)-mediated p73 ubiquitination is a novel regulatory mechanism for the exonuclear function of p73.
Activation of apoptosis triggers MAPL/MUL1-dependent SUMOylation of the fission GTPase Drp1, a process requisite for cytochrome c release.
The interaction of GABARAP with Mulan-Ube2E3 supports the role of Mulan as an important regulator of mitophagy.
MethyLight data demonstrated that C13orf18 and C1orf166 could not be considered as specific, sensitive and suitable prognostic biomarkers in cervical dysplasia related Papillomavirus Infections.
During stress-induced mitochondrial hyperfusion, MULAN forms a complex with TRAF2 and modulates its ubiquitylation, signifying that TRAF2 may serve as an ubiquitylated transmitter of NF-kappaB signaling in this pathway
MUL1 is a novel regulator of the RIG-I-like receptor-dependent antiviral response, that otherwise functions to limit inflammation.
MULAN negatively regulates Akt signaling, facilitating the control of multiple cellular processes.
These findings show that Hades (MUL1)-mediated p53 ubiquitination is a novel mechanism for negatively regulating the exonuclear function of p53
CARP and its regulator calpain 3 appear to occupy a central position in the important cell fate-governing NF-kappaB pathway in skeletal muscle
Confocal- and electron-microscopy studies of MAPL-YFP led to the observation that mitochondria-anchored protein ligase (MAPL) is incorporated within unique, DRP1-independent, 70-100 nm diameter mitochondria-derived vesicles (MDVs).
MULAN (Mitochondrial Ubiquitin Ligase Activator of NF-kB; aka FLJ12875, C1orf166) is a RING finger-type E3 ubiquitin ligase anchored to mitochondria that has been implicated in the regulation of mitochondrial dynamics and in the activation of NF-kB.
The identification of GIDE, a mitochondrially located E3 ubiquitin ligase, is reported.
The mitochondrial-anchored protein ligase (MAPL) is characterized as the first mitochondrial-anchored SUMO E3 ligase.
Melatonin, added together with MPTP or added once MPTP was removed, prevented and recovered, respectively, the parkinsonian phenotype once it was established, restoring gene expression and normal function of the parkin/PINK1/DJ-1/MUL1 loop and also the normal motor activity of the embryos.
Our results indicate that strict maternal transmission of mitochondria relies on mitophagy and uncover a collaboration between MUL1 and PARKIN in this process.
Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy.
These results suggest that Tnrip-1 is a testis-specific and GCNF-interacting protein which may be involved in the modulation of GCNF-mediated gene transcription in spermatogenic cells within the testis.
E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. 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 (By similarity).
E3 SUMO-protein ligase MUL1
, E3 ubiquitin ligase
, E3 ubiquitin-protein ligase MUL1
, growth inhibition and death E3 ligase
, mitochondria-anchored protein ligase
, mitochondrial E3 ubiquitin ligase 1
, mitochondrial ubiquitin ligase activator of NF-kB
, mitochondrial ubiquitin ligase activator of NFKB 1
, mitochondrial-anchored protein ligase
, putative NF-kappa-B-activating protein 266
, ring finger protein 218
, mitochondrial ubiquitin ligase activator of nfkb 1
, E3 ubiquitin-protein ligase mul1
, mitochondrial ubiquitin ligase activator of NFKB 1-like
, E3 ubiquitin-protein ligase mul1-A
, mitochondrial ubiquitin ligase activator of nfkb 1-A