Rabbit Polyclonal E3 ubiquitin-protein ligase MUL1 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human MUL1 aa 1 to C-terminus.
pH: 7
Preservative: 0.025% Proclin 300
Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine)
WB | ICC/IF | |
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Human | Tested | Tested |
Mouse | Predicted | Predicted |
Rat | Predicted | Predicted |
Species | Dilution info | Notes |
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Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
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Species Mouse, Rat | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat | Dilution info - | Notes - |
Select an associated product type
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 proteasomal degradation (PubMed:22410793). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (PubMed:21597459). 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 mitochondrial fragmentation, and influences mitochondrial localization (PubMed:18207745, PubMed:18213395, PubMed:19407830). Likely to promote mitochondrial 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 RIGI-dependent antiviral response (PubMed:23399697). Can mediate RIGI sumoylation and disrupt its polyubiquitination (PubMed:23399697).
C1orf166, GIDE, MAPL, MULAN, RNF218, MUL1, Mitochondrial ubiquitin ligase activator of NFKB 1, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, Growth inhibition and death E3 ligase, Mitochondrial-anchored protein ligase, Protein Hades, Putative NF-kappa-B-activating protein 266, RING finger protein 218, RING-type E3 ubiquitin transferase NFKB 1
Rabbit Polyclonal E3 ubiquitin-protein ligase MUL1 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human MUL1 aa 1 to C-terminus.
pH: 7
Preservative: 0.025% Proclin 300
Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine)
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E3 ubiquitin-protein ligase MUL1 also known as MULAN or MAPL is an important enzyme in cellular processes. It possesses a mass of approximately 45 kDa and functions as an E3 ligase which facilitates the transfer of ubiquitin to specific substrate proteins. This tagging mechanism plays a critical role in directing proteins for degradation through the proteasome pathway. MUL1 is expressed in various tissues including the heart brain and skeletal muscle highlighting its broad biological relevance. As a mitochondrial membrane protein MUL1 helps maintain mitochondrial integrity by targeting specific proteins for ubiquitination.
MUL1 regulates numerous cellular processes such as apoptosis mitophagy and the mitochondrial dynamics by modulating the stability of target proteins. MUL1 operates independently and does not require a specific E2 enzyme for its function. Additionally it participates in cellular homeostasis by mediating the degradation of proteins that impact mitochondrial fusion and fission events. Since MUL1 forms part of the regulatory mechanisms governing cellular adaptation and survival its levels and activity are finely controlled within the cell.
MUL1 is actively involved in the mitophagy and DNA damage response pathways. Its role in the mitophagy pathway links MUL1 to PINK1 and PARKIN proteins that are critical for the removal of damaged mitochondria. In the context of the DNA damage response MUL1 functions to reprogram metabolic pathways yielding protection against cellular stress. This activity associates it with proteins like p53 a well-known tumor suppressor anchoring its presence in mechanisms of cellular defense.
MUL1 presents potential connections to neurodegenerative diseases and cancer. In Parkinson's disease dysfunction in MUL1 activity can disrupt mitochondrial quality control especially when interacting with PINK1 and PARKIN aggravating neuronal damage. Moreover alterations in MUL1 expression can influence cancer progression by impacting the p53 pathway therefore affecting cell cycle and apoptosis regulation. These associations reveal the importance of MUL1's activity for cellular health and its potential as a therapeutic target for disease intervention.
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Confocal immunofluorescent analysis of methanol-fixed A431 cells labeling E3 ubiquitin-protein ligase MUL1 with ab155511 at 1/500 dilution (Green). Alpha-tubulin filaments are labeled red.
10% SDS PAGE
All lanes: Western blot - Anti-E3 ubiquitin-protein ligase MUL1 antibody (ab155511) at 1/2000 dilution
All lanes: A431 whole cell lysate at 30 µg
Predicted band size: 40 kDa
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