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MUL1 (F1P7T) Rabbit Monoclonal Antibody #63208

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  • WB

    Product Specifications

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 35
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    MUL1 (F1P7T) Rabbit Monoclonal Antibody recognizes endogenous levels of total MUL1 protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a recombinant protein specific to human MUL1 protein. This antibody recognizes residues surrounding Pro161 of human MUL1 protein.

    Background

    Mitochondrial E3 Ubiquitin Ligase 1 (MUL1), also known as MULAN, MAPL, GIDE, and HADES, is a RING finger-type E3 ligase anchored to the outer mitochondrial membrane with its catalytic domain facing the cytosol (1). Its localization facilitates the modification of various cytoplasmic and mitochondrial proteins by multiple post-translational modification activities. MUL1 can function as a ubiquitin E3 ligase, targeting substrates, including mitochondrial fusion protein Mitofusin-2 and the autophagy protein ULK1 (2). Additionally, MUL1 can act as a small ubiquitin-like modifier (SUMO) E3 ligase to SUMOylate proteins, such as the mitochondrial fission protein DRP1, leading to enhanced protein stabilization (3). Through these dual functions, MUL1 is involved in the regulation of many cellular processes, such as mitochondrial dynamics (3,4), mitophagy (5), autophagy (2), cell survival (1,3), and metabolism (6).

    Due to its central role in mitochondrial quality control, dynamics, and survival pathways, dysregulation of MUL1 has been implicated in a variety of human diseases. For example, in some cancers, such as clear cell renal cell carcinoma and bladder cancer, MUL1 can act as a tumor suppressor by promoting autophagy and inhibiting metastasis (7,8). Conversely, studies have shown that MUL1 may play an oncogenic role in breast or lung carcinoma by ubiquitinating and negatively regulating the tumor suppressors p53 and p73 (9). Polymorphisms in the MUL1 gene have been associated with Parkinson's disease (PD) risk, possibly due to its shared mitophagy target Mitofusin-2 in a pathway parallel to the PD-associated proteins PINK1 and Parkin (10). Inactivation of MUL1 in mouse models prevents diet-induced obesity and metabolic syndrome, suggesting it as a potential therapeutic target for conditions like non-alcoholic fatty liver disease (NAFLD) and insulin resistance (11).

    Alternate Names

    C1orf166; E3 SUMO-protein ligase MUL1; E3 ubiquitin ligase; E3 ubiquitin-protein ligase MUL1; FLJ12875; GIDE; Growth inhibition and death E3 ligase; MAPL; mitochondria-anchored protein ligase; mitochondrial E3 ubiquitin ligase 1; mitochondrial E3 ubiquitin protein ligase 1; mitochondrial ubiquitin ligase activator of NF-kB; Mitochondrial ubiquitin ligase activator of NFKB 1; Mitochondrial-anchored protein ligase; MUL1; MULAN; Putative NF-kappa-B-activating protein 266; RING finger protein 218; RING-type E3 ubiquitin transferase NFKB 1; RNF218; RP11-401M16.2

    For Research Use Only. Not for Use in Diagnostic Procedures.
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