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Mouse Anti-MUL1 (AA 200-352) Recombinant Antibody (CBFYM-2824) (CBMAB-M3017-FY)

This product is mouse antibody that recognizes MUL1. The antibody CBFYM-2824 can be used for immunoassay techniques such as: WB, IHC, IHC-P.
See all MUL1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2824
Antibody Isotype
IgG1, k
Application
WB, IHC, IHC-P

Basic Information

Immunogen
Recombinant protein made to a C-terminal portion of the human MUL1 protein (between residues 200-352)
Specificity
Human
Antibody Isotype
IgG1, k
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.05% BSA
Preservative
0.05% Sodium azide
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 200-352

Target

Full Name
MITOCHONDRIAL E3 UBIQUITIN PROTEIN LIGASE 1
Introduction
MUL1 is a Protein Coding gene. Among its related pathways are Metabolism of proteins and Deubiquitination. Gene Ontology annotations related to this gene include identical protein binding and ubiquitin-protein transferase activity.
Entrez Gene ID
79594
UniProt ID
Q969V5
Alternative Names
Mitochondrial E3 Ubiquitin Protein Ligase 1; Growth Inhibition And Death E3 Ligase; Ring Finger Protein 218; Mitochondrial Ubiquitin Ligase Activator Of NFKB 1; Putative NF-Kappa-B-Activating Protein 266; RING-Type E3 Ubiquitin Transferase NFKB 1; Mitochondrial-Anchored Protein Ligase; Mitochondria-Anchored Protein Ligase; E3 Ubiquitin-Protein Ligase MUL1; E3 SUMO-Protein Ligase MUL1; C1orf166
Function
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 proteosomal 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:19407830, PubMed:18207745, PubMed:18213395).

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 DDX58-dependent antiviral response (PubMed:23399697).

Can mediate DDX58 sumoylation and disrupt its polyubiquitination (PubMed:23399697).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Apoptotic process Source: UniProtKB-KW
Cellular response to exogenous dsRNA Source: UniProtKB
Mitochondrial fission Source: UniProtKB
Mitochondrion localization Source: UniProtKB
Negative regulation of cell growth Source: UniProtKB
Negative regulation of chemokine (C-C motif) ligand 5 production Source: UniProtKB
Negative regulation of defense response to virus by host Source: UniProtKB
Negative regulation of innate immune response Source: UniProtKB
Negative regulation of mitochondrial fusion Source: UniProtKB
Negative regulation of protein kinase B signaling Source: UniProtKB
Negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
Positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization Source: Ensembl
Positive regulation of dendrite extension Source: Ensembl
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of mitochondrial fission Source: UniProtKB
Positive regulation of protein sumoylation Source: UniProtKB
Protein destabilization Source: ParkinsonsUK-UCL
Protein polyubiquitination Source: UniProtKB
Protein stabilization Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Regulation of mitochondrial membrane potential Source: Ensembl
Regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
Regulation of mitochondrion organization Source: ParkinsonsUK-UCL
Cellular Location
Mitochondrion
Mitochondrion outer membrane
Peroxisome
Note: Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome.
Topology
Cytoplasmic: 1-8
Helical: 9-29
Mitochondrial intermembrane: 30-238
Helical: 239-259
Cytoplasmic: 260-352
PTM
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.

Di Gregorio, J., Appignani, M., & Flati, V. (2023). Role of the Mitochondrial E3 Ubiquitin Ligases as Possible Therapeutic Targets in Cancer Therapy. International Journal of Molecular Sciences, 24(24), 17176.

Vásquez-Trincado, C., Navarro-Márquez, M., Morales, P. E., Westermeier, F., Chiong, M., Parra, V., ... & Lavandero, S. (2023). Myristate induces mitochondrial fragmentation and cardiomyocyte hypertrophy through mitochondrial E3 ubiquitin ligase MUL1. Frontiers in Cell and Developmental Biology, 11, 1072315.

Calle, X., Garrido‐Moreno, V., Lopez‐Gallardo, E., Norambuena‐Soto, I., Martínez, D., Peñaloza‐Otárola, A., ... & Lavandero, S. (2022). Mitochondrial E3 ubiquitin ligase 1 (MUL1) as a novel therapeutic target for diseases associated with mitochondrial dysfunction. IUBMB life, 74(9), 850-865.

Cilenti, L., Mahar, R., Di Gregorio, J., Ambivero, C. T., Merritt, M. E., & Zervos, A. S. (2022). Regulation of Metabolism by Mitochondrial MUL1 E3 Ubiquitin Ligase. Frontiers in Cell and Developmental Biology, 10, 904728.

Puri, R., Cheng, X. T., Lin, M. Y., Huang, N., & Sheng, Z. H. (2020). Defending stressed mitochondria: uncovering the role of MUL1 in suppressing neuronal mitophagy. Autophagy, 16(1), 176-178.

Cilenti, L., Di Gregorio, J., Ambivero, C. T., Andl, T., Liao, R., & Zervos, A. S. (2020). Mitochondrial MUL1 E3 ubiquitin ligase regulates Hypoxia Inducible Factor (HIF-1α) and metabolic reprogramming by modulating the UBXN7 cofactor protein. Scientific reports, 10(1), 1609.

Wang, S. J., Chen, H., Tang, L. J., Tu, H., Liu, B., Li, N. S., ... & Peng, J. (2020). Upregulation of mitochondrial E3 ubiquitin ligase 1 in rat heart contributes to ischemia/reperfusion injury. Canadian Journal of Physiology and Pharmacology, 98(5), 259-266.

Yuan, Y., Li, X., Xu, Y., Zhao, H., Su, Z., Lai, D., ... & Xu, G. (2019). Mitochondrial E3 ubiquitin ligase 1 promotes autophagy flux to suppress the development of clear cell renal cell carcinomas. Cancer science, 110(11), 3533-3542.

Ren, K. D., Liu, W. N., Tian, J., Zhang, Y. Y., Peng, J. J., Zhang, D., ... & Luo, X. J. (2019). Mitochondrial E3 ubiquitin ligase 1 promotes brain injury by disturbing mitochondrial dynamics in a rat model of ischemic stroke. European Journal of Pharmacology, 861, 172617.

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For research use only. Not intended for any clinical use.

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