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BRAND / VENDOR: Abcam

Abcam, ab209263, Anti-E3 ubiquitin-protein ligase MUL1 antibody [EPR20241]

CATALOG NUMBER: ab209263
Regular price$0.99
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal E3 ubiquitin-protein ligase MUL1 antibody. Suitable for IP, WB and reacts with Human samples. Cited in 13 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR20241,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:IP, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
Biological function summary
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.
Pathways
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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Collaboration

Tony Tang

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