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AB153508

Recombinant Human E3 ubiquitin-protein ligase MUL1 (GST tag N-Terminus)

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Recombinant Human E3 ubiquitin-protein ligase MUL1 (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 352 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

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

1 Images
SDS-PAGE - Recombinant Human E3 ubiquitin-protein ligase MUL1 (GST tag N-Terminus) (AB153508)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human E3 ubiquitin-protein ligase MUL1 (GST tag N-Terminus) (AB153508)

ab153508 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q969V5

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Complementary Products

Primary Antibodies

AB209263

Anti-E3 ubiquitin-protein ligase MUL1 antibody [EPR20241]

RabMAb|Recombinant

Immunoprecipitation - Anti-E3 ubiquitin-protein ligase MUL1 antibody [EPR20241] (AB209263)

  • 5
  • 2
Proteins & Peptides

AB269109

Recombinant Human Ubiquitin protein

SDS-PAGE - Recombinant Human Ubiquitin protein (AB269109)

  • 0
  • 0
Proteins & Peptides

AB269103

Recombinant human UBE2I / UBC9 protein (Active)

Functional Studies - Recombinant human UBE2I / UBC9 protein (Active) (AB269103)

  • 0
  • 0
Proteins & Peptides

AB198417

Recombinant human UBE3A protein (His-DDDDK tag N-Terminus)

Functional Studies - Recombinant human UBE3A protein (His-DDDDK tag N-Terminus) (AB198417)

  • 0
  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":352,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q969V5","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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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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Specifications

Form

Liquid

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General info

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 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).

Post-translational modifications

Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.

Subcellular localisation

Mitochondrion outer membrane

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Target data

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).
See full target information MUL1
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