Recombinant Human MG53 protein (GST tag N-Terminus)
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Recombinant Human MG53 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 268 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
MG53, TRIM72, Tripartite motif-containing protein 72, Mitsugumin-53, Mg53
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human MG53 protein (GST tag N-Terminus) (AB132761)
ab132761 on 12.5% SDS-PAGE stained with Coomassie blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MG53 acts as a critical factor in maintaining cellular membrane integrity. It forms part of a complex network where it interacts with other proteins to orchestrate the membrane repair process. MG53 functions as a scaffold bringing together various repair components and coordinating their activity to mend damaged membranes. This repair process is essential for muscle cells which frequently experience mechanical stress.
Pathways
MG53 integrates into cellular repair pathways and is pivotal in the response to membrane damage. It interacts with important pathways like the IRS1/PI3K/AKT signaling pathway where it modulates cellular responses to stress and injury. MG53 also associates with other proteins such as caveolin-3 assisting in stabilizing the membrane during injury response.
Specifications
Form
Liquid
General info
Function
Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites (PubMed : 36944613). Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (By similarity). Acts as a sensor of oxidation : upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site (By similarity). This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation (By similarity). Probably acts upstream of the Ca(2+)-dependent membrane resealing process (By similarity). Required for transport of DYSF to sites of cell injury during repair patch formation (By similarity). Regulates membrane budding and exocytosis (By similarity). May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
Sequence similarities
Belongs to the TRIM/RBCC family.
Post-translational modifications
Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.. S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.
Target data
Product promise
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