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AB154238

Anti-MG53 antibody

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(2 Publications)

Rabbit Polyclonal MG53 antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human TRIM72 aa 50-300.

View Alternative Names

MG53, TRIM72, Tripartite motif-containing protein 72, Mitsugumin-53, Mg53

1 Images
Western blot - Anti-MG53 antibody (AB154238)
  • WB

Supplier Data

Western blot - Anti-MG53 antibody (AB154238)

Samples were separated by 12% SDS-PAGE. Corresponding RNA expression data for the same cell lines are based on Human Protein Atlas program.

All lanes:

Western blot - Anti-MG53 antibody (ab154238) at 1/1000 dilution

Lane 1:

RMS 13 whole cell extracts at 30 µg

Lane 2:

HeLa whole cell extracts at 30 µg

Secondary

All lanes:

HRP-conjugated anti-rabbit IgG antibody

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human TRIM72 aa 50-300. The exact immunogen used to generate this antibody is proprietary information.

Q6ZMU5

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/3000", "WB-species-notes": "<p></p>" }, "Mouse": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Rat": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Shipped at conditions
Blue Ice
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
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MG53 also known as TRIM72 is a protein that plays an important role in membrane repair. This protein has a molecular mass of approximately 72 kDa and is classified as a member of the tripartite motif-containing (TRIM) protein family. MG53 is expressed highly in striated muscles including the cardiac and skeletal muscles. Its mechanical action involves sensing membrane disruptions and facilitating the repair process by recruiting vesicles to the site of injury.
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.

MG53 has relevance to conditions like muscular dystrophy and cardiomyopathy. Mutations or dysregulation of MG53 can lead to inadequate membrane repair contributing to muscle weakness and cardiac dysfunction. In muscular disorders MG53 interacts with dysferlin another repair protein to support membrane stabilization and disruptions in this interaction exacerbate disease progression.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

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).
See full target information TRIM72
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nature structural & molecular biology 30:1695-1706 PubMed37770719

2023

Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.

Applications

Unspecified application

Species

Unspecified reactive species

Si Hoon Park,Juhyun Han,Byung-Cheon Jeong,Ju Han Song,Se Hwan Jang,Hyeongseop Jeong,Bong Heon Kim,Young-Gyu Ko,Zee-Yong Park,Kyung Eun Lee,Jaekyung Hyun,Hyun Kyu Song

Scientific reports 7:960 PubMed28424461

2017

A lack of coordination between sister-chromatids segregation and cytokinesis in the oocytes of B6.Y (XY) sex-reversed female mice.

Applications

Unspecified application

Species

Unspecified reactive species

Jia-Qiao Zhu,Seang Lin Tan,Teruko Taketo
View all publications
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