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TRIM72 Antibody (C-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession Q6ZMU5
Clone Names 100408357
Peptide ID 100408357
Additional Information
Gene ID 493829
Other Names Tripartite motif-containing protein 72, Mitsugumin-53, Mg53, TRIM72 (HGNC:32671), MG53
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name TRIM72 (HGNC:32671)
Synonyms MG53
Function Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. 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. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
Cellular Location Cell membrane, sarcolemma. Cytoplasmic vesicle membrane. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
Research Areas
Citations (0)

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Background

TRIM72 is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. 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. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).

References

Park, E.Y., et al. Proteins 78(3):790-795(2010)Han, S., et al. Hum. Mol. Genet. 18(6):1171-1180(2009)Martin, J., et al. Nature 432(7020):988-994(2004)

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$ 80.00
Cat# BP11980b
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