The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use a concentration of 1 µg/ml. Predicted molecular weight: 53 kDa.Can be blocked with Human TRIM72 peptide (ab111656). Good results were obtained when blocked with 5% non-fat dry milk in 0.05% PBS-T.
Use at an assay dependent concentration.
ELISA titre using peptide based assay, 1:1562500.
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.
Belongs to the TRIM/RBCC family. Contains 1 B box-type zinc finger. Contains 1 B30.2/SPRY domain. Contains 1 RING-type zinc finger.
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.
Cell membrane > sarcolemma. Cytoplasmic vesicle membrane. Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
Ichikawa Y et al. Modulation of caveolins, integrins and plasma membrane repair proteins in anthracycline-induced heart failure in rabbits. PLoS One12:e0177660 (2017).
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