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Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Additionally we are shipping Tripartite Motif Containing 72 Antibodies (64) and Tripartite Motif Containing 72 Kits (14) and many more products for this protein.
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serum TRIM72 may be a potential biomarker for the diagnosis and the prognosis of colon cancer.
MG53 is an effective biomarker of myocardial injury and dysfunction in murine hearts. However, MG53 is not expressed in human heart and therefore does not hold utility as a clinical biomarker of myocardial injury
MG53 is a facilitator of rapid injury repair, a mediator of cell migration, and a modulator of myofibroblast differentiation during wound healing
Zn(2+) interacts with MG53 in protection against injury to the cell membrane
MG53 induces FAK (show PTK2 Proteins) ubiquitination with the aid of UBE2H (show UBE2H Proteins) during skeletal myogenesis.
MG53/TRIM72 protein can be directly applied as a therapeutic agent to increase membrane repair capacity of many cell types.
data reveal NM-IIA as a key cytoskeleton motor protein that facilitates vesicle trafficking during MG53-mediated cell membrane repair
membrane-delimited interaction between MG53 and PTRF (show PTRF Proteins) contributes to initiation of cell membrane repair
MG53, annexin A1, and dysferlin localize to the t-tubule network and show enriched labeling at longitudinal tubules of the t-system in overstretch
Crystal structure of PRY-SPRY domain of human TRIM72.
Results show that MG53 binds to Orai1 (show TMEM132A Proteins) via its PRY-SPRY region and co-localizes with Orai1 (show TMEM132A Proteins) in the plasma membrane in skeletal muscle which enhances extracellular Ca2 (show CA2 Proteins)+ entry via Orai1 (show TMEM132A Proteins) by store-operated Ca(2 (show CA2 Proteins)+) entry mechanism.
MG53 is essential to preserve T-tubule integrity and thereby Ca(2 (show CA2 Proteins)+) handling properties and cardiac function under pathological cardiac stress.
TRIM72 directly and indirectly modulates caveolar endocytosis
MG53 protein is expressed in lung tissue.
Findings indicate that the manifestation of metabolic syndrome alters MG53 activity by reducing its extracellular expression in the serum and causing it to aggregate around mitochondria within striated (show NSDHL Proteins) muscle cells.
MG53 is a vital component of reno-protection, and targeting MG53-mediated repair of renal proximal tubular epithelium cells represents a potential approach to prevention and treatment of acute kidney injury
MG53-deficient hearts downregulated PPARalpha (show PPARA Proteins) target genes. MG53 plays a novel role in transcriptional upregulation of PPARalpha (show PPARA Proteins) and its target genes, resulting in lipid accumulation and lipid toxicity, thereby contributing to diabetic cardiomyopathy.
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. 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).
tripartite motif-containing 72
, tripartite motif-containing protein 72
, mitsugumin 53