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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 Proteins (9) and Tripartite Motif Containing 72 Kits (8) and many more products for this protein.
Showing 10 out of 56 products:
Human Polyclonal TRIM72 Primary Antibody for IP, WB - ABIN4890482
Cheng, Zhang, Gao, Ali Samie, Azar, Tsang, Dong, Sahoo, Li, Zhuo, Garrity, Wang, Ferrer, Dowling, Xu, Han, Xu: The intracellular Ca²⁺ channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy. in Nature medicine 2014
Show all 2 references for ABIN4890482
Cow (Bovine) Polyclonal TRIM72 Primary Antibody for WB - ABIN2775659
Martin, Han, Gordon, Terry, Prabhakar, She, Xie, Hellsten, Chan, Altherr, Couronne, Aerts, Bajorek, Black, Blumer, Branscomb, Brown, Bruno, Buckingham, Callen, Campbell, Campbell, Campbell, Caoile et al.: The sequence and analysis of duplication-rich human chromosome 16. ... in Nature 2004
Dog (Canine) Polyclonal TRIM72 Primary Antibody for EIA, IHC (p) - ABIN569633
Park, Kwon, Jeong, Yi, Lee, Ko, Song: Crystal structure of PRY-SPRY domain of human TRIM72. in Proteins 2010
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 Antibodies) ubiquitination with the aid of UBE2H (show UBE2H Antibodies) 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 Antibodies) contributes to initiation of cell membrane repair
MG53, annexin A1 (show ANXA1 Antibodies), and dysferlin (show DYSF Antibodies) 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.
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 Antibodies) 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 Antibodies) target genes. MG53 plays a novel role in transcriptional upregulation of PPARalpha (show PPARA Antibodies) and its target genes, resulting in lipid accumulation and lipid toxicity, thereby contributing to diabetic cardiomyopathy.
These data suggest an essential role for TRIM72 in repair of alveolar epithelial cells under plasma membrane stress failure.
MG53 is an ubiquitin E3 ligase that induces IRS-1 (show IRS1 Antibodies) ubiquitination with the help of an E2-conjugating enzyme, UBE2H (show UBE2H Antibodies).
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