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Mutations in dysferlin, a protein associated with the plasma membrane, can cause muscle weakness that affects both proximal and distal muscles. Additionally we are shipping Myoferlin Kits (7) and and many more products for this protein.
Showing 10 out of 21 products:
Human Polyclonal MYOF Primary Antibody for ICC, IF - ABIN4337241
Volakis, Li, Ackerman, Mihai, Bechel, Summerfield, Ahn, Powell, Zielinski, Rosol, Ghadiali, Kniss: Loss of myoferlin redirects breast cancer cell motility towards collective migration. in PLoS ONE 2014
Show all 2 Pubmed References
Myoferlin is a general component of cancer cell derived exosomes from different breast and pancreatic cancer cell lines.
the cleavage of myoferlin, yielding a membrane-associated dual C2 domain 'mini-myoferlin', is reported.
A novel regulator, myoferlin, of ADAM12 (show ADAM12 Antibodies) is discovered in HeLa cells and this protein increases ADAM12 (show ADAM12 Antibodies) expression level, stability, and its enzymatic activity, leading to the reduction of its substrate, E-cadherin (show CDH1 Antibodies), which plays important roles in the regulation of cell adhesion and tumor metastasis.
Data show myoferlin depletion did not affect STAT3 (show STAT3 Antibodies) transcription factor (STAT3 (show STAT3 Antibodies)) phosphorylation, but completely blocked STAT3 (show STAT3 Antibodies) translocation to nucleus.
This study is the first to report robust age associations for DNA methylation (show HELLS Antibodies) in MYOF and DDO (show DDO Antibodies), both of which have plausible functional roles in aging
Results demonstrate for the first time that nuclear myoferlin expression independently predicts poor clinical outcome in OPSCC patients.
Myoferlin plays a key role in VEGFA (show VEGFA Antibodies) secretion and impacts tumor-associated angiogenesis in human pancreas cancer.
MYOF regulates cell adhesions and cell-substrate adhesion strength and may account for the high degree of motility in invasive breast cancer cells.
These data provide the first evidence of myoferlin expression in solid human and mouse tumors.
Data indicate that dysferlin (show DYSF Antibodies), otoferlin (show OTOF Antibodies), and myoferlin do not merely passively adsorb to membranes but actively sculpt lipid bilayers.
these findings demonstrate the importance of dysferlin (show DYSF Antibodies) and myoferlin for transverse tubule function and in the genesis of muscular dystrophy.
Myoferlin gene knockdown not only decreases lipid vesicle fusion in EC but also attenuates Vascular Endothelial Growth Factor (VEGF) Receptor-2 (VEGFR-2) expression.
IGF1 (show IGF1 Antibodies) receptor recycling is required for normal myogenesis and myoferlin is a critical mediator of postnatal muscle growth mediated by IGF1 (show IGF1 Antibodies)
Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. (myoferlin)
myoferlin plays role in the maturation of myotubes and the formation of large myotubes that arise from the fusion of myoblasts to multinucleate myotubes.
myoferlin forms a complex with dynamin-2 (show DNM2 Antibodies) and VEGFR-2 (show KDR Antibodies), which prevents CBL (show CBL Antibodies)-dependent VEGFR-2 (show KDR Antibodies) polyubiquitination and proteasomal degradation.
interaction of myoferlin with EHD2 (show EHD3 Antibodies) identifies molecular overlap between the endocytic recycling pathway and the machinery that regulates myoblast membrane fusion
Mutations in dysferlin, a protein associated with the plasma membrane, can cause muscle weakness that affects both proximal and distal muscles. The protein encoded by this gene is a type II membrane protein that is structurally similar to dysferlin. It is a member of the ferlin family and associates with both plasma and nuclear membranes. The protein contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. Two transcript variants encoding different isoforms have been found for this gene. Other possible variants have been detected, but their full-length nature has not been determined.
fer-1-like 3, myoferlin
, Fer-1-like protein 3
, fer-1-like protein 3