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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. Zusätzlich bieten wir Ihnen Myoferlin Kits (7) und und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal MYOF Primary Antibody für 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 (zeige ADAM12 Antikörper) is discovered in HeLa cells and this protein increases ADAM12 (zeige ADAM12 Antikörper) expression level, stability, and its enzymatic activity, leading to the reduction of its substrate, E-cadherin (zeige CDH1 Antikörper), which plays important roles in the regulation of cell adhesion and tumor metastasis.
Data show myoferlin depletion did not affect STAT3 (zeige STAT3 Antikörper) transcription factor (STAT3 (zeige STAT3 Antikörper)) phosphorylation, but completely blocked STAT3 (zeige STAT3 Antikörper) translocation to nucleus.
This study is the first to report robust age associations for DNA methylation (zeige HELLS Antikörper) in MYOF and DDO (zeige DDO Antikörper), 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 (zeige VEGFA Antikörper) 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 (zeige DYSF Antikörper), otoferlin (zeige OTOF Antikörper), and myoferlin do not merely passively adsorb to membranes but actively sculpt lipid bilayers.
these findings demonstrate the importance of dysferlin (zeige DYSF Antikörper) 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 (zeige IGF1 Antikörper) receptor recycling is required for normal myogenesis and myoferlin is a critical mediator of postnatal muscle growth mediated by IGF1 (zeige IGF1 Antikörper)
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 (zeige DNM2 Antikörper) and VEGFR-2 (zeige KDR Antikörper), which prevents CBL (zeige CBL Antikörper)-dependent VEGFR-2 (zeige KDR Antikörper) polyubiquitination and proteasomal degradation.
interaction of myoferlin with EHD2 (zeige EHD3 Antikörper) 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