Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
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 (4) and and many more products for this protein.
Showing 10 out of 22 products:
Human Monoclonal MYOF Primary Antibody for IHC, ELISA - ABIN346907
Jaiswal, Marlow, Summerill, Mahjneh, Mueller, Hill, Miyake, Haase, Anderson, Richard, Kiuru-Enari, McNeil, Simon, Bashir: Patients with a non-dysferlin Miyoshi myopathy have a novel membrane repair defect. in Traffic (Copenhagen, Denmark) 2007
Show all 2 references for ABIN346907
Chicken Polyclonal MYOF Primary Antibody for WB - ABIN2782797
Patel, Harris, Geddes, Strehle, Watson, Bashir, Bushby, Driscoll, Keep: Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b. in Journal of molecular biology 2008
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.
High myoferlin expression is associated with breast cancer.
The effect of myoferlin on the expression of ZO-1 (show TJP1 Antibodies) in airway epithelial cells indicates its role in membrane fusion events that regulate cell detachment and apoptosis within the airway epithelium.
suggest a novel role of MYOF in breast tumor cell invasion and a potential reversion to an epithelial phenotype upon loss of MYOF
MYOF plays a previously unrecognized role in cancer cell invasion.
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.
solution structure of the inner DysF (show DYSF Antibodies) domain of the dysferlin (show DYSF Antibodies) paralogue myoferlin, which has a unique fold held together by stacking of arginine and tryptophans, mutations that lead to clinical disease in dysferlin (show DYSF Antibodies)
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.
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