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The protein encoded by DYSF belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. Additionally we are shipping Dysferlin, Limb Girdle Muscular Dystrophy 2B (Autosomal Recessive) Kits (11) and and many more products for this protein.
Showing 10 out of 64 products:
Cow (Bovine) Polyclonal DYSF Primary Antibody for WB - ABIN2782235
Leshinsky-Silver, Argov, Rozenboim, Cohen, Tzofi, Cohen, Wirguin, Dabby, Lev, Sadeh: Dysferlinopathy in the Jews of the Caucasus: a frequent mutation in the dysferlin gene. in Neuromuscular disorders : NMD 2007
Show all 2 references for ABIN2782235
Chicken Polyclonal DYSF Primary Antibody for WB - ABIN2782236
Dubowitz: Commentary from the editor. in Neuromuscular disorders : NMD 2007
zebrafish dysferlin expression is involved in stabilizing muscle structures and its downregulation causes muscle disorganization.
dysferlin-deficient cardiomyocytes showed slower Ca2 (show CA2 Antibodies)+ re-sequestration. Dysferlin deficiency blunted the beta-adrenergic effect on relaxation and pumping function of ex vivo working hearts.
Using both naturally occurring and genetically engineered dysferlin-deficient mice, the authors demonstrated that loss of dysferlin confers increased susceptibility to coxsackievirus infection and myocardial damage.
By targeting DYSF premRNA introns harbouring differentially defined 3' splice sites (3' SS), we found that target introns encoding weakly defined 3' SSs were trans-spliced successfully in vitro in human myoblasts also in vivo in skeletal muscle of mice.
Dysferlin does not regulate cardiac voltage-dependent ion channels in cardiomyocytes.
results show that dysferlin exerts protective effects on the fukutin (show FKTN Antibodies)(Hp/-) FCMD (show FKTN Antibodies) mouse model, and the (dysferlin(sjl/sjl): fukutin (show FKTN Antibodies)(Hp/-)) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD (show FKTN Antibodies)
results provide the mechanism for dysferlin-mediated repair of skeletal muscle sarcolemma and identify ASM (show SMPD1 Antibodies) as a potential therapy for dysferlinopathy
These novel observations of conspicuous intermyofibrillar lipid and progressive adipocyte replacement in dysferlin-deficient muscles.
Laser-wounding induced rapid recruitment of local dysferlin-containing sarcolemma, formation of stable dysferlin accumulations surrounding lesions, endocytosis of dysferlin, and formation of large cytoplasmic vesicles from distal regions of the fiber.
Dysferlin, a calcium-triggered exocytotic membrane repair protein, is required for the cytoprotective effects of TRAF2 (show TRAF2 Antibodies)-mediated signaling after myocardial ischemia reperfusion injury.
Alternate splicing of the dysferlin C2A domain confers Ca(2 (show CA2 Antibodies)+)-dependent and Ca(2 (show CA2 Antibodies)+)-independent binding for membrane repair.
DYSF expression is significantly upregulated in human masticatory mucosa during wound healing
DYSF mutations in Chinese patients clustered in the N-terminal region of the gene. Exonic rearrangements were found in 23% of patients with only one pathogenic mutation identified by Sanger sequencing or NGS. The novel mutations found in this study greatly expanded the mutational spectrum of dysferlinopathy.
This study showed that 4 patients with Inflammatory Myopathy associated with DYSF mutation.
results support a function for dysferlin as a calcium-sensing SNARE (show NAPA Antibodies) effector for membrane fusion events
These differences in the structural dynamics of the predicted binding site suggest that mutation R959W alters recognition dynamics of the inner DysF domain.
This study demonstrated that novel mutation of DYSF in patient with Dysferlinopathy in Iran.
We conclude that two independent mutations in ALMS1 (show ALMS1 Antibodies) and DYSF cause CRD (show CRX Antibodies) and muscular dystrophy in the studied consanguineous Israeli Arab family.
Dysferlin carrier frequency and the number of affected individuals at risk for dysferlinopathy could be higher than previously estimated.
Our study underlines clinical heterogeneity and a high proportion of novel mutations for dysferlin in Chinese patients affected with dysferlinopathy.
C2 domains mediate high affinity self-association of dysferlin in a parallel homodimer
dysferlin mediates lysosome fusion to the plasma membrane and thereby leads to ASMase (show SMPD1 Antibodies) translocation, membrane raft clustering and NADPH oxidase (show NOX1 Antibodies) activation in coronary arterial endothelial cells, which consequently results in endothelial dysfunction
The protein encoded by this gene belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. It is involved in muscle contraction and contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. In addition, the protein encoded by this gene binds caveolin-3, a skeletal muscle membrane protein which is important in the formation of caveolae. Specific mutations in this gene have been shown to cause autosomal recessive limb girdle muscular dystrophy type 2B (LGMD2B) as well as Miyoshi myopathy. Alternative splicing results in multiple transcript variants.
dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)
, dysferlin variant a
, dystrophy-associated fer-1-like protein
, fer-1-like protein 1
, dystrophy-associated fer-1-like 1
, Dystrophy-associated fer-1-like protein
, Fer-1-like protein 1