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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. Zusätzlich bieten wir Ihnen Dysferlin, Limb Girdle Muscular Dystrophy 2B (Autosomal Recessive) Kits (12) und und viele weitere Produktgruppen zu diesem Protein an.
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Cow (Bovine) Polyclonal DYSF Primary Antibody für 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 Pubmed References
zebrafish dysferlin expression is involved in stabilizing muscle structures and its downregulation causes muscle disorganization.
dysferlin has membrane tubulating capacity and that it shapes the T-tubule system.
These results provide one mechanism by which the C57BL/6J background intensifies dysferlinopathy, giving rise to a more severe form of muscular dystrophy in the Dysf(B6) mouse model through increased membrane leak and inflammation.
dysferlin-deficient cardiomyocytes showed slower Ca2 (zeige CA2 Antikörper)+ 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 (zeige FKTN Antikörper)(Hp/-) FCMD (zeige FKTN Antikörper) mouse model, and the (dysferlin(sjl/sjl): fukutin (zeige FKTN Antikörper)(Hp/-)) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD (zeige FKTN Antikörper)
results provide the mechanism for dysferlin-mediated repair of skeletal muscle sarcolemma and identify ASM (zeige SMPD1 Antikörper) 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.
Data suggest that dysferlin exhibits modular architecture of 4 tertiary domains: 1) C2A, readily removed as solo domain; 2) midregion C2B-C2C-Fer-DysF, excised as intact module with several dynamic folding options; 3) C-terminal four-C2 domain module; 4) calpain-2 (zeige CAPN2 Antikörper)-cleaved mini-dysferlinC72, particularly resistant to proteolysis. Missense variant L344P in muscular dystrophy patient largely escapes proteasomal surveillance.
Human deltoid muscle biopsies of 5 Chilean dysferlinopathy patients exhibited the presence of muscular connexins (Cx40.1, Cx43 (zeige GJA1 Antikörper) and Cx45 (zeige GJC1 Antikörper)).
This review suggested that the functions of dysferlin in vesicle trafficking and membrane remodeling in skeletal muscle.
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 (zeige NAPA Antikörper) 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.
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 (zeige SMPD1 Antikörper) translocation, membrane raft clustering and NADPH oxidase (zeige NOX1 Antikörper) 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