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DES encodes a muscle-specific class III intermediate filament. Additionally we are shipping Desmin Antibodies (408) and Desmin Proteins (26) and many more products for this protein.
Showing 10 out of 65 products:
Human Desmin ELISA Kit for Sandwich ELISA - ABIN417384
Kobayashi, Olson, Sly, Swanson, Chung, Naryshkin, Narasimhan, Bhattacharyya, Mullenix, Chen: Utility of survival motor neuron ELISA for spinal muscular atrophy clinical and preclinical analyses. in PLoS ONE 2011
Show all 3 Pubmed References
Human Desmin ELISA Kit for Sandwich ELISA - ABIN1379903
Tidball: Desmin at myotendinous junctions. in Experimental cell research 1992
Desmin intermediate filaments are required for normal active force generation.
Desmin distribution during muscle maturation changes from dispersed aggregates to a perinuclear concentration to striated (show NSDHL ELISA Kits) afterwards.
Targeted sequencing revealed trigenic mutations: c.700G>A/p.E234K in DES, c.2966G>A/p.R989H in MYPN (show MYPN ELISA Kits), and c.5918G>C/p.R1973P in CACNA1C (show CACNA1C ELISA Kits) in a family of hypertrophic cardiomyopathy with early repolarization and short QT syndrome.
demonstrate that the expression of mutant desmin causes disruption of the extrasarcomeric desmin cytoskeleton and extensive mitochondrial abnormalities regarding subcellular distribution, number and shape
Mutation in the Core Structure of Desmin Intermediate Filaments Affects Myoblast Elasticity
Data show that the filament elongation of both desmin and keratin K8/K18 (show KRT18 ELISA Kits) proceeds very similar to that of vimentin (show VIM ELISA Kits).
Cdk1 (show CDK1 ELISA Kits)-induced desmin phosphorylation is required for efficient separation of desmin-IFs and generally detected in muscular mitotic cells in vivo.
Desmin, Lamin A/C, MMP9, and histone H4 were upregulated in the placental villi of women experiencing early pregnancy loss.
Increasing desmin abnormalities were correlated with diastolic dysfunction progression.
expression level of mutant versus wild-type desmin in mouse model as well as in skeletal muscle specimens derived from human R350P desminopathies; findings demonstrate missense-mutant desmin inflicts changes of the subcellular localization and turnover of desmin itself and of direct desmin-binding partners
Results propose that the mutations affect desmin structure and cause its aberrant folding and subsequent aggregation, triggering disruption of myofibrils organization.
identified disruption of the desmin system in gastrocnemius myofibers as an index of the myopathy and limitation of muscle function in patients with peripheral artery disease.
The disease-mutant desmin variants E245D and T453I exhibited increased binding affinity for nebulette (show NEBL ELISA Kits), delayed filament assembly kinetics, and caused significant weakening of networks.
desmin and alphaBeta-crystallin are localized at sarcoplasmic reticulum (SR)-mitochondria-associated membranes (MAMs), where they interact with VDAC, Mic60 - the core component of mitochondrial contact site and cristae organizing system (MICOS) complex - and ATP synthase, suggesting that these associations could be crucial in mitoprotection at different levels.
Complete lack or markedly decreased expression of mutant R349P desmin impairs the structural and functional integrity of neuromuscular endplates.
the coordinated up-regulations of desmin and alpha- actinin (show ACTN1 ELISA Kits) specifically in the early stage of diastolic heart failure mouse models indicate a novel myocardial response.
E413K mutation induces desmin network disorganization, desmin aggregate formation and alters the traction forces generation of single myoblasts.
This study identifies desmin as a new Asb2b target for proteasomal degradation in cardiomyocytes and suggests that accumulation of desmin could contribute to UPS impairment in Hypertrophic cardiomyopathy mice and patients
found that inhibition of the Rac1 pathway (a G protein signaling pathway involved in diverse cellular processes), antioxidant treatment, and stimulation of macroautophagy reduced desmin aggregation by up to 75% in this model
This demonstration of biomechanical integration by the desmin intermediate filament system suggests that it plays an active biological role in muscle in addition to its accepted structural role
Results show that expression of desmin increased during the late fattening stage of of hanwoo steers and it contributes to the muscle contractile apparatus.
This gene encodes a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.
, desmin, gene 1
, intermediate filament protein
, muscle-specific intermediate filament desmin