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Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. Additionally we are shipping Emerin Antibodies (131) and Emerin Kits (3) and many more products for this protein.
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bocks is a nonessential gene; complete loss of Bocks causes no overt developmental defects
Association of emerin with nuclear BAF (show BANF1 Proteins) in cells required the LEM domain (residues 1-47).
These data suggest a new role of EMD as an enhancer of autophagosome formation in the C16-ceramide autophagy pathway in colon cancer cells.
Results highlight the interactions at the nuclear envelope where mutations in the EMD and TMPO (show TMPO Proteins) gene in combination with mutations in SUN1 (show SUN1 Proteins) have an impact on several components of the network.
Emerin, a conserved LEM-domain protein, is among the few nuclear membrane proteins for which extensive basic knowledge--biochemistry, partners, functions, localizations, posttranslational regulation, roles in development and links to human disease
the nucleoplasmic domains of Samp1 and Emerin can bind directly to each other.
Findings show a novel EMD deletion causing rare clinical presentations which broaden the heterogeneous spectrum of phenotypes attributed to EMD mutations and provide new insight of genotype-phenotype correlations between EMD mutations and EDMD symptoms.
Emerin and BAF (show BANF1 Proteins) associated only in histone- and lamin-B (show LMNB1 Proteins)-containing fractions. The S173D mutation specifically and selectively reduced GFP-emerin association with BAF (show BANF1 Proteins) by 58%
Immunofluorescence assay and biochemical analysis of infected or transfected cells showed that Kaposi's sarcoma-associated herpesvirus p29 (show PRTN3 Proteins) expression resulted in delocalization and hyperphosphorylation of emerin.
Genetic testing identified the mutation in the EMD gene, confirming X-linked recessive (XR) EDMD. The patient's asymptomatic mother was confirmed as a carrier.
Data augment the number of EMD mutations by 13.8%, equating to an increase of 5.2% in the total known EMD mutations and to an increase of 6.0% in the number of different mutations.
Results suggest that emerin protein is an essential component of the cellular apparatus constraining and fine-tuning Wnt/b-catenin signaling in the heart providing tight control of cardiomyocyte numbers.
emerin functions with myosin IIB to polarize actin flow and nuclear movement in fibroblasts, suggesting a novel function for the nuclear envelope in organizing directional actin flow and cytoplasmic polarity.
Interactions between HDAC3 (show HDAC3 Proteins) and Emerin mediate the interaction of myogenic regulatory loci with the nuclear lamina.
a novel mechanism that could provide insight into the disease aetiology for the cardiac phenotype in many laminopathies, whereby lamin A/C and emerin regulate gene expression through modulation of nuclear and cytoskeletal actin polymerization
report significant perturbations in the expression and activation of p38/Mapk14 (show MAPK14 Proteins) in emerin-null myogenic progenitors, showing that perturbed expression of Wnt (show WNT2 Proteins), IGF-1 (show IGF1 Proteins), TGF-beta (show TGFB1 Proteins), and Notch (show NOTCH1 Proteins) signaling components disrupts normal downstream myogenic signaling
emerin facilitates repressive chromatin formation at the nuclear periphery by increasing the catalytic activity of HDAC (show HDAC3 Proteins)
Perturbation to or total loss of the emerin-beta-catenin (show CTNNB1 Proteins) complex compromises both intercalated disc function and beta-catenin (show CTNNB1 Proteins) signalling in cardiomyocytes.
These findings suggest roles for emerin as a downstream effector and signal integrator for tyrosine kinase (show TYRO3 Proteins) signaling pathway(s) at the nuclear envelope.
emerin and lamin A/C are bound to actin at the late stages of myotube differentiation
the lamin a (show LMNA Proteins)-emerin complex might have a role in muscular dystrophy and cardiomyopathy
Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene.
emerin (Emery-Dreifuss muscular dystrophy)
, LEM domain containing 5