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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 Proteins (5) and Emerin Kits (3) and many more products for this protein.
Showing 10 out of 132 products:
Hamster Polyclonal Emerin Primary Antibody for ICC, IF - ABIN4307811
Collard, Herledan, Pincini, Guerci, Randrianarison-Huetz, Sotiropoulos: Nuclear actin and myocardin-related transcription factors control disuse muscle atrophy through regulation of Srf activity. in Journal of cell science 2014
Show all 4 references for ABIN4307811
Human Polyclonal Emerin Primary Antibody for EIA, WB - ABIN452956
Asioli, Bussolati: Emerin immunohistochemistry reveals diagnostic features of nuclear membrane arrangement in thyroid lesions. in Histopathology 2009
Show all 2 references for ABIN452956
Human Monoclonal Emerin Primary Antibody for IHC (fro), IHC (p) - ABIN180665
Nagano, Koga, Ogawa, Kurano, Kawada, Okada, Hayashi, Tsukahara, Arahata: Emerin deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy. in Nature genetics 1996
Show all 2 references for ABIN180665
Rabbit Monoclonal Emerin Primary Antibody for ICC, IF - ABIN1042591
Manilal, Nguyen, Sewry, Morris: The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. in Human molecular genetics 1996
Human Polyclonal Emerin Primary Antibody for EIA, IHC (p) - ABIN499790
Schirmer, Florens, Guan, Yates, Gerace: Nuclear membrane proteins with potential disease links found by subtractive proteomics. in Science (New York, N.Y.) 2003
bocks is a nonessential gene; complete loss of Bocks causes no overt developmental defects
Association of emerin with nuclear BAF (show BANF1 Antibodies) 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 Antibodies) gene in combination with mutations in SUN1 (show SUN1 Antibodies) 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 Antibodies) associated only in histone- and lamin-B (show LMNB1 Antibodies)-containing fractions. The S173D mutation specifically and selectively reduced GFP-emerin association with BAF (show BANF1 Antibodies) by 58%
Immunofluorescence assay and biochemical analysis of infected or transfected cells showed that Kaposi's sarcoma-associated herpesvirus p29 (show PRTN3 Antibodies) 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 Antibodies) 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 Antibodies) in emerin-null myogenic progenitors, showing that perturbed expression of Wnt (show WNT2 Antibodies), IGF-1 (show IGF1 Antibodies), TGF-beta (show TGFB1 Antibodies), and Notch (show NOTCH1 Antibodies) 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 Antibodies)
Perturbation to or total loss of the emerin-beta-catenin (show CTNNB1 Antibodies) complex compromises both intercalated disc function and beta-catenin (show CTNNB1 Antibodies) signalling in cardiomyocytes.
These findings suggest roles for emerin as a downstream effector and signal integrator for tyrosine kinase (show TYRO3 Antibodies) 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 Antibodies)-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