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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 Kits (6) and Emerin Proteins (5) and many more products for this protein.
Showing 10 out of 106 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
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Human Polyclonal Emerin Primary Antibody for IHC, ELISA - ABIN1002239
Cai, Huang, Ghirlando, Wilson, Craigie, Clore: Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. in The EMBO journal 2001
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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
bocks is a nonessential gene; complete loss of Bocks causes no overt developmental defects
the mobility of YFP-Emerin was higher in Samp1 knock out cells and lower in cells overexpressing Samp1, suggesting that Samp1 significantly attenuates the mobility of Emerin in the nuclear envelope. The mobility of Emerin depends on RanGTP. The affinity between Samp1 and Emerin is decreased in the presence of Ran, suggesting that Ran attenuates the interaction between Samp1 and Emerin.
Epstein-Barr virus early lytic protein BFRF1 alters emerin distribution and post-translational modifications.
results indicate that emerin negatively regulates Notch (show NOTCH1 Antibodies) signaling by promoting the retention of the NICD (show NOTCH1 Antibodies) at the nuclear membrane
It has been concluded that the LEM domain, responsible for binding to the chromatin protein BAF (show BANF1 Antibodies), undergoes a conformational change during self-assembly of emerin N-terminal region.
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.
these data indicate that Emerin, a conserved nuclear lamina protein, couples extracellular matrix mechanics and SRF-Mkl1 (show MKL1 Antibodies)-dependent transcription.
Emerin-null progenitors were delayed in their cell cycle exit, had decreased myosin heavy chain (MyHC (show MYH13 Antibodies)) expression and formed fewer myotubes. Emerin binds to and activates histone deacetylase 3 (HDAC3 (show HDAC3 Antibodies)).
changes in nuclear size and shape, which are mediated by nuclear envelope structural proteins lamin A/C (show LMNA Antibodies) and/or emerin, also impact gene regulation and lineage differentiation in early embryos.
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.
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