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Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. Zusätzlich bieten wir Ihnen Emerin Proteine (5) und Emerin Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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Hamster Polyclonal Emerin Primary Antibody für 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 für 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 für 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
Epstein-Barr virus early lytic protein BFRF1 alters emerin distribution and post-translational modifications.
results indicate that emerin negatively regulates Notch (zeige NOTCH1 Antikörper) signaling by promoting the retention of the NICD (zeige NOTCH1 Antikörper) at the nuclear membrane
It has been concluded that the LEM domain, responsible for binding to the chromatin protein BAF (zeige BANF1 Antikörper), undergoes a conformational change during self-assembly of emerin N-terminal region.
Association of emerin with nuclear BAF (zeige BANF1 Antikörper) 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 (zeige TMPO Antikörper) gene in combination with mutations in SUN1 (zeige SUN1 Antikörper) 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 (zeige BANF1 Antikörper) associated only in histone- and lamin-B (zeige LMNB1 Antikörper)-containing fractions. The S173D mutation specifically and selectively reduced GFP-emerin association with BAF (zeige BANF1 Antikörper) by 58%
Emerin-null progenitors were delayed in their cell cycle exit, had decreased myosin heavy chain (MyHC (zeige MYH13 Antikörper)) expression and formed fewer myotubes. Emerin binds to and activates histone deacetylase 3 (HDAC3 (zeige HDAC3 Antikörper)).
changes in nuclear size and shape, which are mediated by nuclear envelope structural proteins lamin A/C (zeige LMNA Antikörper) 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 (zeige HDAC3 Antikörper) 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 (zeige MAPK14 Antikörper) in emerin-null myogenic progenitors, showing that perturbed expression of Wnt (zeige WNT2 Antikörper), IGF-1 (zeige IGF1 Antikörper), TGF-beta (zeige TGFB1 Antikörper), and Notch (zeige NOTCH1 Antikörper) signaling components disrupts normal downstream myogenic signaling
emerin facilitates repressive chromatin formation at the nuclear periphery by increasing the catalytic activity of HDAC (zeige HDAC3 Antikörper)
Perturbation to or total loss of the emerin-beta-catenin (zeige CTNNB1 Antikörper) complex compromises both intercalated disc function and beta-catenin (zeige CTNNB1 Antikörper) signalling in cardiomyocytes.
These findings suggest roles for emerin as a downstream effector and signal integrator for tyrosine kinase (zeige TYRO3 Antikörper) signaling pathway(s) at the nuclear envelope.
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